Record Details

Phosphatidyl Inosito Inhibition Of a Sperm Cyclic Amp-Independent Protein Kinase

EPrints@IICB

View Archive Info
 
 
Field Value
 
Title Phosphatidyl Inosito Inhibition Of a Sperm
Cyclic Amp-Independent Protein Kinase
 
Creator Dey, Chinmoy S.
Majumder, Gopal Chandra
 
Subject Cell Biology & Physiology
 
Description Phosphatidyl inositol has been found to inhibit strongly the activity of
a cyclic AMP-independent protein kinase located on the external surface of goat epididymal
intact spermatozoa. Phosphatidyl inositol at a concentration as low ai 10 &/ml
inhibited nearly 50% of the ecto-kinase activity for the phosphorylation of the exogenous
protein substrate: casein. Phosphatidyl ethanolamine at a relatively high concentration
(125 &ml) inhibited slightly (approx 25%) the activity of the enzyme whereas other
phospholipids: phosphatidyl serine and choline, diacyl glycerol, phosphatidic acid and
myo-inositol-2-phosphate had no appreicable effect on the kinase activity. Phosphatidyl
inositol has also served as a potent inhibitor of the phosphorylation of sperm ectophosphoproteins
by the endogenous kinase activity of intact spermatozoa. By thin
layer chromatography it has been shown that the observed inhibitory effect of the
phospholipid was not due to any impurities or degraded products of phosphatidyl inositol.
Phosphatidyl iy$tol inhibited the kinase activity noncompetitively with respect to
casein and Mg but uncompetitively with respect to ATP. The results raised the
possibility that phosphatidyl inositol-mediated high affinity inhibition of protein kinase(s),
may constitute a novel mechanism for the regulatory actions of the phospholipid in mammalian cells.
 
Publisher Elsevier
 
Date 1987
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://www.eprints.iicb.res.in/1423/1/BIOCHEMICAL_AND_BIOPHYSICAL_RESEARCH_COMMUNICATIONS__146(_2);_1987[29].pdf
Dey, Chinmoy S. and Majumder, Gopal Chandra (1987) Phosphatidyl Inosito Inhibition Of a Sperm Cyclic Amp-Independent Protein Kinase. Biochemical and Biophysical Research Communications, 146 (2). pp. 422-429.
 
Relation http://dx.doi.org/10.1016/0006-291X(87)90546-8
http://www.eprints.iicb.res.in/1423/