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Blood, Vol. 95 No. 11 (June 1), 2000:
pp. 3412-3422
Distinct localization and function of
1,4,5IP3 receptor subtypes and the
1,3,4,5IP4 receptor GAP1IP4BP in
highly purified human platelet membranes
Samer S. El-Daher,
Yatin Patel,
Ashia Siddiqua,
Sheila Hassock,
Scott Edmunds,
Benjamin Maddison,
Geeta Patel,
David Goulding,
Florea Lupu,
Richard J. H. Wojcikiewicz, and
Kalwant S. Authi
From the Platelet Section, Thrombosis Research Institute, London,
UK, and the Department of Pharmacology, State University of New York
Health Science Center, Syracuse, NY.
Platelet activation is associated with an increase of cytosolic
Ca++ levels. The 1,4,5IP3
receptors [1,4,5IP3R] are known to mediate
Ca++ release from intracellular stores of many cell
types. Currently there are at least 3 distinct subtypes of
1,4,5IP3R type I, type II, and type IIIwith
suggestions of distinct roles in Ca++ elevation.
Specific receptors for 1,3,4,5IP4 belonging to
the GAP1 family have also been described though their involvement with
Ca++ regulation is controversial. In this study we
report that platelets contain all 3 subtypes of
1,4,5IP3R but in different amounts. Type I and
type II receptors are predominant. In studies using highly purified
platelet plasma (PM) and intracellular membranes (IM) we report a
distinct localization of these receptors. The PM fractions were found
to contain the type III 1,4,5IP3R and
GAP1IP4BP in contrast to IM, which contained type I
1,4,5IP3R. The type II receptor exhibited a
dual distribution. In studies examining the labeling of surface
proteins with biotin in intact platelets only the type III
1,4,5IP3R was significantly labeled. Immunogold
studies of ultracryosections of human platelets showed significantly
more labeling of the PM with the type III receptor antibodies than with
type I receptor antibodies. Ca++ flux studies were
carried out with the PM to demonstrate in vitro function of inositol
phosphate receptors. Ca++ release activities were
present with both 1,4,5IP3 and
1,3,4,5IP4 (EC50 = 1.3 and 0.8 µmol/L, respectively). Discrimination of the
Ca++-releasing activities was demonstrated with cyclic
adenosine monophosphate (cAMP)-dependent protein kinase (cAMP-PK)
specifically inhibiting 1,4,5IP3 but not
1,3,4,5IP4-induced Ca++ flux.
In experiments with both PM and intact platelets, the
1,4,5IP3Rs but not GAP1IP4BP were
found to be substrates of cAMP-PK and cGMP-PK. Thus the Ca++ flux property of
1,3,4,5IP4 is insensitive to cAMP-PK. These
studies suggest distinct roles for the
1,4,5IP3R subtypes in Ca++
movements, with the type III receptor and GAP1IP4BP
associated with cation entry in human platelets and the type I receptor
involved with Ca++ release from intracellular stores.
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