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[Effect of Defensin on Platelet Functional Activity]

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Date 1993 Jan 1
PMID 8054565
Citations 1
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Abstract

The effects of human neutrophil peptide defensin were studied on human platelet function. Defensin (0.1-40 micrograms/mL) did not promote platelet aggregation. Defensin decreased platelet aggregation responses to ADF, collagen or thrombin. Defensin significantly lessened ATP level, released during platelet aggregation, and malondialdehyde production, induced by thrombin and collagen. These data reveal that defensins involve in cell-cell interaction between platelets and neutrophils counteracting agonist-induced platelet activation.

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References
1.
Smith J, Ingerman C, Silver M . Malondialdehyde formation as an indicator of prostaglandin production by human platelets. J Lab Clin Med. 1976; 88(1):167-72. View

2.
Ganz T, Selsted M, Lehrer R . Defensins. Eur J Haematol. 1990; 44(1):1-8. DOI: 10.1111/j.1600-0609.1990.tb00339.x. View

3.
Mustard J, Perry D, Ardlie N, Packham M . Preparation of suspensions of washed platelets from humans. Br J Haematol. 1972; 22(2):193-204. DOI: 10.1111/j.1365-2141.1972.tb08800.x. View

4.
Lichtenstein A, Ganz T, Nguyen T, Selsted M, Lehrer R . Mechanism of target cytolysis by peptide defensins. Target cell metabolic activities, possibly involving endocytosis, are crucial for expression of cytotoxicity. J Immunol. 1988; 140(8):2686-94. View

5.
Kajikawa N, Kaibuchi K, Matsubara T, Kikkawa U, Takai Y, NISHIZUKA Y . A possible role of protein kinase C in signal-induced lysosomal enzyme release. Biochem Biophys Res Commun. 1983; 116(2):743-50. DOI: 10.1016/0006-291x(83)90587-9. View