Purification And Mechanism Study Of Collagen-Specific Platelet Aggregation Inhibitory Factor From The Salivary Gland Of Haemaphysalis Longicornis
Keywords
Haemaphysalis Longicornis, Salivary Gland, Longicornin, Collagen, Antiplatelet
Abstract
new collagen-specific platelet aggregation inhibitory factor was purified from the salivary gland homogenate of Haemaphysalis longicornis, named “longicornin”. It can specifically inhibit collagen-induced platelet aggregation reaction, while other agonists such as ADP, peanut Purified platelet aggregation induced by tetraenoic acid, thrombin, ristocetin, A23187, U46619, and phorbol acetate had no inhibitory effect. Longicornin can also inhibit the platelet activation process, including the release of platelet granules and the intercellular matrix. The increase in free Ca2+ concentration has no inhibitory effect on the adhesion between collagen and platelets. Longicorin may have the same receptor on platelets as collagen, and its binding to the platelet receptor is reversible.
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Original research was done by Cheng Yuanguo, Wu Houyong, Li De
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