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PubMed1979

The turnover in normal dogs of prothrombin and its fragments; effect of induced intravascular coagulation.

When 125I-labeled canine prothrombin was given to normal adult dogs intravenously, it was calculated that 240% of the plasma prothrombin crossed the capillary barrier per day, 410% of the interstitial prothrombin returned to the blood stream daily, and 79% of the plasmatic prothrombin was catabolized per day. These data are in close agreement with those observed for bovine prothrombin in calves by Takeda (1970). When derived from normal dog prothrombin, prethrombin-1 is a mixture of 2 polypeptides, one larger than the other, and both present in about equal amounts. The longer peptide, "prethrombin-1-long," was catabolized twice as fast as prothrombin, and the shorter, "prethrombin-1-short," 4 times faster. Prothrombin fragment-1 was catabolized by the normal dog still more rapidly. The catabolism of prothrombin was not accelerated in 3 dogs receiving continuous infusions of a thromboplastic emulsion of dog brain. Nor was the level of prothrombin in their plasma remarkably altered.

Afibrinogenemia↗
PubMed1972

Effects of cationic polypeptides on thrombasthenic and afibrinogenemic blood platelets.

Cationic polypeptides are known to cause the conversion of fibrinogen to fibrin gel and the immediate aggregation of blood platelets. In the present study, the effects of the cationic polypeptides, polybrene and polylysine, on normal, afibrinogenemic and thrombasthenic platelets were examined by nephelometry and electron microscopy. Normal and afibrinogenemic platelets aggregated rapidly and irreversibly after exposure to either agent. Thus, fibrinogen was not an essential factor for the interaction, though it may facilitate the rate of clumping produced by polybrene or polylysine. Thrombasthenic platelets did not aggregate rapidly or irreversibly in the presence of either agent. Shape change and slight degrees of clumping were induced by the cationic substances, a response essentially identical to the reaction of thrombasthenic platelets to collagen. The failure of cationic polypeptides to cause immediate aggregation of thrombasthenic platelets was not due to a failure of the agents to interact with the abnormal cells. Electron microscopy revealed that normal, afibrinogenemic and thrombasthenic platelets all adsorbed polybrene and polylysine, and transferred the agents to intracellular organelles.

Adenosine Diphosphate↗
PubMed1972

Exocytosis of secretory organelles from blood platelets incubated with cationic polypeptides.

The blood platelet release reaction involves the secretion, in parallel, of specific chemical constituents stored in intracellular organelles to the plasma without loss of substances suggestive of cell damage. The present investigation has employed an unusual effect of cationic polypeptides to follow the platelet secretory process. When platelets were incubated with polybrene and polylysine, the agents were taken up and deposited in cytoplasmic organelles. The matrix of granules developed a lattice-like substructure not produced by other chemical agents, and dark zones of granules and dense bodies became more electron opaque. Subsequently, the platelets exposed to cationic polypeptides underwent the shape change and internal transformation similar to that produced by potent aggregating agents. Granules and dense bodies appeared in the open canalicular system and were extruded in a relatively intact state from the altered platelets. No differences were observed in the response of normal, afibrinogenemic or thrombasthenic platelets to incubation with polybrene and polylysine. The results indicate that cationic polypeptides can stimulate the extrusion of secretory organelles, and support the previous reports suggesting that channels of the open canalicular system serve as conduits for discharging the products of the release reaction.

Afibrinogenemia↗