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Decreased expression of phospholipase C-beta 2 isozyme in human platelets
with impaired function
SB Lee, AK Rao, KH Lee, X Yang, YS Bae and SG Rhee
Laboratory of Cell Signaling, National Heart, Lung and Blood Institute,
National Institutes of Health, Bethesda, MD 20892-0340, USA.
Platelets from a patient with a mild inherited bleeding disorder and
abnormal platelet aggregation and secretion show reduced generation of
inositol 1,4,5-trisphosphate, mobilization of intracellular Ca2+, and
phosphorylation of pleckstrin in response to several G protein mediated
agonists, suggesting a possible defect at the level of phospholipase C
(PLC) activation (see accompanying report). A procedure was developed that
allows quantitation of platelet PLC isozymes. After fractionation of
platelet extracts by high-performance liquid chromatography, 7 out of 10
known PLC isoforms were detected by immunoblot analysis. The amount of
these isoforms in normal platelets decreased in the order PLC- gamma 2 >
PLC-beta 2 > PLC-beta 3 > PLC-beta 1 > PLC-gamma 1 > PLC- delta
1 > PLC-beta 4. Compared with normal platelets, platelets from the
patient contained approximately one-third the amount of PLC-beta 2, whereas
PLC-beta 4 was increased threefold. These results suggest that the impaired
platelet function in the patient in response to multiple G protein mediated
agonists is attributable to a deficiency of PLC-beta 2. They document for
the first time a specific PLC isozyme deficiency in human platelets and
provide an unique opportunity to understand the role of different PLC
isozymes in normal platelet function.
Volume 88,
Issue 5,
pp. 1684-1691,
09/01/1996
Copyright © 1996 by The American Society of Hematology
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