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J Biol Chem, Vol. 274, Issue 40, 28344-28350, October 1, 1999

Ca2+ Release and Heat Production by the Endoplasmic Reticulum Ca2+-ATPase of Blood Platelets
EFFECT OF THE PLATELET ACTIVATING FACTOR

Fernanda Mitidieri and Leopoldo de Meis

From the Instituto de Ciências Biomédicas, Departamento de Bioquímica Médica, Universidade Federal do Rio de Janeiro, Cidade Universitária, Rio de Janeiro 21941-590,-Brasil

Different sarco/endoplasmic reticulum Ca2+-ATPases isoforms are found in blood platelets and in skeletal muscle. The amount of heat produced during ATP hydrolysis by vesicles derived from the endoplasmic reticulum of blood platelets was the same in the absence and presence of a transmembrane Ca2+ gradient. Addition of platelets activating factor (PAF) to the medium promoted both a Ca2+ efflux that was arrested by thapsigargin and an increase of the yield of heat produced during ATP hydrolysis. The calorimetric enthalpy of ATP hydrolysis (Delta Hcal) measured during Ca2+ transport varied between -10 and -12 kcal/mol without PAF and between -20 and -24 kcal/mol with 4 µM PAF. Different from platelets, in skeletal muscle vesicles a thapsigargin-sensitive Ca2+ efflux and a high heat production during ATP hydrolysis were measured without PAF and the Delta Hcal varied between -10 and -12 kcal/mol in the absence of Ca2+ and between -22 up to -32 kcal/mol after formation of a transmembrane Ca2+ gradient. PAF did not enhance the rate of thapsigargin-sensitive Ca2+ efflux nor increase the yield of heat produced during ATP hydrolysis. These findings indicate that the platelets of Ca2+-ATPase isoforms are only able to convert osmotic energy into heat in the presence of PAF.


Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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