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Evidence for N ‐formyl chemotactic peptide‐stimulated GTPase activity in human neutrophil homogenates
Author(s) -
Hyslop Paul A.,
Oades Zenaida G.,
Jesaitis Algirdas J.,
Painter Richard G.,
Cochrane Charles G.,
Sklar Larry A.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80065-4
Subject(s) - gtpase , guanosine , biochemistry , guanine , adenylate kinase , stimulation , chemotaxis , formyl peptide receptor , gtp' , peptide , biology , chemistry , nucleotide , receptor , enzyme , endocrinology , gene
Neutropil homogenates contained a high affinity guanosine triphosphatase (GTPase) that was stimulatable (+ 27%) by the addition of 100 nM N ‐formyl chemotactic peptide (CHO‐pep), but not by 1 μg·ml −1 phorbolmyristate acetate (PMA). Kinetic analysis of the stimulation demonstrated an apparent lagtime of 14.3 ± 6.9 s between the addition of CHO‐pep and the optimal GTPase stimulation. The GTPase activity (but not CHO‐pep‐stimulated GTPase activity) was preserved in a highly purified plasma membrane fraction of the homogenate. From these observations we suggest that both a high affinity guanine nucleotide binding protein and GTPase are closely associated with the plasma membrane CHO‐pep receptor. The possibility that GTPase activity may influence guanine nucleotide regulation of adenylate cyclase during CHO‐pep stimulation of neutrophils is discussed.