Inhibition of calmodulin-dependent myosin light-chain kinase by growth-hormone-releasing factor and vasoactive intestinal peptide

In view of the ability of calmodulin to bind vasoactive intestinal peptide (VIP) and growth-hormone-releasing factor (GRF) with high affinity [Stallwood, Brugger, Baggenstoss, Stemmer, Shiraga, Landers and Paul (1992) J. Biol. Chem. 267, 19617-19621], the effects of these neuropeptides on a model ca...

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Bibliographic Details
Published in:Biochemical journal 1994-06, Vol.300 (3), p.901-905
Main Authors: SHIRAGA, H, STALLWOOD, D, EBADI, M, PFEIFFER, R, LANDERS, D, PAUL, S
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Calmodulin - physiology
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Growth Hormone-Releasing Hormone - pharmacology
Molecular Sequence Data
Myosin-Light-Chain Kinase - antagonists & inhibitors
Oligopeptides - chemistry
Oligopeptides - metabolism
Rats
Signal Transduction
Transferases
Vasoactive Intestinal Peptide - pharmacology
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Summary:In view of the ability of calmodulin to bind vasoactive intestinal peptide (VIP) and growth-hormone-releasing factor (GRF) with high affinity [Stallwood, Brugger, Baggenstoss, Stemmer, Shiraga, Landers and Paul (1992) J. Biol. Chem. 267, 19617-19621], the effects of these neuropeptides on a model calmodulin-dependent enzyme, myosin light-chain kinase (MLCK), were studied. Both peptides were potent inhibitors of MLCK activity. The inhibition of enzyme activity by VIP and GRF was progressively overcome with increasing calmodulin concentrations, with no inhibition observed at a saturating calmodulin concentration. Nanomolar concentrations of MLCK blocked the formation of calmodulin-[125I-Tyr10]VIP complexes. These data provide support for a functional role of VIP and GRF binding by calmodulin.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj3000901