nach oben

Erschienen in:

2017 | OriginalPaper | Buchkapitel

2. Blood Coagulation

verfasst von : Antonio Fasano, Adélia Sequeira

Erschienen in: Hemomath

Verlag: Springer International Publishing

Einloggen

Aktivieren Sie unsere intelligente Suche, um passende Fachinhalte oder Patente zu finden.

search-config

KI-gestützte Suche

Aus

Abstract

This chapter is devoted to the description and modeling of the process of blood coagulation which is crucial for life and is the result of an intricate sequence of chemical reactions, involving an active role of platelets and of a surprisingly large number of blood born massive molecules performing a sequence of operations aimed at the formation of the clot and at its subsequent dissolution. Due to such a complexity there is an enormous variety of conditions leading to insufficient or excessive coagulation. We will discuss also the biological and mathematical aspects regarding these pathologies.

Sie haben noch keine Lizenz? Dann Informieren Sie sich jetzt über unsere Produkte:

Springer Professional "Wirtschaft+Technik"

Online-Abonnement

Mit Springer Professional "Wirtschaft+Technik" erhalten Sie Zugriff auf:

über 102.000 Bücher
über 537 Zeitschriften

aus folgenden Fachgebieten:

Automobil + Motoren
Bauwesen + Immobilien
Business IT + Informatik
Elektrotechnik + Elektronik
Energie + Nachhaltigkeit
Finance + Banking
Management + Führung
Marketing + Vertrieb
Maschinenbau + Werkstoffe
Versicherung + Risiko

Jetzt Wissensvorsprung sichern!

Jetzt informieren

Springer Professional "Technik"

Online-Abonnement

Mit Springer Professional "Technik" erhalten Sie Zugriff auf:

über 67.000 Bücher
über 390 Zeitschriften

aus folgenden Fachgebieten:

Automobil + Motoren
Bauwesen + Immobilien
Business IT + Informatik
Elektrotechnik + Elektronik
Energie + Nachhaltigkeit
Maschinenbau + Werkstoffe

Jetzt Wissensvorsprung sichern!

Jetzt informieren

Springer Professional "Wirtschaft"

Online-Abonnement

Mit Springer Professional "Wirtschaft" erhalten Sie Zugriff auf:

über 67.000 Bücher
über 340 Zeitschriften

aus folgenden Fachgebieten:

Bauwesen + Immobilien
Business IT + Informatik
Finance + Banking
Management + Führung
Marketing + Vertrieb
Versicherung + Risiko

Jetzt Wissensvorsprung sichern!

Jetzt informieren

Vorheriges Kapitel Hemorheology and Hemodynamics

Nächstes Kapitel Blood Filtration in Kidneys

A widespread belief, still alive in the nineteenth century, was that limb swelling accompanying pregnancy was due to the accumulation of excess milk which found its way to reach the legs. The name “phlegmatia lactea” was coined for this condition by the French physician and botanist François Boissier de Sauvages de Lacroix (1706–1767) (known as Sauvage) in his Nosologia Methodica (1768). Pregnancy may increase the risk of thrombosis in various ways. The swollen uterus can compress pelvic vessels, reducing blood circulation in the legs. Hormonal changes can also produce hypercoagulability by increasing the concentration in blood of pro-coagulant factors and reducing the concentration of anticoagulant factors. A more serious condition sometimes related to pregnancy is the Antiphospholipid Antibody (or Hughes, or sticky blood) Syndrome, due to the autoimmune production of antibodies against a cell membrane substance called phospholipid, eventually producing clots.

Nevertheless, we must consider that in this context “heat” was not meant just as a physical quantity, but as a vital entity carried by blood.

Such a fibrous component was isolated much later by Marcello Malpighi (1628–1694).

Despite his fame (testified by the great success of his book Several Chirurgical Treatises—London, Flesher 1676) as member of the Company of Barber-Surgeons his social rank was inferior to the one of physicians.

Though he was one of the founders of pathology, it is reductive to call him just a pathologist, since this great man was also a biologist, the editor of the Archiv für pathologische Anatomie und Physiologie und für klinische Medizin (known as the Virchow’s journal), the founder of the Gesellschaft für Anthropologie, Ethnologie und Urgeschichte (very influential in German archaeology), and the leader of a democratic party. He wrote about many different subjects. He was such a strong opponent of Bismarck, that he was challenged by him to a duel in 1865. The legend says that, having to choose the weapons, he selected two pork sausages, one of them charged with trichinosis larvae, thus discouraging his adversary. Not everything he did was perfect: he was skeptic about Darwin’s evolution theory.

Virchow described the mechanism of thromboembolism [253], a phenomenon that was by no means clear at his time (inflammation was considered by many physicians the real cause of thrombosis: this was the subject of a famous dispute with the French pathologist Jean Cruveilhier). Curiously, he did not formulate the famous “triad”, which for some reason found a firm place in the literature much after his death (apparently not before 1950!). See the interesting review [22].

Circumcision is a very old practice, already found in ancient Egypt and that was widely adopted also in the Islamic world. Its origin in Egypt was probably as an initiation practice to religious offices. The Book of the Dead describes self-circumcision by the sun-god Ra: Blood fell from the phallas of Ra after he had finished cutting himself.

The fact that hemophilia is gender related was suggested by the American physician John Conrad Otto (1774–1844) as early as 1803.

In numbers, 1 over 10,000 men is hemophilic. The probability that a woman is hemophilic is the square of that number. Cases of hemophilic women have been reported (see e.g. [90]).

The only male child of Tsar Nicholas II (Aleksej Nikolaevič Romanov) got hemophilia through his mother Alice (third row in Fig. 2.5), who as a Tsarina took the name Aleksandra Fëdorovna Romanova. The Tsarina believed that Grigory Rasputin (a controversial character) was able to heal the tsarevich with his prayers (he actually recommended not to credit the physicians) and in this way he acquired great power at court.

A distinguished French Medicine Professor, Trousseau related a state of hypercoagulability to the presence of some malignancies. He diagnosed his fatal illness having got a thromboflebitis in his left upper arm. The presence of cancer induced thromboflebitis has become known as Trousseau Syndrome.

We will refer his contributions in the field of leukemia in the last chapter. The list of people who contributed to the early studies on platelets is actually longer (see the review paper [55]).

In this connection the name of the eminent French hematologist Georges Hayem (1841–1933) has to be remembered as one of the founders of modern hematology. He performed the first count of platelets. In 1882 he illustrated the effects of thrombocytopenia (low platelets count)

The eminent Canadian Physician William Osler (1849–1919) called them third corpuscles. The name platelets was introduced in 1910 by the American pathologist James Wright (1869–1928).

Large molecules like proteins have specific sites which are engaged in specific reactions.

The volume unit femtoliter is often used for small particles. It corresponds to 1 μm³ = 10⁻¹⁵ l.

All data concerning human blood are subjected to large variations, according to sex, body weight, and health conditions. A parameter which instead is bound to stay in a narrow range is blood pH whose value must be between 7.35 and 7.45.

Most cells interact with the environment thanks to receptors able to recognize molecules carrying signals and inducing specific stimuli (cytokines).

Gp recalls that these receptors are glycoproteins receptors denoted as GPIb (i.e. containing sugar chains).

A protein with elongated molecule (fibril) which comes in many different types and is abundant in many tissues, including blood vessels. It makes 1/4–1/3 of the protein content in the body.

Commonly known as Adrenaline, it was the first hormone to be discovered (1900) though the term hormone was introduced in 1905 by Ernest Starling (see the next chapter), after the Greek word ormè (impetus), for the hormone he discovered (secretin).

In 1998 the Nobel Prize in Medicine was awarded to R.F. Furchgott, L.J. Ignarro, and F. Murad for their work on the signalling role of NO.

For instance Thrombospondin 1, a multifunctional protein (e.g. antiangiogenic), and Nexin II, whose role will be discussed later. Platelets also release Growth Factors which help repairing the damaged tissue.

Through the same property it exerts the anti-inflammatory and analgesic action. For more information on the transformation of arachidonic acid in platelets and the possible consequences of COX deficiency see [148].

Drugs containing citrates have the effects of lowering Calcium concentration, inducing some anticoagulant effect. Therefore their use must be avoided in while assuming potent anticoagulants.

Mast Cells are another group of granulocytes, affine to basophils, which reside in connective and mucosal tissues (as different species) and may live for weeks or months. They are part of the immune system, which includes WBCs along with dendritic cells (present in blood in the immature stage and residing in various tissues: see the book [206]).

B-cells types: Plasmocytes, memory B-cells, B1- and B2-cells, marginal zone B-cells, Follicular B-cells, regulatory B-cells. The “B” comes from the name of the organ in which they mature in birds, Bursa of Fabricius, where B-cells were first discovered. It was then found that in humans B-cells mature in the Gut Associated Lymphoid Tissue (GALT), mainly located in the intestine.

T-cells types: helper, cytotoxic, memory, regulatory, natural killer (not the same as the ones already listed), mucosal associated invariant, gamma-delta.

From which the “T” derives.

Each RBC contains 270 million hemoglobin molecules.

RBCs smaller than 80 fL are typical of microcytic anemia. When their volume exceeds 100 fL we have macrocytic anemia.

AMP, ADP, ATP contain 1 (Mono-), 2 (Di-), 3 (Tri-) atoms of phosphorus and they are obtained in that sequence by addition of a P atom (a process called phosphorylation). ATP has a vital importance in cells metabolism.

This condition can be produced by arterial stenosis, possibly as a consequence of clotting itself, or because of the mechanical action of implanted devices (rigid artificial heart valves).

Platelet Factors 1–3 actually regulate interactions with the Coagulation Factors IIa (thrombin), V, X.

Prostaglandins make a large family. The first prostaglandin was isolated in seminal liquid (1935) by the Swedish physiologist Ulf von Euler (1905–1983) and believed to be produced only in the prostate gland. Actually several other tissues are able to secrete prostaglandins. See the section on anticoagulants.

Ecto-enzymes act at the exterior of cells. For more details about this enzyme see [85].

Though there is some disagreement on the exact meaning of this name, it is sometimes attributed to TF.

Serine proteases are a large class of enzymes. The list of serine proteases is impressively long. See http://biochem.wustl.edu/~protease/ser_pro_help.html.

A distinguished physiologist born in today Estonia, Schmidt had the idea that fibrin had to come from fibrinogen as the result of an enzymatic reaction, whose agent he called thrombin, which in turn had a precursor, which he called prothrombin [220, 221].

Publication was delayed because of II World War.

Fibrinogen was described as the precursor of Fibrin by R. Virchow in 1847 [252]. It has also other specific functions, illustrated in this chapter. It is also known to intervene in RBC’s aggregation (forming the so-called rouleaux), a phenomenon of great importance in blood rheology.

Found by B. Alexander in 1949 [7] and isolated a few years later [131].

Isolated in 1937 by A.J. Patek and F.H.L. Taylor [185], following the experiments made a year earlier by Patek and R.H. Stetson [184].

Stephen Christmas was the first patient diagnosed with FIX deficiency (hemophilia B) (Oxford, 1952) at the age of five. He was a patient of R. Biggs and R.G. Mcfarlane [32]. He died in 1993 by AIDS. Many of transfusion dependent patients were infected by the HIV virus before blood screening became obligatory. A case which became emblematic was the one of Ryan Wayne White, affected by hemophilia A, who became discriminated when he was diagnosed with AIDS. He died still a teenager in 1990.

Named after the patients Rufus Stuart and Audrey Prower and described in 1957 by C. Hougie ad coworkers [109].

Identified in 1953 by R.L. Rosenthal and coworkers [212].

Named after Ratnoff’s patient John Hageman (1955) [200, 201]. Oscar David Ratnoff (1916–2008) was one of the leading American scientists in hematology. See more in the section on anticoagulants.

K. Laki and L. Lorand suggested its existence in 1948 [136].

Discovered in 1960 by Walter H. Seegers.

A very important function of Protein S in the organism is to facilitate phagocytosis of apoptotic cells by macrophages. Discovered in 1979 (by E.W. Davie) in Seattle, takes its name after that city.

Denominated after the German name Koagulationvitamin. Discovered in the 1930s, a Nobel prize was attributed in 1943 to H.K.P. Dam and to E.A. Doisy for their studies on it, though its real action in the coagulation process became clear only in the 1970s.

See the section on Anticoagulants for some historical news on Warfarin.

Already in the 1950s it was known that deficiency of vWF was accompanied by a deficiency of FVIII.

The symbol X-ase is sometimes used.

It was first described in 1965 by W.E. Hathaway [101] who investigated treats of abnormal coagulation in members of Fletcher family (Kentuky), not exhibiting bleeding disorders. Prekallikrein as a precursor of kallilkrein was isolated in 1972 by K.D. Wuepper [280] who identified it with Fletcher factor one year later [279].

Kininogens are proteins which are precursors of kinins (see next footnote), such as bradikinin and kallidin, which are vasodilator. HMWK is also known as Williams Factor or Flaujeac Factor. The Flaujeac trait was described by J.M. Lacombe in 1975 [135]. The cause was soon identified with HMWK deficiency [281].

Here we refer to Plasma Kallikrein, distinct from the numerous group of Tissue Kallikreins which are enzymes performing various actions. It was named after the Greek words kalli (sweet, in this context) and krein (flesh) referring to pancreatic tissue. Plasma Kallikrein (like some of its tissue analogs) liberates kinins from the kininogens. The so-called kinin-kallikrein system has a role in regulating blood pressure, owing to its vasodilation action (see e.g. the book [69]). In 1909 J.E. Abelous and E. Bardier [1] observed that human urine injected in dogs caused a drop in blood pressure and conjectured that a substance produced in some organ and eliminated through urine had to be responsible. The (Kallikrein) substance was identified and named in 1930 [132], then extensively studied by E.K. Frey, E. Werle and others.

Also Kallikrein and FXIIa can activate plasminogen.

So-called because it is secreted by some bacteria in the streptococci family. Since it is not produced in the body it may trigger immune response and must be used with care.

Proteases are enzymes attacking proteins (proteolysis).

AT I-IV are also found in the literature, with specific targets.

Discovered in 1918 [110], though isolated in 1916 in canine liver tissue [158]. See more in the section on Anticoagulants. Heparin can be secreted by basophils.

Its deficiency leads to degradation of tissues, particularly in the lungs, causing emphysema. Smoke is believed to inactivate this serpin, thus causing additional damage to lungs.

The main function of C1-inhibitor is to contrast some of the molecules in the C1-complement group part of the so called complement system having an adjuvant role in the immune system.

PAI-2 is detectable only in pregnant women, a fact that may justify the increased risk of thrombosis during pregnancy.

Some FVIIa can reach TF in nonvascular tissues even in the absence of a lesion [289], thus making FIXa and FXa accidentally available. However, coagulation does not start because it requires for instance the intervention of platelets, which are not available out of the bloodstream.

FXa itself is an extremely mild activator of prothrombin. The rate of thrombin generation by prothrombinase is 300,000 times larger the one by FXa alone [149]. The prothrombin to thrombin transition is a quite complicated process. Details can be found in the review paper [133].

The proteins responsible for this regulatory action have a fundamental role in eventually halting the clot growth. They are inevitably produced at this initial stage too, but it is known that free FVa inhibition by APC is far less efficient than on the surface of endothelial cells. One can wonder whether, besides the clotting confining action, the simultaneous slowing down of the initial process may have a precise aim, for instance letting the platelet plug become thicker.

FVa on platelets membrane is inactivated faster than the same factor complexed with FXa (see e.g. [173, 238]). Likewise FVIIIa is partially protected when it is complexed with FIXa. For more details and for the role of Protein S is these processes see [174].

The book [154] collects and comments a number of historical papers on bleeding disorders and other blood diseases.

The Latin word for purple. Purpura denotes spots in the range 3–10 mm, smaller spots are called petechiae, and those more extended are called ecchymoses.

The Latin equivalent of the Greek derived word idiopathic is sui generis. In this context it means “of no specific origin”.

Congenital deficiency accounts for a small fraction of TTP cases and is known as Upshaw-Schülman syndrome.

In 1944 an Argentinean doctor (Alfredo Pavlosky) had the idea of mixing two blood samples from hemophilic patients and observed that the mixture had acquired the ability to clot. He concluded that there must have been different types of the illness.

More common among Ashkenazi Jews.

Mr. John Hageman died in 1968, quite unexpectedly, by pulmonary embolism following a hip fracture, a fact that was puzzling for Ratnoff himself [203]. It was conjectured that FXII may actually protect against thrombosis. Such a behavior has been explained considering that FXII is a plasminogen activator (see Sect. 2.3, ref. [94]). Correlations of FXII deficiency with miscarriage, coronary infarct, etc. have been reported, but the interpretation of such findings is not unanimous (see [236]). An interesting review paper on FXII is [48].

As we said, the kallikrein-kinin system is particularly important in the regulation of blood pressure. Therefore any dysfunction of it can cause hypertension (see [194]).

Since immobilization is a frequent cause, DVT is also called the economy class syndrome, because many cases have been reported in passengers after long flights.

As in the Paget-Schrötter disease. We also recall the tumor related Trusseau syndrome (see the historical section).

Not with fibrinolytic proteins (like tPA or urokinase), because they could fragment rather than gradually dissolve the clot. Fibrinolytic therapies are instead used to attack arterial thrombosis in the heart or the brain.

Major veins are provided with valves preventing flux inversion, thus helping circulation in the presence of reduced pressure gradients (see more on valves in Chap. 1).

Some hemophilia therapies actually bypass the intervention of FVIII and FIX. We will return to this question in Sect. 2.7.

Nevertheless, in the paper [50] experiments were performed emphasizing the importance of the Hageman Factor FXII in resting blood.

Reduced oxygen concentration is more marked in valves, since, differently from veins and other blood vessel, they do not possess their own vessels (vasa vasorum).

This paper is an extensive study on the role of TF and of thrombin in promoting angiogenesis and contains a large bibliography. Excessive TF production may be accompanied by upregulated expression of VEGF (the angiogenic factor) and downregulated expression of thrombospondin 1 (see Sect.2.3).

Clots are mostly originated in the left atrium and more precisely in an area called left atrial appendage.

For this reason patients receiving artificial mechanical heart valves are permanently treated with anticoagulants. Valves taken from pigs do not have this inconvenience, but have a limited duration ( ∼ 15 years).

It was the American chemist Linus Carl Pauling (1901–1994), Nobel laureate (1954), to describe the causes of the disease in 1949 [187]. This was an early success of molecular biology, of which Pauling was one of the founders.

Veterinarians know that some mammals, like whales and dolphins, do not even possess FXII.

For the sake of brevity we omit to list hemostatic drugs. Some of them act on platelets stimulating their adhesion (microfibrillar collagen hemostat, chitosan), some force strong vasoconstriction (anhydrous aluminum phosphate). Batroxobin (or reptilase) acts in a way similar to thrombin. It is contained in the venom of a group of Southern American vipers. Venoms of many snakes exert a strong coagulant action in various ways (including direct activation of Factor X).

The history of Aspirin is controversial. The synthesis of pure ASA (1897) has been credited to the young Bayer chemist Felix Hoffmann (impure ASA had been previously produced by the French chemist Charles Frédéric Gerhardt in 1857). Many years later Arthur Eichengrün, another German chemist employed at Bayer at the time of Aspirin discovery, claimed that Hoffmann had just followed his plans. Though recent studies have confirmed that Eichengrün’s thesis was credible, Bayer officially dismissed his claims. The analgesic and anti-inflammatory properties of the willow (latin salix) leaf have been known since antiquity. It has been documented in a Sumer tablet and in the Ebers Papyrus. Hippocrates mentioned it and its effects were well known in western and also Arab civilizations well before ASA chemical synthesis.

Farming, and especially milk production, was the backbone of Wisconsin economy (“the Dairy State”). The disease, described in 1924 by the veterinarian Frank Shofield, was brought to Link’s attention by a Wisconsin farmer in 1933.

This theory may have some ground, since Stalin was going to launch another purge and Beria would have been one of the first victims. The symptoms produced by warfarin poisoning would have been compatible with the brain hemorrhage that actually killed Stalin and with his clinical picture. Others claim that Stalin ‘s murder was ordered by Tito.

Equation (13) (as well as (14) and (15)) shows the phenomenon of dissociation of FVIIa in subunits. This factor has a very complicated structure. For an illustration see e.g. [73].

An intermediate step in prothrombin activation.

It consists in a term proportional to the product of viscosity and velocity, typical of the equation describing the flow of a Newtonian fluid through coarse porous media.

Named after the Australian mathematician Renfrey Potts [197].

See e.g. [84].

See e.g. [5, 66].

100

The case in which a finite bound is imposed to particles volume requires a different setting, with the introduction of a volume scattering term (see [70]).

101

See the experimental literature quoted therein.

102

Actually applicable to spheres, it practically coincides with (2.9).

103

From that paper it can be concluded that slip up to 20% of blood maximal velocity in the vessel is possible.

104

If Ω is a circle of radius R, then H = πR∕2.

J.E. Abelous, E. Bardier, Les substances hypotensives de l’urine humaine normale. C. R. Soc. Biol. 66, 51120 (1909)

K. Affeld, A.J. Reininger, J. Gadischke, K. Grunert, S. Schmidt, F. Thiele, Fluid mechanics of the stagnation point flow chamber and its platelet deposition. Artif. Org. 19, 597–602 (1995)CrossRef

W. Ageno, A.C. Spyropoulos, A.G.G. Turpie, Role of new anticoagulants for the prevention of venous thromboembolism after major orthopaedic surgery and in hospitalized acutely ill medical patients. Thromb. Haemost. 107, 1027–1034 (2012)CrossRef

W.C. Aird, Vascular bed-specific thrombosis. J. Thromb. Haemost. 5(Suppl. 1), 283–291 (2007)CrossRef

D.J. Aldous, Deterministic and stochastic models for coalescence (aggregation and coagulation): a review of the mean-field theory for probabilists. Bernoulli 5(1), 3–48 (1999)MATHMathSciNetCrossRef

R.A. Aldrich, A.G. Steinberg, D.C. Campbell, Pedigree demonstrating a sex-linked recessive condition characterised by draining ears, eczematoid dermatitis and bloody diarrhoea. Pediatrics 13, 133–139 (1954)

B. Alexander, A. De Vries, R. Goldstein, A factor in serum which accelerates the conversion of prothrombin to thrombin; its evolution with special reference to the influence of conditions which affect blood coagulation. Blood 4, 739–46 (1949)

M. Anand, K.R. Rajagopal, A mathematical model to describe the change in the constitutive character of blood due to platelet activation. C. R. Méc. 330(8), 557–562 (2002)MATHCrossRef

M. Anand, K. Rajagopal, K.R. Rajagopal, A model incorporating some of the mechanical and biochemical factors underlying clot formation and dissolution in flowing blood. J. Theor. Med. 5(3–4), 183–218 (2003)MATHMathSciNetCrossRef

10.

M. Anand, K. Rajagopal, K.R. Rajagopal, A model for the formation and lysis of blood clots. Pathophysiol. Haemost. Thromb. 34, 109–120 (2005)CrossRef

11.

M. Anand, K. Rajagopal, K.R. Rajagopal, A viscoelastic fluid model for describing the mechanics of a coarse ligated plasma clot. Theor. Comput. Fluid. Dyn. 20, 239–250 (2006)MATHCrossRef

12.

M. Anand, K. Rajagopal, K.R. Rajagopal, A model for the formation, growth, and lysis of clots in quiescent plasma. A comparison between the effects of antithrombin III deficiency and protein C deficiency. J. Theor. Biol. 253, 725–738 (2008)

13.

S.T. Anning, The historic aspects of venous thrombosis. Med. Hist. 1, 28–37 (1957)CrossRef

14.

F.I. Ataullakhanov, D.A. Molchanova, A.V. Pokhilko, Mathematical model of the blood coagulation system: intrinsic pathway. Biofizika 40(2), 434–442 (1995)

15.

F.I. Ataullakhanov, G.T. Guna, V.I. Sarbash, R.I. Volkova, Spatio-temporal dynamics of clotting and pattern formation in human blood. Biochim. Biophys. Acta Gen. Subjects 1425(3), 453–468 (1998)CrossRef

16.

F.I. Ataullakhanov, Y.V. Krasotkina, V.I. Sarbash, R.I. Volkova, E.I. Sinauridse, A.Y. Kondratov, Spatio-temporal dynamics of blood coagulation and pattern formation. An experimental study. Int. J. Bifurcation Chaos 12(9), 1969–1983 (2002)MathSciNetCrossRef

17.

F.I. Ataullakhanov, V.I. Zarnitsina, A.V. Pokhilko, A.I. Lobanov, O.L. Morozova, Spatio-temporal dynamics of blood coagulation and pattern formation. A theoretical approach. Int. J. Bifurcation Chaos 12(9), 1985 (2002)

18.

E. Bächli, History of tissue factor. Br. J. Hematol. 110, 248–255 (2000)CrossRef

19.

F. Bachmann, The discovery of factor X: a personal reminiscence. Thromb. Haemost. 98, 16–19 (2007)

20.

J. Bäck, J. Sanchez, G. Elgue, K.N. Ekdahl, B. Nilsson, Activated human platelets induce factor XIIa-mediated contact activation. Biochem. Biophys. Res. Commun. 39(1), 11–17 (2010)CrossRef

21.

P. Bagchi, Mesoscale simulation of blood flow in small vessels. Biophys. J. 92, 1858–1877 (2007)CrossRef

22.

C.N. Bagot, R. Arya, Virchow and his triad: a question of attribution. Br. J. Haematol. 143, 180–190 (2008)CrossRef

23.

H.A. Barnes, The yield stress - a review or “παντα ρες” - everything flows? J. Non-Newtonian Fluid Mech. 81, 133–178 (1999)

24.

L. Baronciani, P.M. Manucci, The molecular basis of disease, in Molecular Hematology, 3rd edn., ed. by D. Provan, J.G. Gribben, chap. 19 (Wiley-Blackwell, Hoboken, 2010), pp. 233–245

25.

C. Basciano, C. Kleinstreuer, S. Hyun, E.A. Finol, A relation between near-wall particle-hemodynamics and onset of thrombus formation in abdominal aortic aneurysms. Ann. Biomed. Eng. 39(7), 2010–2026 (2011)CrossRef

26.

R.C. Becker, Cell-based models of coagulation: a paradigm in evolution. J. Thromb. Thrombolysis 20(1), 65–68 (2005)CrossRef

27.

E. Beltrami, J. Jesty, Mathematical analysis of activation thresholds in enzyme-catalyzed positive feedbacks: application to the feedbacks of blood coagulation. Proc. Natl. Acad. Sci. USA 92, 8744–8748 (1995)MATHCrossRef

28.

T.K. Belval, J.D. Hellums, Analysis of shear-induced platelet aggregation with population balance mathematics. Biophys. J. 50(3), 479–487 (1986)CrossRef

29.

J. Bernard, J.P. Soulier, Sur une nouvelle varit de dystrophie thrombocytaire hemorragipare congnitale. Semaine des Hpitaux de Paris 24, 3217–3223 (1948)

30.

J. Bernsdorf, S.E. Harrison, S.M. Smith, P.V. Lawford, D.R. Hose, Applying the lattice Boltzmann technique to biofluids: a novel approach to simulate blood coagulation. Comput. Math. Appl. 55(7), 1408–1414 (2008)MATHMathSciNetCrossRef

31.

R.M. Bertina, B.P. Koeleman, T. Koster et al., Mutation in blood coagulation factor V associated with resistance to activated protein C. Nature 369, 6467 (1994)CrossRef

32.

R. Biggs, A.S. Douglas, R.G. Macfarlane, J.V. Dacie, W.R. Pitney, C. Merskey, J.R. OBrien, Christmas disease: a condition previously mistaken for haemophilia. Br. Med. J. 2, 113–129 (1952)CrossRef

33.

T. Bodnár, A. Sequeira, Numerical simulation of the coagulation dynamics of blood. Comp. Math. Methods Med. 9(2), 83–104 (2008)MATHMathSciNetCrossRef

34.

T. Bodnár, K.R. Rajagopal, A. Sequeira, Simulation of the three-dimensional flow of blood using a shear-thinning viscoelastic fluid model. Math. Model. Nat. Phenom. 6, 1–24 (2011)MATHMathSciNetCrossRef

35.

T. Bodnár, A. Fasano, A. Sequeira, Mathematical models for blood coagulation, in FluidStructure Interaction and Biomedical Applications, ed. by T. Bodnár, G.P. Galdi, S. Nečasová. Advances in Mathematical Fluid Mechanics, chap. 7 (Birkhäuser, Basel, 2014), pp. 483–569

36.

P.H. Bolton-Maggs, E.A. Chalmers, P.W. Collins, P. Harrison, S. Kitchen, R.J. Liesner, A. Minford, A.D. Mumford, L.A. Parapia, D.J. Perry, S.P. Watson, J.T. Wilde, M.D. Williams, A review of inherited platelet disorders with guidelines for their management on behalf of the UKHCDO. Br. J. Haematol. 135(5), 603–33 (2006)CrossRef

37.

I. Borsi, A. Farina, A. Fasano, K.R. Rajagopal, Modelling the combined chemical and mechanical action for blood clotting. Math. Sci. Appl. 9(2), 83–104 (2008)MATH

38.

K. Boryczko, W. Dzwinela, D.A. Yuen, Modeling fibrin aggregation in blood flow with discrete-particles. Comput. Methods Prog. Biomed. 75, 181–194 (2004)CrossRef

39.

D.B. Brewer, Max Shultze (1865), G. Bizzozero (1882) and the discovery of the platelet. Br. J. Haematol. 133, 251–258 (2006)

40.

L. Brugnano, F. Di Patti, G. Longo, An incremental mathematical model for Immune Thrombocytopenic Purpura (ITP). Math. Comput. Modell. 42(1112), 1299–1314 (2005)MATHMathSciNetCrossRef

41.

K. Brummel-Ziedins, Models for thrombin generation and risk of disease. J. Thromb. Haemost. 11(Suppl.1), 212–223 (2013)CrossRef

42.

K.E. Brummel-Ziedins, T. Orfeo, M. Gissel, K.G. Mann, F.R. Rosendaal, Factor Xa generation by computational modeling: an additional discriminator to thrombin generation evaluation. PLoS ONE 7(1), e29178 (2012)

43.

D. Brune, S. Kim, Predicting protein diffusion coefficients. Proc. Natl. Acad. Sci. USA 90(9), 3835–3839 (1993)CrossRef

44.

S. Butenas, K.E. Brummel, R.F. Branda, S.G. Paradis, K.G. Mann, Mechanism of factor VIIa-dependent coagulation in hemophilia blood. Blood 99, 923–930 (2002)CrossRef

45.

S. Butenas, K.E. Brummel, B.A. Bouchard, K.G. Mann, How factor VIIa works in hemophilia. J. Thromb. Haemost. 1, 1158–1160 (2003)CrossRef

46.

S. Butenas, T. Orfeo, M.T. Gissel, K.E. Brummel, K.G. Mann, The significance of circulating factor IXa in blood. J. Biol. Chem. 279(22), 22875–22882 (2004)CrossRef

47.

S. Butenas, T. Orfeo, K.G. Mann, Tissue factor in coagulation: Which? Where? When? Arterioscler. Thromb. Vasc. Biol. 29, 1989–1996 (2009)CrossRef

48.

J. Caen, Q. Wu, Hageman factor, platelets and polyphosphates: early history and recent connection. J. Thromb. Haemost. 8(8), 1670–1674 (2010)CrossRef

49.

S.L. Carpenter, P. Mathew, α2-antiplasmin and its deficiency: fibrinolysis out of balance. Haemophilia 14, 1250–1254 (2008)

50.

M.S. Chatterjee, W.S. Denney, H. Jing, S.L. Diamond, System biology of coagulation initiation: kinetics of thrombin generation in resting and activated human blood. PLoS Comp. Biol. 6(9), 1–23 (2010)CrossRef

51.

S. Cito, M.D. Mazzeo, L. Badimon, A review of macroscopic thrombus modeling methods. Thromb. Res. 131, 116–124 (2013)CrossRef

52.

K.J. Clementson, Platelets disorders, in Molecular Hematology, 3rd edn., ed. by D. Provan, J.G. Gribben, chap. 20 (Wiley-Blackwell, Hoboken, 2010), pp. 246–258

53.

B.S. Coller, A brief history of ideas about platelets in health and disease. Foreword to [175], pp. xxiii–xl (2007)

54.

M.E. Combariza, X. Yu, W.S. Nesbitt, A. Mitchell, F.J. Tovar-Lopez, Nonlinear dynamic modelling of platelet aggregation via microfluidic devices. IEEE Trans. Biomed. Eng. 62, 1718–1727 (2015)CrossRef

55.

B. Cooper, Oslers role in defining the third corpuscle, or blood plates. Proceedings (Baylor University, Medical Center) 18(4), 376–378 (2005)

56.

J.M. Coutinho, J.M. Ferro, P. Canhão, F. Barinagarrementeria, C. Cantù M.G. Bousser, J. Stam, Cerebral venous and sinus thrombosis in women. Stroke 40, 2356–2361 (2009)CrossRef

57.

K.J. Croce, M. Sakuma, D.I. Simon, Platelet-leukocyte-endothelium cross talk. Chapter 7 of [96] (2008)

58.

L.M. Crowl, A.L. Fogelson, Computational model of whole blood exhibiting lateral platelet motion induced by red blood cells. Int. J. Numer. Method Biomed. Eng. 26, 471–487 (2010)MATHMathSciNetCrossRef

59.

B. Dahlbäck, Blood coagulation and its regulation by anticoagulant pathways: genetic pathogenesis of bleeding and thrombotic diseases. J. Intern. Med. 257(3), 209–223 (2005)CrossRef

60.

B. Dählbeck, A. Hillarp, Molecular coagulation and thrombophilia, in Molecular Hematology, 3rd edn., ed. by D. Provan, J.G. Gribben, chap. 17 (Wiley-Blackwell, Hoboken, 2010), pp. 208–218

61.

G. Davì, C. Patrono, Platelets activation and atherothrombosis. N. Engl. J. Med. 367, 2482–2494 (2007)CrossRef

62.

T. David, S. Thomas, P.G. Walker, Platelet deposition in stagnations point flow: an analytical and computational simulation. Med. Eng. Phys. 23, 299–132 (2001)CrossRef

63.

E.W. Davie, A brief historical review of the Waterfall/Cascade of blood coagulation. J. Biol. Chem. 278, 50819–50832 (2003)CrossRef

64.

E.W. Davie, O.D. Ratnoff, Waterfall sequence for intrinsic blood clotting. Science 145(3638), 1310–1312 (1964)CrossRef

65.

S.M. Dopheide, M.J. Maxwell, S.P. Jackson, Shear-dependent tether formation during platelet translocation on von Willebrand factor. Blood 99, 159–167 (2002)CrossRef

66.

R.L. Drake, A general mathematical survey of the coagulation equation, in Topics in Current Aerosol Research (Part 2), ed. by G.M. Hidy, J.R. Brock. International Reviews in Aerosol Physics and Chemistry, vol. 3 (Pergamon Press, Oxford, 1972), pp. 201–376

67.

W. Dzwinel, K. Boryczko, D.A. Yuen, A discrete-particle model of blood dynamics in capillary vessels. J. Colloid Interface Sci. 258, 163–173 (2003)MATHCrossRef

68.

K.E. Eilertsen, B. Østerud, The role of blood cells and their microparticles in blood coagulation. Biochem. Soc. Trans. 33(2), 418–422 (2005)CrossRef

69.

S.G. Farmer (ed.), The Kinin System (Academic, London, 1997)

70.

A. Fasano, The dynamics of two-phase liquid dispersions: necessity of a new approach. Milan J. Math. 70, 245–264 (2002)MATHMathSciNetCrossRef

71.

A. Fasano, R. Santos, A. Sequeira, Blood coagulation: a puzzle for biologists, a maze for mathematicians, in Modelling Physiological Flows, ed. by D. Ambrosi, A. Quarteroni, G. Rozza, chap. 3 (Springer Italia, Milano, 2011), pp. 44–77. doi:10.1007/978-88-470-1935-53

72.

A. Fasano, J. Pavlova, A. Sequeira, A synthetic model for blood coagulation including blood slip at the vessel wall. Clin. Hemorheol. Microcirc. 54, 1–14 (2013)

73.

P-J. Fay, P.J. Haidaris, T.M. Smudzin, Human factor VIIIa subunit structure. J. Biol. Chem. 14, 8957–8962 (1991)

74.

D.A. Fedosov, G.E. Karniadakis, Triple-decker: interfacing atomistic - mesoscopic - continuum flow regimes. J. Comput. Phys. 228(4), 1157–1171 (2009)MATHMathSciNetCrossRef

75.

B.G. Firkin, The Platelets and its Disorders (MTP Press, Washington, 1984)CrossRef

76.

A.L. Fogelson, A mathematical model and numerical method for studying platelet adhesion and aggregation during blood clotting. J. Comput. Phys. 56, 111–134 (1984)MATHMathSciNetCrossRef

77.

A.L. Fogelson, Continuum models of platelet aggregation: formulation and mechanical properties. SIAM J. Appl. Math. 52(4), 1089–1110 (1992)MATHMathSciNetCrossRef

78.

A.L. Fogelson, R.D. Guy, Platelet-wall interactions in continuum models of platelet thrombosis: formulation and numerical solution. Math. Med. Biol. 21(4), 293–334 (2004)MATHCrossRef

79.

A.L. Fogelson, R.D. Guy, Immersed-boundary-type models of intravascular platelet aggregation. Comput. Methods Appl. Mech. Eng. 197, 2087–2104 (2008)MATHMathSciNetCrossRef

80.

A.L. Fogelson, J.P. Keener, Toward an understanding of fibrin branching structure. Phys. Rev. E Stat. Nonlin. Soft Matter Phys. 81, 1–24 (2010)MathSciNetCrossRef

81.

A.L. Fogelson, N. Tania, Coagulation under flow: the influence of flow-mediated transport on the initiation and inhibition of coagulation. Pathophysiol. Haemost. Thromb. 34, 91–108 (2005)CrossRef

82.

W.B. Foster, M.E. Nesheim, K.G. Mann, The factor Xa-catalyzed activation of factor V. J. Biol. Chem. 258, 13970–13977 (1983)

83.

D. Gailani, A. Zivelin, D. Sinha, P.N. Walsh, Do platelets synthesize factor XI? J. Thromb. Haemost. 2(10), 1709–1712 (2004)CrossRef

84.

H. Galina, J.B. Lechowicz, Mean-field kinetic modeling of polymerization: the Smoluchowski coagulation equation. Adv. Polym. Sci. 137, 135–172 (1998)CrossRef

85.

R.B. Gayle III, Ch.R. Maliszewski, S.D. Gimpel, M.A. Schoenborn, R. Guy Caspary, C. Richards, K. Brasel, V. Price, J.H.F. Drosopoulos, N. Islam, T.N. Alyonycheva, M.J. Broekman, A.J. Marcus, Inhibition of platelet function by recombinant soluble Ecto-ADPase/CD39. J. Clin. Invest. 101, 1851–1859 (1998)CrossRef

86.

V. Gazzaniga, L. Ottini, The discovery of platelets and their function. Vesalius 17, 22–26 (2001)

87.

J.N. George, Thrombotic thrombocytopenic purpura. New Engl. J. Med. 354, 1927–1935 (2006)CrossRef

88.

P. Giangrande, Six characters in search of an author: the history of the nomenclature of coagulation factors. Br. J. Haematol. 121, 703–712 (2003)CrossRef

89.

P. Giangrande, Acquired hemophilia (revised ed.), in Treatment of Hemophilia, vol. 38 (World Federation of Hemophilia, 2012), pp. 1–7

90.

L. Gilchrist, A female case of haemophilia. Proc. R. Soc. Med. 54(9), 813814 (1961)

91.

W.E. Glanzmann, Hereditäre hämorrhägische Thrombasthenie. Ein Beitrag zur Pathologie der Blutplättchen. Jahrbuch für Kinderheilkunde 88, 1–42, 113–141 (1918)

92.

S.Z. Goldhaber, A. Leizorovicz, A.K. Kakkar et al., Apixaban versus enoxaparin for thrombophylaxix in medically ill patients. N. Engl. J. Med. 365, 2167–2177 (2011)CrossRef

93.

H.L. Goldsmith, V.T. Turitto, Rheological aspects of thrombosis and haemostasis: basic principles and applications. Thromb. Heamost. 55(3), 100–105 (1986)

94.

G.H. Goldsmith Jr., H. Saito, O.D. Ratnoff, The activation of Plasminogen by Hageman Factor (Factor XII) and Hageman Factor fragments. J. Clin. Invest. 62, 54–60 (1978)CrossRef

95.

A. Gómez-Outes, A. Terleira-Fernández, G. Calvo-Rojas, M.L. Suárez-Gea, E. Vargas-Castrillón, Dabigatran, rivaroxaban, or apixaban versus warfarin in patients with nonvalvular atrial fibrillation: a systematic review and meta – analysis of subgroups. Thrombosis (2013). doi:10.1155/2013/640723

96.

P. Gresele, V. Fuster, J.A. Lopez, C.P. Page, J. Vermylen (eds.), Platelets in Hematologic and Cardiovascular Disorders: A Clinical Handbook (Cambridge University Press, Cambridge, 2008)

97.

L. Grinberg, D.A. Fedosov, G.E. Karniadakis, Parallel multiscale simulations of a brain aneurysm. J. Comput. Phys. 244, 131–147 (2013)MathSciNetCrossRef

98.

R.I. Handin, Inherited platelets disorders. Hematology 2005, 396–402 (2005)CrossRef

99.

C.M. Hanley, P.R. Kowey, Are the novel anticoagulants better than warfarin for patients with atrial fibrillation? J. Thorac. Dis. 7(2), 165–171 (2015)

100.

S.E. Harrison, S.M. Smith, J. Bernsdorf, D.R. Hose, P.V. Lawford, Application and validation of the lattice Boltzmann method for modelling flow-related clotting. J.Biomech. 3023–3028 (2007)

101.

W.E. Hathaway, L.P. Belhasen, H.S. Hathaway, Evidence for a new plasma thromboplastin factor. I. Case report, coagulation studies and physico-chemical properties. Blood 26, 521 (1965)

102.

C.R.M. Hay, Thrombosis and recombinant factor VIIa. J. Thromb. Haemost. 2, 1698–1699 (2004)CrossRef

103.

U. Hedner, M. Ezban, Tissue Factor and Factor VIIa as therapeutic targets in disorders of hemostasis. Annu. Rev. Med. 59, 29–41 (2008)CrossRef

104.

H.C. Hemker, S. Kerdelo, R.M. Kremers, Is there value in kinetic modeling of thrombin generation? No (unless). J. Thromb. Haemost. 10, 1470–1477 (2002)CrossRef

105.

D. Hershey, S.J. Cho, Blood flow in rigid tubes: thickness and slip velocity of plasma film at the wall. J. Appl. Physiol. 21, 27–32 (1966)

106.

O. Hetland, A.B. Brovold, R. Holme, G. Gaudernack, H. Prydz, Thromboplastin (tissue factor) in plasma membranes of human monocytes. Biochem. J. 228(3), 735–743 (1985)CrossRef

107.

M.F. Hockin, K.C. Jones, S.J. Everse, K.G. Mann, A model for the stoichiometric regulation of blood coagulation. J. Biol. Chem. 277(21), 18322–18333 (2002)CrossRef

108.

M. Hoffman, Remodeling the blood coagulation cascade. J. Thromb. Thrombolysis 16(1–2), 17–20 (2003)CrossRef

109.

C. Hougie, E.M. Barrow, J.M. Graham, Segregation of an hereditary hemorrhagic group heretofore called stable factor (SPCA), proconvertin, factor VII deficiency. J. Clin. Invest. 36, 485–496 (1957)CrossRef

110.

W.H. Howell, E. Holt, Two new factors in blood coagulation: heparin and pro-antithrombin. Am. J. Physiol. 47, 228–241 (1918)

111.

L. Hsieh, D. Nugent, Factor XIII deficiency. Haemophilia 14, 1190–1200 (2008)CrossRef

112.

P.Y. Huang, J.D. Hellums, Aggregation and disaggregation kinetics of human blood platelets: part I. Development and validation of a population balance method. Biophys. J. 65(1), 334–343 (1993)

113.

P.Y. Huang, J.D. Hellums, Aggregation and disaggregation kinetics of human blood platelets: part II. Shear-induced platelet aggregation. Biophys. J. 65(1), 344–353 (1993)

114.

P.Y. Huang, J.D. Hellums, Aggregation and disaggregation kinetics of human blood platelets: part III. The disaggregation under shear stress of platelet aggregates. Biophys. J. 65(1), 354–361 (1993)

115.

Y. Ikeda, M. Handa, K. Kawano, T. Kamata, M. Murata, Y. Araki, H. Anbo, Y. Kawai, K. Watanabe, I. Itagaki, K. Sakai, Z.M. Ruggeri, The role of von Willebrand Factor and Fibrinogen in platelet aggregation under varying shear stress. J. Clin. Invest. 87, 1234–1240 (1991)CrossRef

116.

G.I.C. Ingram, The history of haemophilia. J. Clin. Pathol. 29(6), 469–479 (1976)CrossRef

117.

J. Jesty, E. Beltrami, Positive feedbacks of coagulation. Their role in threshold regulation. Arterioscler. Thromb. Vasc. Biol. 25, 2463–2469 (2005)MATHCrossRef

118.

K.C. Jones, K.G. Mann, A model for the tissue factor pathway to thrombin. II. A mathematical simulation. J. Biol. Chem. 269(37), 23367–23373 (1994)

119.

G. Karniadakis, S. Sherwin, Spectral/hp Element Methods for Computational Fluid Dynamics, 3rd edn. (Oxford University Press, Oxford, 2013)MATH

120.

C.J. Kastrup, F. Shen, M.K. Runyon, R.F. Ismagilov, Characterization of the threshold response of initiation of blood clotting to stimulus patch size. Biophys. J. 93, 2969–2977 (2007)CrossRef

121.

A. Kauskot, M.F. Hoylaerts, Platelet receptors, in Antiplatelet Agents, Handbook of Experimental Pharmacology, ed. by P. Gresele, G.V.R. Born, C. Patrono, C.P. Page (eds.) (Springer, Berlin, Heidelberg, 2012), pp. 23–57

122.

C. Kearon, S.R. Kahn, G. Agnelli, Antithrombotic therapy for venous thromboembolic disease: American College of Chest Physicians evidence-based clinical practice guideline (8th edition). Chest 133, 454S–545S (2008)CrossRef

123.

E.F. Keller, L.A. Segel, Initiation of slime mold aggregation viewed as an instability. J. Theor. Biol. 26, 399–415 (1970)MATHCrossRef

124.

J.G. Kelton, T.E. Warkentin, Heparin-induced thrombocytopenia: historical perspective. Blood 112, 2607–2616 (2008)CrossRef

125.

N. Key, M. Makris, D. O’Shaughnessy, D. Lillicrap (eds.), Practical Hemostasis and Thrombosis, 2nd edn. (Wiley-Blackwell, Hoboken, 2009)

126.

M.A. Khanin, V.V. Semenov, A mathematical model of the kinetics of blood coagulation. J. Theor. Biol. 136, 127–134 (1989)MathSciNetCrossRef

127.

P. Kleinbongard, R. Schulz, T. Rassaf, T. Lauer, A. Dejam, T. Jax, I. Kumara, P. Gharini, S. Kabanova, B. Özüyaman, H.G. Schnäurch, A. Gäodecke, A.A. Weber, M. Robenek, H. Robenek, W. Bloch, P. Rösen, M. Kelm, Red blood cells express a functional endothelial nitric oxide synthase. Blood 107, 2943–2951 (2006)CrossRef

128.

C. Kleinstreuer, J.R. Buchanan, M. Lei, G.A. Truskey, Computational analysis of particle hemodynamics and prediction of the onset of arterial diseases, in Biomechanical Systems, Techniques and Applications, Volume II. Cardiovascular Techniques (CRC Press, West Palm Beach, 2001)

129.

K. Knauer, R. Huber, Fibrinolysis and beyond: bridging the gap between local and systemic clot removal. Front. Neurol. 2 (2011). doi:10.3389/fneur.2011.00007

130.

A.E. Kogan, D.V. Kardakov, M.A. Khanin, Analysis of the activated partial thromboplastin time test using mathematical modeling. Thromb. Res. 101(4), 299–310 (2001)CrossRef

131.

F. Koller, A. Loeliger, F. Duckert, Experiments on a new clotting factor (factor VII). Acta Haematol. 6, 1–18 (1951)CrossRef

132.

H. Kraut, E.K. Frey, E. Werle, Über die Inaktivierung des Kallikreins. Hoppe-Seyler’ s Z. Physiol. Chem. 192, 1–21 (1930)CrossRef

133.

S. Krishnaswamy, The transition of prothrombin to thrombin. J. Thromb. Haemost. 11(01), 265–276 (2013). doi:10.1111/jth.12217CrossRef

134.

A.L. Kuharsky, A.L. Fogelson, Surface-mediated control of blood coagulation: the role of binding site densities and platelet deposition. Biophys. J. 80(3), 1050–1074 (2001)CrossRef

135.

M.J. Lacombe, Deficit constitutionnel en un nouveau facteur de la coagulation intervenant au niveau de contact: le facteur “Flaujeac”. C. R. Hebd. Seances Acad. Sc. Ser. D. Sci. Nat. 280, 1039–1041 (1975)

136.

K. Laki, L. Lorand, On the solubility of fibrin clots. Science 108, 280 (1948)CrossRef

137.

M.R. Lassen, W. Ageno, L.C. Borris, Rivaroxaban versus enoxaparin for thrombophylaxix after total knee arthroplasty. N. Engl. J. Med. 358, 2776–2786 (2008)CrossRef

138.

M.R. Lassen, A. Gallus, G.E. Raskob et al., Apixaban versus enoxaparin for thrombophylaxix after hip replacement. N. Engl. J. Med. 363, 2487–2498 (2010)CrossRef

139.

I.J. Laurenzi, S.L. Diamond, Monte Carlo simulation of the heterotypic aggregation kinetics of platelets and neutrophils. Biophys. J. 77(3), 1733–1746 (1999)CrossRef

140.

K. Leiderman, A.L. Fogelson, Grow with the flow: a spatial-temporal model of platelet deposition and blood coagulation under flow. Math. Med. Biol. 28, 47–84 (2011)MATHMathSciNetCrossRef

141.

R.J. Leipold, T.A. Bozarth, A.L. Racanelli, I.B. Dicker, Mathematical model of serine protease inhibition in the tissue factor pathway to thrombin. J. Biol. Chem. 270(43), 25383–25387 (1995)CrossRef

142.

S.N. Levine, Enzyme amplifier kinetics. Science 152(3722), 651–653 (1966)CrossRef

143.

B.B.C. Lim, E.H. Lee, M. Sotomayor, K. Schulten, Molecular basis of fibrin clot elasticity. Structure 16, 449–459 (2008)CrossRef

144.

Y. Liu, L. Zhang, X. Wang, W.K. Liu, Coupling of Navier-Stokes equations with protein molecular dynamics and its application to hemodynamics. Int. J. Numer. Methods Fluids 46(12), 1237–1252 (2004)MATHMathSciNetCrossRef

145.

K. Lo, W.S. Denney, S.L. Diamond, Stochastic modeling of blood coagulation initiation. Pathophysiol. Haemost. Thromb. 34(2–3), 80–90 (2006)

146.

I. Lopez-Vilchez, G. Escolar, M. Diaz-Ricart, B. Fuste, A.M. Galan, J.G. White, Tissue factor-enriched vesicles are taken up by platelets and induce platelet aggregation in the presence of factor VIIa. Thromb. Haemost. 97(2), 202–211 (2007)

147.

R.G. MacFarlane, An enzyme cascade in the blood clotting mechanism, and its function as a biochemical amplifier. Nature 202(4931), 498–499 (1964)CrossRef

148.

C. Malmsten, M. Hamberg, J. Svenson, B. Samuelsson, Physiological role of an endoperoxide in human platelets: hemostatic defect due to platelet Cyclo-Oxygenase deficiency. Proc. Natl. Acad. Sci. USA 72, 1446–1450 (1975)CrossRef

149.

K.G. Mann, M.E. Nesheim, P.B. Tracy, L.S. Hibbard, J.W. Bloom, Assembly of the prothrombinase complex. Biophys. J. 37, 106–107 (1982)CrossRef

150.

K.G. Mann, S. Butenas, K. Brummel, The dynamics of thrombin formation. Arterioscler. Thromb. Vasc. Biol. 23(1), 17–25 (2003)CrossRef

151.

K.G. Mann, K. Brummel-Ziedins, T. Orfeo, S. Butenas, Models of blood coagulation. Blood Cells Mol. Dis. 36(2), 108–117 (2006)CrossRef

152.

J.A. Marcum, The origin of the dispute over the discovery of heparin. J. Hist. Med. Allied Sci. 55, 37–66 (2000)CrossRef

153.

V.J. Marder, W.C. Aird, J.S. Bennett, S. Schulman, G.C. White II (eds.), Hemostasis and Thrombosis: Basic Principles and Clinical Practice, 6th edn. (Lippincott Williams & Wilkins, Wolters Kluwer, Philadelphia, 2013)

154.

A.L. Marshal, J.L. Spivak, L.A. Boxer, S.J. Shattil, E.S. Henderson (eds.), Hematology: Landmark Papers of the Twentieth Century (Academic, London, 2000)

155.

F. Martorana, A. Moro, On the kinetics of enzyme amplifier systems with negative feedback. Math. Biosci. 21, 77–84 (1974)MATHCrossRef

156.

A.V. Mattioli, Heparin-induced thromboytopenia: a misdiagnosed clinical syndrome. Bol. SPHM 27, 5–10 (2012)

157.

M. Maxey, B. Patel, Localized force representations for particles sedementing in Stokes flow. Int. J. Multiphase Flow 27(9), 1603–1626 (2001)MATHCrossRef

158.

J. Mc Lean, The discovery of heparin. Circulation 19, 75–78 (1959)CrossRef

159.

S. Melchionna, A model for red blood cells in simulations of large-scale blood flows. Macromol. Theory Simul. 20, 548–561 (2011)CrossRef

160.

A.D. Michelson, Platelets, 3rd edn. (Elsevier Inc., London, 2013)

161.

A.Y. Mitrophanov, J. Reifman, Kinetic modeling sheds light on the mode of action of recombinant factor VIIa on thrombin generation. Thromb. Res. 128, 381–390 (2011)CrossRef

162.

A.Y. Mitrophanov, A.S. Wolberg, J. Reifman, Kinetic model facilitates analysis of fibrin generation and its modulation by clotting factors: implications for hemostasis-enhancing therapies. Mol. BioSyst. 10, 2347–2357 (2004)CrossRef

163.

A.Y. Mitrophanov, F.R. Rosendaal, J. Reifman, Therapeutic correction of thrombin generation in dilution-induced coagulopathy: computational analysis based on a data set of healthy subjects. J. Trauma Acute Care Surg. 73, S95YS102 (2012)

164.

J.L. Moake, Thrombotic microangiopathies. New Engl. J. Med. 347, 589–600 (2002)CrossRef

165.

G. Moiseyev, S. Givli, P.Z. Bar-Yoseph, Fibrin polymerization in blood coagulation: a statistical model. J. Biomech. 46(1), 26–30 (2013)CrossRef

166.

P. Monage (ed.), Haemostasis: Methods and Protocols. Methods in Molecular Biology, vol. 992 (Springer Science + Business Media, New York, 2013)

167.

D.D. Monkovict, P.B. Tracy, Activation of human Factor V by Factor Xa and thrombin. Biochemistry 29, 1118–1128 (1990)CrossRef

168.

D.M. Monroe, Factor VIIa: on its own and loving it. Blood 120, 705–707 (2012)CrossRef

169.

P. Morawitz, Die Chemie der Blutgerinnung. Ergebn. Physiol. 4, 307–422 (1905)CrossRef

170.

D. Mori, K. Yano, K.-I. Tsubota, T. Ishikawa, S. Wada, T. Yamaguchi, Computational study on effect of red blood cells on primary thrombus formation. Thromb. Res. 123, 114–121 (2008)CrossRef

171.

A. Moro, A.T. Bharucha-Reid, On the kinetics of enzyme amplifier systems. Math. Biosci. 5, 391–402 (1969)MATHCrossRef

172.

N.J. Mutch, L. Thomas, N.R. Moore, K.M. Lisiak, N.A. Booth, TAFIa, PAI-1 and alpha 2-antiplasmin: complementary roles in regulating lysis of thrombi and plasma clots. J. Thromb. Haemost. 5, 812–817 (2007)CrossRef

173.

M.E. Nesheim, W.M. Canfield, W. Kisiel, K.G. Mann, Studies of the capacity of factor Xa to protect factor Va from inactivation by activated protein C. J. Biol. Chem. 257(3), 1443–1447 (1982)

174.

L.M. O’Brien, M. Mastri, P.J. Fay, Regulation of Factor VIIIa by human activated protein C and protein S: inactivation of cofactor in the intrinsic factor Xase. Hemost. Thromb. Vasc. Biol. 95, 1714–1720 (2000)

175.

T. Orfeo, S. Butenas, K.E. Brummel-Ziedins, K.G. Mann, The Tissue Factor requirement in blood coagulation. J. Biol. Chem. 280, 42887–42896 (2005)CrossRef

176.

R. Ouared, B. Chopard, B. Stahl, D.A. R’́ufenacht, H. Yilmaz, G. Courbebaisse, Thrombosis modeling in intracranial aneurysms: a lattice Boltzmann numerical algorithm. Comput. Phys. Commun. 179(1–3), 128–131 (2008)

177.

C.A. Owen, A History of Blood Coagulation (Mayo Foundation for Medical Education and Research, Rochester, MN, 2001)

178.

P.A. Owren, The coagulation of blood. Investigations on a new clotting factor. Acta Med. Scand. 194, 521–549 (1947)

179.

P.A. Owren, Parahaemophilia. Haemorragic diathesis due to absence of a previously unknown clotting factor. Lancet 1, 446–451 (1947)

180.

O. Panes, V. Matus, C.G. Sáez, T. Quiroga, J. Pereira, D. Mezzano, Human platelets synthesize and express functional tissue factor. Blood 109, 5242–5250 (2007)CrossRef

181.

M.A. Panteleev, M.V. Ovanesov, D.A. Kireev, A.M. Shibeko, E.I. Sinauridze, N.M. Ananyeva, A.A. Butylin, E.L. Saenko, F.I. Ataullakhanov, Spatial propagation and localization of blood coagulation are regulated by intrinsic and protein C pathways, respectively. Biophys. J. 90(5), 1489–1500 (2006)CrossRef

182.

V. Pappu, P. Bagchi, 3D computational modeling and simulation of leukocyterolling adhesion and deformation. Comput. Biol. Med. 38, 738–753 (2008)CrossRef

183.

V. Pappu, S.K. Doddi, P. Bagchi, A computational study of leukocyte adhesion and its effect on flow pattern in microvessels. J. Theor. Biol. 254, 483–498 (2008)MathSciNetCrossRef

184.

A.J. Patek, R.H. Stetson, Hemophilia. I. The abnormal coagulation of the blood and its relation to the blood platelets. J. Clin. Invest. 15, 531–542 (1936)

185.

A.J. Patek, F.H.L. Taylor, Hemophilia. Some properties of a substance obtained from normal human plasma effective in accelerating the coagulation of hemophilic blood. J. Clin. Invest. 16, 113–124 (1937)

186.

C. Patrono, G. Ciabattoni, E. Pinca, F. Pugliese, G. Castrucci, A. De Salvo, M.A. Satta, B. A. Peskar, Low-dose aspirin and inhibition of thromboxane B2 production in healthy subjects. Thromb. Res. 17, 317–327 (1980)CrossRef

187.

L. Pauling, H.A. Itano, S.J. Singer, I.C. Wells, Sickle cell anemia, a molecular disease. Science 110, 543–548 (1949)CrossRef

188.

J. Pavlova, Mathematical modelling and numerical simulations of blood coagulation. PhD Thesis, University of Lisbon (2014)

189.

J. Pavlova, A. Fasano, J. Janela, A. Sequeira, Numerical validation of a synthetic cell-based model of blood coagulation. J. Theor. Biol. 380, 367–379 (2015)MATHMathSciNetCrossRef

190.

J. Pavlova, A. Fasano, A. Sequeira, Numerical simulations of a reduced model for blood coagulation. Z. Angew. Math. Phys. (ZAMP) 67(2), 28 (2016). doi:10.1007/s00033-015-0610-2

191.

H. Petscheck, D. Adamis, A. Kantrowitz, Stagnation flow thrombus formation. Trans. ASAIO 14, 256–260 (1968)

192.

I.V. Pivkin, P.D. Richardson, G. Karniadakis, Blood flow velocity effects and role of activation delay time on growth and form of platelet thrombi. PNAS 103(46), 17164–17169 (2006)CrossRef

193.

I.V. Pivkin, P.D. Richardson, G. Karniadakis, Effect of red blood cells on platelet aggregation. IEEE Eng. Med. Biol. Mag. 28(2), 32–37 (2009)CrossRef

194.

A. Pizard, C. Richer, N. Bouby, N. Picard, P. Meneton, M. Azizi, F. Alhenc-Gelas, Genetic deficiency in tissue kallikrein activity in mouse and man: effect on arteries, heart and kidney. Biol. Chem. 389(6), 701–706 (2008)CrossRef

195.

A. Podmore, M. Smith, G. Savidge, A. Alhaq, Real-time quantitative PCR analysis of factor XI mRNA variants in human platelets. J. Thromb. Haemost. 2(10), 1713–1719 (2004)CrossRef

196.

A.V. Pokhilko, F.I. Ataullakhanov, Contact activation of blood coagulation: trigger properties and hysteresis. J. Theor. Biol. 191(2), 213–219 (1998)CrossRef

197.

R.B. Potts, Some generalized order-disorder transformations. Proc. Camb. Philos. Soc. 48, 106–109 (1952)MATHMathSciNetCrossRef

198.

D. Raabe, Overview of the lattice Boltzmann method for nano- and microscale fluid dynamics in materials science and engineering. Model. Simul. Mater. Sci. Eng. 12(6), R13–R46 (2004)CrossRef

199.

K.R. Rajagopal, A.R. Srinivasa, A thermodynamic framework for rate type fluid models. J. Non-Newtonian Fluid Mech. 88(3), 207–227 (2000)MATHCrossRef

200.

O.D. Ratnoff, E.W. Davie, The purification of activated Hageman factor (activated Factor XII). Biochemistry 1, 967–974 (1962)CrossRef

201.

O.D. Ratnoff, J.M. Rosenblum, Role of Hageman factor in the initiation of clotting by glass: evidence that glass frees Hageman factor from inhibition. Am. J. Med. 25, 160–168 (1958)CrossRef

202.

O.D. Ratnoff, E.W. Davie, D.L. Mallett, Studies on the action of Hageman factor: evidence that activated Hageman factor in turn activates plasma thromboplastin antecedent. J. Clin. Invest. 40, 803–819 (1961)CrossRef

203.

O.D. Ratnoff, R.J. Busse, R.P. Sheon, The demise of John Hageman. New Engl. J. Med. 279, 760–761 (1968)CrossRef

204.

R.L. Reddick, T.R. Griggs, M.A. Lamb, K.M. Brinkhous, Platelet adhesion to damaged coronary arteries: comparison in normal and von Willebrand disease swine. Proc. Natl. Acad. Sci. USA 79(16I), 5076–5079 (1982)CrossRef

205.

D. Ribatti, E. Crivellato, Giulio Bizzozero and the discovery of platelets. Leuk. Res. 31, 1339–1441 (2007)CrossRef

206.

P. Ricciardi-Castagnoli (ed.), Dendritic Cells in Fundamental and Clinical Immunology (Plenum Press, New York, 1997)

207.

F.R. Rickles, S. Patierno, P.M. Fernandez, Tissue factor, thrombin, and cancer. Chest 124, 58S–68S (2003)CrossRef

208.

J.P. Riddel Jr., B.E. Aouizerat, C. Miaskowski, D.P. Lillicrap, Theories of blood coagulation. J. Pediatr. Oncol. Nurs. 24(3),123–131 (2007)CrossRef

209.

J. Rivera, M.L. Lozano, L. Navarro-Núñez, V. Vicente, Platelet receptors and signaling in the dynamics of thrombus formation. Haematologica 94(5), 700–711 (2009)CrossRef

210.

H.R. Roberts, Oscar Ratnoff: his contributions to the golden era of coagulation research. Br. J. Haematol. 122(2), 180–192 (2003)CrossRef

211.

F. Rodeghiero, R. Stasi, T. Gernsheimer, M. Michel, D. Provan, D.M. Arnold, J.B. Bussel, D.B. Cines, B.H. Chong, N. Cooper, B. Godeau, K. Lechner, M.G. Mazzucconi, R. McMillan, M.A. Sanz, P. Imbach, V. Blanchette, T. Kühne, M. Ruggeri, J.N. George, Standardization of terminology, definitions and outcome criteria in immune thrombocytopenic purpura of adults and children: report from an international working group. Blood 113(11), 2386–93 (2009)CrossRef

212.

R.L. Rosenthal, O.H. Dreskin, N. Rosenthal, New hemophilia-like disease caused by deficiency of a third plasma thromboplastin factor. Proc. Soc. Exp. Biol. Med. 82, 171–174 (1953)CrossRef

213.

R. Rosner, Medicine in the Bible and Talmud ( KTAV, New York, 1937)

214.

Z.M. Ruggeri, Perspective series: cell adhesion and vascular biology. J. Clin. Invest. 99, 559–564 (1997)CrossRef

215.

E.A. Ryan, L.F. Mockros, J.W. Weisel, L. Lorand, Structural origin of fibrin clot rheology. Biophys. J. 77, 2813–2826 (1999)CrossRef

216.

J.E. Sadler, Biochemistry and genetics of von Willebrand factor. Annu. Rev. Biochem. 67, 395–424 (1998)CrossRef

217.

B. Savage, J.J. Sixmad, Z.M. Ruggeri, Functional self-association of von Willebrand factor during platelet adhesion under flow. PNAS 99(1), 425–430 (2002)CrossRef

218.

A.H. Schmaier, G. LaRusch, Factor XII: new life for an old protein. Thromb. Haemost. 104(5), 915–918 (2010)CrossRef

219.

A.H. Schmaier, L.D. Dahl, A.J. Rozemuller, R.A. Roos, S.L. Wagner, R. Chung, W.E. Van Nostrand, Protease nexin-2/amyloid beta protein precursor. A tight-binding inhibitor of coagulation factor IXa. J. Clin. Invest. 92(5), 2540–2545 (1993)

220.

H.A.A. Schmidt, Über den Faserstoff und die. Ursachen seiner Gerinnung. Archiv. f’́ur Anatomie, Physiologie und wissenschaftliche Medicin, Leipzig, 545–587 (1861)

221.

H.A.A. Schmidt, Weiteres über den Faserstoff und die Ursachen seiner Gerinnung. Archiv fr Anatomie, Physiologie und wissenschaftliche Medicin, Leipzig, 428–469 (1862)

222.

S. Schulman, H. Eriksson, S. Goldhaber et al., Dabigratan or warfarin for extended manteinance therapy of venous thromboembolism. J. Thromb. Haemost. 9, O-TH-033 (2011)

223.

W.H. Seegers, Blood clotting mechanisms: three basic reactions. Annu. Rev. Physiol. 31, 269–294 (1969)CrossRef

224.

A. Sequeira, R.F. Santos, T. Bodnár, Blood coagulation dynamics: mathematical modeling and stability results. Math. Biosci. Eng. 8(2), 425–443 (2011)MATHMathSciNetCrossRef

225.

V. Shankar, G.B. Wright, A.L. Fogelson, R.M. Kirbya, A study of different modeling choices for simulating platelets within the immersed boundary method. Appl. Numer. Math. 63, 58–77 (2013)MATHMathSciNetCrossRef

226.

Z. Shariat-Madar, F. Mahdi, A.H. Schmaier, Identification and characterization of prolylcarboxypeptidase as an endothelial cell prekallikrein activator. J. Biol. Chem. 277(20), 17962–179629 (2002)CrossRef

227.

E.A. Shavlyugin, L.G. Hanin, M.A. Khanin, Dynamics of pathologic clot formation: a mathematical model. J. Theor. Biol. 340, 96–104 (2014)MathSciNetCrossRef

228.

G.J. Shaw, J.M. Meunier, S.L. Huang, C.J. Lindsell, D.D. McPherson, C.K. Holland, Ultrasound-enhanced thrombolysis with tPA-loaded echogenic liposome. Thromb. Res. 124(3), 306–310 (2009)CrossRef

229.

F. Shen, C.J. Kastrup, Y. Liu, R.F. Ismagilov, Threshold response of initiation of blood coagulation by tissue factor in patterned microfluidic capillaries is controlled by shear rate. Arterioscler. Thromb. Vasc. Biol. 28, 2035–2041 (2008)CrossRef

230.

F. Shen, R.R. Pompano, C.J. Kastrup, R.F. Ismagilov, Confinement regulates complex biochemical networks: initiation of blood clotting by “diffusion acting”. Biophys. J. 97, 2137–2145 (2009)CrossRef

231.

A.M. Shibeko, E.S. Lobanova, M.A. Panteleev, F.I. Ataullakhanov, Blood flow controls coagulation onset via the positive feedback of factor vii activation by factor XA. BMC Syst. Biol. 4, 5 (2010)CrossRef

232.

A.M. Shibeko, S.A. Woodle, T.K. Lee, M.V. Ovanesov, Unifying the mechanism of recombinant FVIIa action: dose dependence is regulated differently by tissue factor and phospholipids. Blood 120(4), 891–899 (2012)CrossRef

233.

S.A. Smith, The cell-based model of coagulation: State-Of-The-Art Review. J. Vet. Emerg. Crit. Care 19(1), 310 (2009)

234.

M.V. Smoluchowski, Drei vorträge über diffusion, brownsche bewegung und koagulation von kolloidteilchen. Z. Phys.17, 557–585 (1916)

235.

M. Spreafico, M. Peyvandi, Combined FV and FVIII deficiency. Hemophilia 14, 1201–1208 (2008)CrossRef

236.

E. Stavrou, A.H. Schmaier, Factor XII: what does it contribute to our understanding of the physiology and pathophysiology of hemostasis & thrombosis. Thromb. Res. 125(3), 210–215 (2010)CrossRef

237.

H. Stormorken, Paul A. Owren & the Golden Era of Haemostasis (Gazettebok, Sandvika, 2005)

238.

K. Suzuki, J. Stenflo, B. Dahlbäck, B. Teodorsson, Inactivation of human coagulation factor V by activated protein C. J. Biol. Chem. 258(3), 1914–1920 (1983)

239.

K. Tanaka, E.W. Davie (eds.), Recent Advances in Thrombosis and Hemostasis (Springer, New York, 2008)

240.

A.N. Tikhonov, Systems of differential equations containing small parameters multiplying the derivatives. Mat. Sborn. 31, 575–586 (1952)

241.

The EINSTEIN-PE Investigators, Oral rivaroxaban for the treatment of symptomatic pulmonary embolism. N. Engl. J. Med. 366, 1287–1297 (2012)

242.

A.A. Tokarev, Y.V. Krasotkina, M.V. Ovanesov, M.A. Panteleev, M.A. Azhigirova, V.A. Volpert, F.I. Ataullakhanov, A.A. Butilin, Spatial dynamics of contact-activated fibrin formation in vitro and in silico in haemophilia B: effects of severity and haemophilia B treatment. Math. Model. Nat. Phenom. 1(2), 124–137 (2006)MATHMathSciNetCrossRef

243.

A. Tokarev, I. Sirakov, G. Panasenko, V. Volpert, E. Shnol, A. Butylin, F. Ataullakhanov, Continuous mathematical model of platelet thrombus formation in blood flow. Russ. J. N. Anal. Math. Model. 27(2), 191–212 (2012)MATHMathSciNet

244.

A. Tosenberger, F. Ataullakhanov, N. Bessonov, M. Panteleev, A. Tokarev, V. Volpert, Modelling of thrombus growth in flow with a DPD-PDE method. J. Theor. Biol. 337, 30–41 (2013)MATHMathSciNetCrossRef

245.

S.D. Treadwell, B. Thanvi, T.G. Robinson, Stroke in pregnancy and the puerperium. Postgrad. Med. J. 84, 238–245 (2008)CrossRef

246.

A. Tripodi, The laboratory and the new oral anticoagulants. Clin. Chem. 59(2), 353–362 (2013)CrossRef

247.

A. Tripodi, G. Palareti, New anticoagulant drugs for the treatment of venous thromboembolism and stroke prevention in atrial fibrillation. J. Intern. Med. 271, 554–565 (2012)CrossRef

248.

A. Trousseau, Phlegmasia alba dolens: Clinique medicale de lHotel-Dieu de Paris, 2nd edn. (J. B. Balliere et Fils, Paris, 1865), pp. 654–712

249.

V.T. Turitto, H.R. Baumgartner, Platelet deposition on subendothelium exposed to flowing blood: mathematical analysis of physical parameters. Trans. Am. Soc. Artif. Intern. Org. 21, 593–601 (1975)

250.

B.O. Villoutreix, Structural bioinformatics: methods, concepts and applications to blood coagulation proteins. Curr. Protein Pept. Sci. 3, 341–364 (2002)CrossRef

251.

B.O. Villoutreix, O. Sperandio, In silico studies of blood coagulation proteins: from mosaic proteases to nonenzymatic cofactor inhibitors. Curr. Opin. Struct. Biol. 20, 168–179 (2010)CrossRef

252.

R. Virchow, Faserstoffarten und fibrinogene Substanz. Archiv für pathologische Anatomie und Physiologie und für klinische Medicin 1, 581 (1847)

253.

R.L.K. Virchow, Thrombose und Embolie. Gefässentzündung und septische infektion. gesammelte abhandlungen zur wissenschaftlichen medicin (Von Meidinger & Sohn., Frankfurt am Main, 1856), pp. 219–732

254.

C.Q. Xu, Y.J. Zeng, H. Gregersen, Dynamic model of the role of platelets in the blood coagulation system. Med. Eng. Phys. 24, 587–593 (2002)CrossRef

255.

C. Xu, X.H. Xu, Y. Zeng, Y.W. Chen, Simulation of a mathematical model of the role of the TFPI in the extrinsic pathway of coagulation. Comput. Biol. Med. 35(5), 435–445 (2005)CrossRef

256.

Z. Xu, N. Chen, M.M. Kamocka, E.D. Rosen, M. Alber, A multiscale model of thrombus development. J. R. Soc. Interface 5, 705–722 (2008)CrossRef

257.

Z. Xu, N. Chen, S.C. Shadden, J.E. Marsden, M.M. Kamocka, E.D. Rosen, M. Alber, Study of blood flow impact on growth of thrombi using a multiscale model. Soft Matter 5(4), 769–779 (2009)CrossRef

258.

Z. Xu, M. Kamocka, M. Alber, E.D. Rosen, Computational approaches to studying thrombus development. Arterioscler. Thromb. Vasc. Biol. 31, 500–505 (2011)CrossRef

259.

Z. Xu, O. Kim, M. Kamocka, E.D. Rosen, M. Alber, Multiscale models of thrombogenesis. Wiley Interdiscip. Rev. Syst. Biol. Med. 4, 237–246 (2012)CrossRef

260.

D. Xu, E. Kaliviotis, A. Munjiza, E. Avital, C. Ji, J. Williams, Large scale simulation of red blood cell aggregation in shear flows. J. Biomech. 46, 1810–1817 (2013)CrossRef

261.

K. Yano, D. Mori, K. Tsubota, T. Ishikawa, S. Wada, T. Yamaguchi, Analysis of destruction process of the primary thrombus under the influence of the blood flow. J. Biomech. Sci. Eng. 2(1), 3–44 (2007)CrossRef

262.

A. Yazdani, G.E. Karniadakis, Sub-cellular modeling of platelet transport in blood flow through microchannels with constriction. Soft Matter 12, 4339–4351 (2016). doi:10.1039/C6SM00154HCrossRef

263.

A. Yazdani, H. Li, J.D. Humphrey, G.E. Karniadakis, A general shear-dependent model for thrombus formation. PLoS Comput. Biol. 13(1), e1005291 (2017). doi:10.1371/journal.pcbi.1005291

264.

M.E. Young, P.A. Carroad, R.L. Bell, Estimation of diffusion coefficients of proteins. Biotechnol. Bioeng. 22(5), 947–955 (1980)CrossRef

265.

C. Wagner, P. Steffen, S. Svetina, Aggregation of red blood cells: from rouleaux to clot formation. C. R. Phys. 14(6), 459–469 (2013)CrossRef

266.

F.J. Walburn, J. Schneck, A constitutive equation for whole human blood. Biorheology 13, 201–210 (1978)CrossRef

267.

F.J. Walker, P.W. Sexton, C.T. Esmon, The inhibition of blood coagulation by activated Protein C through the selective inactivation of activated Factor V. Biochim. Biophys. Acta 571, 333 (1979)CrossRef

268.

P.N. Walsh, Roles of platelets and factor XI in the initiation of blood coagulation by thrombin. Thromb. Haemost. 86, 75–82 (2001)

269.

D. Wardrop, D. Keeling, The story of the discovery of heparin and warfarin. Br. J. Haematol. 141, 757–763 (2008)CrossRef

270.

H.J. Weiss, Flow-related platelet deposition on subendothelium. Thromb. Haemost. 74, 117–122 (1995)

271.

F.F. Weller, Platelet deposition in non-parallel flow: influence of shear stress and changes in surface reactivity. J. Math. Biol. 57(3), 333–359 (2008)MATHMathSciNetCrossRef

272.

F.F. Weller, A free boundary problem modeling thrombus growth: model development and numerical simulation using the level set method. J. Math. Biol. 61(6), 805–818 (2010)MATHMathSciNetCrossRef

273.

N.K. Wenger, Clinical characteristics of coronary heart disease in women: emphasis on gender differences. Cardiovasc. Res. 53(3), 558–567 (2002)CrossRef

274.

J.G. White, G. Escolar, The blood platelet open canalicular system: a two-way street. Eur. J. Cell Biol. 56(2), 233–242 (1991)

275.

G.M. Willems, T. Lindhout, W.T. Hermens, H.C. Hemker, Simulation model for thrombin generation in plasma. Haemostasis 21(4), 197–207 (1991)

276.

A. Wiskott, Familiarer, angeborener Morbus Werlhofii. Monatsschrift Kinderheilkunde 68, 212–216 (1937)

277.

I.S. Wright, The nomenclature of blood clotting factors. Can. Med. Assoc. J. 86, 373–374 (1962)

278.

J. Wu, C.K. Aidun, Simulating 3D deformable particle suspensions using lattice Boltzmann equation with external boundary force. Int. J. Numer. Methods Fluids 62(7), 202–2019 (2010)MATH

279.

K.D. Wuepper, Prekallikrein deficiency in man. J. Exp. Med. 138, 1345–1355 (1973)CrossRef

280.

K.D. Wuepper, C.G. Cochrane, Plasma Prekallikrein: isolation, characterization, and mechanism of activation. J. Exp. Med. 135, 1–20 (1972)CrossRef

281.

K.D. Wuepper, D.R. Miller, M.J. Lacombe, Flaujeac trait. Deficiency of human plasma kininogen. J. Clin. Invest. 56(6), 1663–1672 (1975)CrossRef

282.

V.I. Zarnitsina, A.V. Pokhilko, F.I. Ataullakhanov, A mathematical model for the spatio-temporal dynamics of intrinsic pathway of blood coagulation. I. The model description. Thromb. Res. 84(4), 225–236 (1996)CrossRef

283.

V.I. Zarnitsina, A.V. Pokhilko, F.I. Ataullakhanov, A mathematical model for the spatio-temporal dynamics of intrinsic pathway of blood coagulation. II. Results. Thromb. Res. 84(5), 333–344 (1996)CrossRef

284.

V.I. Zarnitsina, F.I. Ataullakhanov, A.I. Lobanov, O.L. Morozova, Dynamics of spatially nonuniform patterning in the model of blood coagulation. Chaos 11(1), 57–70 (2001)MATHCrossRef

285.

Y. Zhang, J.M. Scandura, W.E. Van Nostrand, P.N. Walsh, The mechanism by which heparin promotes the inhibition of coagulation factor XIa by protease nexin-2. J. Biol. Chem. 272(42), 26139–26144 (1997)CrossRef

286.

J. Zhang, P.C. Johnson, A.S. Popel, An immersed boundary lattice Boltzmann approach to simulate deformable liquid capsules and its applicationto microscopic blood flows. Phys. Biol. 4, 285–295 (2007)CrossRef

287.

P. Zhang, C. Gao, N. Zhang, M.J. Slepian, Y. Deng, D. Bluestein, Multiscale particle-based modeling of flowing platelets in blood plasma using dissipative particle dynamics and coarse grained molecular dynamics. Cell. Mol. Bioeng. 7(4), 552–574 (2014)CrossRef

288.

R.F. Zwaal, H.C. Hemker, Blood Coagulation (Elsevier Science Publisher, London, 1986)

289.

R.F. Zwaal, P. Comfurius, E.M. Bevers, Surface exposure of phosphatidylserine in pathological cells. Cell Mol. Life Sci. 62(9), 971–988 (2005)CrossRef

Titel: Blood Coagulation
verfasst von: Antonio Fasano
Adélia Sequeira
Verlag: Springer International Publishing
Buch: Hemomath
Print ISBN: 978-3-319-60512-8

Electronic ISBN: 978-3-319-60513-5

Copyright-Jahr: 2017
DOI: https://doi.org/10.1007/978-3-319-60513-5_2

Springer Professional

Abstract

Bitte loggen Sie sich ein, um Zugang zu Ihrer Lizenz zu erhalten.

Sie haben noch keine Lizenz? Dann Informieren Sie sich jetzt über unsere Produkte:

Springer Professional "Wirtschaft+Technik"

Springer Professional "Technik"

Springer Professional "Wirtschaft"

Premium Partner