Mechanism of Action of Thrombin on Platelets*

Schmid, Hans; Jackson, Dudley P.; Conley, C. Lockard

doi:10.1172/jci104508

Cited by 84 publications

(40 citation statements)

References 26 publications

(30 reference statements)

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“…Substrates 2 labeled with 14C were tested for radiochemical purity by paper chromatography: at least 98% of the radioactivity traveled with the authentic compound, and no contaminants were found. Solutions of puromycin dihydrochloride,3 adenosine diphosphate (ADP),4 and ethylenediaminetetraacetic acid (EDTA) 5 were prepared fresh for each experiment.…”

Section: Methodsmentioning

confidence: 99%

“…Thrombin, a proteolytic enzyme, is believed to cleave a fibrinogen-like constituent of the platelet membrane (4,5). This change in the platelet membrane renders it more permeable to serotonin, ADP, protein, and ions such as potassium and calcium (33,36), but the increased permeability may be relatively specific, since quite different proportions of various intracellular substances escape (33).…”

Section: Uu U)mentioning

confidence: 99%

“…Thrombin, possibly by cleaving fibrinogen in the plasma membrane of the platelet (4,5), produces a morphologic change in the membrane (6) and causes platelets to become adherent and aggregate; in the midst of a clot they fasten to fibrin strands (7). It has been suggested that retraction of the fibrin clot is effected by thrombosthenin, an actomyosinlike contractile protein of platelets (8).…”

mentioning

confidence: 99%

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The stimulation by thrombin of glucose oxidation in human platelets.

Warshaw¹,

Laster²,

Shulman³

1966

J. Clin. Invest.

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Section: Methodsmentioning

confidence: 99%

Section: Uu U)mentioning

confidence: 99%

mentioning

confidence: 99%

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The stimulation by thrombin of glucose oxidation in human platelets.

Warshaw¹,

Laster²,

Shulman³

1966

J. Clin. Invest.

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“…After incubation with trypsin under appropriate conditions, platelets remain morphologically intact but no longer contain clottable protein (5). Trypsinized platelets, unlike normal platelets, are not aggregated by fresh serum or by a solution of thrombin and calcium chloride.…”

mentioning

confidence: 99%

Role of Platelet Fibrinogen in the Reactions of Platelets to Thrombin*

Morse¹,

Jackson²,

Conley³

1965

J. Clin. Invest.

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Washed human blood platelets contain a clottable protein that is similar to, if not identical with, plasma fibrinogen (1-4). After incubation with trypsin under appropriate conditions, platelets remain morphologically intact but no longer contain clottable protein (5). Trypsinized platelets, unlike normal platelets, are not aggregated by fresh serum or by a solution of thrombin and calcium chloride. When resuspended in plateletfree plasma or in a buffered solution of fibrinogen containing glucose, trypsinized platelets produce retraction of clots formed by thrombin; during the formation of the clot and its subsequent retraction, trypsinized platelets aggregate and undergo the usual changes of viscous metamorphosis (5). These observations suggest that fibrinogen on the surface of platelets is involved in the reaction of platelets to thrombin. This reaction does not consist simply of the coagulation of fibrinogen with entrapment of platelets in the fibrin mesh. Under usual conditions divalent cations are required for thrombin-induced platelet aggregation but not for clotting of fibrinogen (5, 6). Electron photomicrographs of platelet aggregates show no striated fibrin strands between adherent

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“…The discovery of the mechanism of action of thrombin on platelets (through fibrinogen) was published in the JCI (62). 1963…”

mentioning

confidence: 99%