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Evidence and nature of a novel thiol-oxidase in human platelets

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Abstract

The study, addressed to understand whether or not human platelets possess a unique thiol-oxidase whose activity could be modulated by signalling pathway initiated upon the activation of Receptor-‘C’k revealed the existence of disulphide-dependent oxidation within these cells and this phenomenon was regulated by Receptor-‘C’k-dependent generation of second messengers especially phosphatidic acid (PA); cAMP and cGMP. Purification of this activity revealed the existence of 47 kDa protein having thiol-oxidase activity. Keeping in view these results we propose that the existence of this novel 47 kDa Thiol-oxidase within human platelets may provide a ‘crucial switch’ for the regulation of Receptor-‘C’k-dependent mevalonate pathway in human platelets.

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Authors and Affiliations

  1. Experimental Medicine and Biotechnology Department, Postgraduate Institute of Medical Education and Research, 160 012, Chandigarh, India

    D. Kaul, V. Dhawan & M. Kaur

Authors
  1. D. Kaul
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  2. V. Dhawan
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  3. M. Kaur
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Kaul, D., Dhawan, V. & Kaur, M. Evidence and nature of a novel thiol-oxidase in human platelets. Mol Cell Biochem 159, 81–84 (1996). https://doi.org/10.1007/BF00226066

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  • DOI: https://doi.org/10.1007/BF00226066

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