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Identification of the pertussis toxin-sensitive G proteins in platelets,
megakaryocytes, and human erythroleukemia cells
AG Williams, MJ Woolkalis, M Poncz, DR Manning, AM Gewirtz and LF Brass
Department of Medicine, University of Pennsylvania, Philadelphia 19104.
Guanine nucleotide-binding regulatory proteins, or G proteins, mediate the
interaction of agonist receptors on the platelet surface with phospholipase
C and adenylyl cyclase. To better understand this process, we have used
several approaches to identify which G proteins are present in platelets,
normal human megakaryocytes, and human erythroleukemia (HEL) cells, a
leukemic cell line with megakaryocytic features. Because platelet and HEL
cell responses to thrombin are inhibited by pertussis toxin, we have
focused upon the members of the Gi family, whose alpha subunits can be
ADP-ribosylated by that toxin. Western blots with antisera specific for Gi
alpha demonstrated the presence in both platelets and HEL cells of the
three best-described forms of this protein: Gi alpha 1, Gi alpha 2, and Gi
alpha 3. Based upon immunoprecipitation studies with
[35S]-methionine-labeled HEL cells, their relative abundance appears to be
Gi alpha 2 much greater than Gi alpha 3 greater than Gi alpha 1. A HEL cell
cDNA library screened with the Gi alpha antisera produced clones encoding
Gi alpha 2 and Gi alpha 3 that had sequences similar to those reported from
other sources. Gi alpha-specific probes created from these cDNA clones
confirmed the presence of mRNA encoding Gi alpha 2 and Gi alpha 3 in both
platelets (by Northern blotting) and megakaryocytes (by in situ
hybridization). Thus the pertussis toxin substrates that have previously
been detected in platelets and HEL cells are shown to be members of the Gi
alpha family, all of which are candidates for interaction with receptors
for thrombin and other agonists.
Volume 76,
Issue 4,
pp. 721-730,
08/15/1990
Copyright © 1990 by The American Society of Hematology
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