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Thromb Haemost 1986; 56(03): 260-262
DOI: 10.1055/s-0038-1661662
Original Article
Schattauer GmbH Stuttgart

Interaction of Vasopressin with Human Blood Platelets: Dependency on Mg2+

Isabella Roos
The Department of Research, Kantonsspital Basel, Switzerland
,
Fabrizia Ferracin
The Department of Research, Kantonsspital Basel, Switzerland
,
Alfred Pletscher
The Department of Research, Kantonsspital Basel, Switzerland
› Author Affiliations
Further Information

Publication History

Received 12 March 1986

Accepted after revision 19 August 1986

Publication Date:
18 July 2018 (online)

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Summary

Arginine-vasopressin (AVP) in the presence of Mg2+ but not in the absence of bivalent cations led to accumulation of [32P]-phosphatidic acid ([32P]-PA) in human blood platelets. Mg2+ also enhanced the specific binding of [3H]-AVP to intact platelets. The concentrations of the cation which enabled AVP to cause half maximal rise of [32P]-PA and those inducing half maximal [3H]-AVP-binding were of the same order. It is concluded that the stimulation of phosphatidyl inositide breakdown by AVP in presence of Mg2+ is at least partially due to a Mg2+-induced enhancement of specific AVP-binding to the platelet membranes.

Key words

Blood platelets of man - Arginine-vasopressin - Phos-phoinositide turnover: dependence on Mg2+ - Magnesium ions - Vasopressin binding: dependence on Mg2+
 

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