Isotopic studies of therapeutic anticoagulation with a coagulating enzyme

Bell, William R.; Regoeczi, E.

doi:10.1172/jci106406

Cited by 11 publications

(2 citation statements)

References 30 publications

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“…Lastly, brief note may be taken of the two venoms. Arvin and Reptilase [19,61,249]. Both split off peptide A, which results in formation of loose fibrin clots.…”

Section: Figmentioning

confidence: 99%

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Fibrinogen Synthesis, Distribution and Degradation

Reeve¹,

Franks²

2008

Semin Thromb Hemost

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Fibrinogen is a plasma protein of approximately 340,000 daltons containing everal per cent carbohydrate [169]. It is at least chiefly synthesized in the liver [156]. On exposure to thrombin it loses peptides [169] and forms long thin solid fibers [82]. These under the influence of fibrinase, Factor XIII [126,133], become markedly insoluble in the blood and tissue fluids, unless attacked by proteolytic enzymes such as plasmin [225]. Collections of intertwined fibers block holes in vessels thereby inhibiting blood loss, sometimes block the lumen of vessels thereby causing thrombosis, sometimes circulate in the blood stream till they lodge in vessels to cause emboli [72] and probably form a matrix for cell growth as in wound healing [7,278] and neoplastic spread [4]. A number of the many recent reviews of various aspects of fibrinogen behavior are noted below. Particularly relevant to what follows are reviews of the molecular structure of fibrinogen [169], the effects of proteolytic enzymes on fibrinogen [137], the pathways of catabolism of fibrinogen [167], the polymerization of fibrin monomers [63], the plasma and tissue fibrinogenolytic and fibrinolytic enzyme systems [152] and the control of protein synthesis in metazoan cells [168,271,232]. This review attempts to describe the physiology and pathophysiology of fibrinogen as it is synthesized, distributed to the blood stream and tissue fluids and catabolized, and to relate its somewhat extraordinary behavior to a few relevant features of what is known about other proteins. This requires discussion of some recent methods for studying fibrinogen metabolism and presentation of a picture of the fibrinogen molecule in continual motion from the time during which it is synthesized till the time when it is broken down through one or other of its several possible catabolic pathways. Also, this requires, because of the resulting clarification-and perhaps some readers may think this unfortunate-the use of some elementary mathematics of rate processes, which we try to keep as simple as possible and the use of which is

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“…Lastly, brief note may be taken of the two venoms. Arvin and Reptilase [19,61,249]. Both split off peptide A, which results in formation of loose fibrin clots.…”

Section: Figmentioning

confidence: 99%

“…Antibodies may develop after repeated use [124]. Arvin, unlike thrombin, does not stimulate fibrinogen synthesis [19].…”

Section: Figmentioning

confidence: 99%