EVIDENCE AND NATURE OF A NOVEL THIOL-OXIDASE IN HUMAN PLATELETS

The study, addressed to understand whether or not human platelets poss ess a unique thiol-oxidase whose activity could be modulated by signal ling pathway initiated upon the activation of Receptor-'C'(k) revealed the existence of disulphide-dependent oxidation within these cells an d this phenomenon was regulated by Receptor-'C'(k)-dependent generatio n of second messengers especially phosphatidic acid (PA); cAMP and cGM P. Purification of this activity revealed the existence of 47 kDa prot ein having thiol-oxidase activity. Keeping in view these results we pr opose that the existence of this novel 47 kDa Thiol-oxidase within hum an platelets may provide a 'crucial switch' for the regulation of Rece ptor-'C'(k)-dependent mevalonate pathway in human platelets.