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Inhibition of platelet aggregation by S ‐nitroso‐cysteine via cGMP‐independent mechanisms: evidence of inhibition of thromboxane A 2 synthesis in human blood platelets
Author(s) -
Tsikas Dimitrios,
Ikic Milos,
Tewes Kathrin S.,
Raida Manfred,
Frölich Jürgen C.
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01633-0
Subject(s) - platelet , cysteine , thromboxane a2 , chemistry , thromboxane , platelet aggregation , biochemistry , human blood , medicine , biology , enzyme , physiology
S ‐Nitroso‐cysteine (SNC), a putative endothelium‐derived relaxing factor, potently inhibited collagen‐ and arachidonic acid‐induced platelet aggregation (IC 50 =100 nM) and thromboxane A 2 (TxA 2 ) synthesis of human blood platelets. ODQ, a selective inhibitor of the soluble guanylyl cyclase, inhibited SNC‐induced formation of cGMP but did not reverse inhibition by SNC of collagen‐ and arachidonic acid‐induced platelet aggregation. Combination of ODQ with SQ‐29548, a specific platelet TxA 2 receptor antagonist, did not modify the antiaggregatory action of SNC. Our study shows that SNC inhibits platelet aggregation by cGMP‐independent mechanisms that may involve inhibition of TxA 2 synthesis in human platelets.