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

H. Shiraga, D. Stallwood, M. Ebadi, Ronald Pfeiffer, D. Landers, S. Paul

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

In view of the ability of calmodulin to bind vasoactive intestinal peptide (VIP) and growth-hormone-releasing factor (GRF) with high affinity, 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.

Original languageEnglish (US)
Pages (from-to)901-905
Number of pages5
JournalBiochemical Journal
Volume300
Issue number3
StatePublished - 1994
Externally publishedYes

Fingerprint

Myosin-Light-Chain Kinase
Growth Hormone-Releasing Hormone
Vasoactive Intestinal Peptide
Calmodulin
Gastrointestinal Hormones
Peptide Hormones
Enzyme inhibition
Enzyme activity
Enzymes
Neuropeptides
Peptides

ASJC Scopus subject areas

  • Biochemistry

Cite this

Inhibition of calmodulin-dependent myosin light chain kinase by growth-hormone-releasing factor and vasoactive intestinal peptide. / Shiraga, H.; Stallwood, D.; Ebadi, M.; Pfeiffer, Ronald; Landers, D.; Paul, S.

In: Biochemical Journal, Vol. 300, No. 3, 1994, p. 901-905.

Research output: Contribution to journalArticle

@article{028a1ba13cf14c2887d91a00960a2d5c,
title = "Inhibition of calmodulin-dependent myosin light chain kinase by growth-hormone-releasing factor and vasoactive intestinal peptide",
abstract = "In view of the ability of calmodulin to bind vasoactive intestinal peptide (VIP) and growth-hormone-releasing factor (GRF) with high affinity, 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.",
author = "H. Shiraga and D. Stallwood and M. Ebadi and Ronald Pfeiffer and D. Landers and S. Paul",
year = "1994",
language = "English (US)",
volume = "300",
pages = "901--905",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "3",

}

TY - JOUR

T1 - Inhibition of calmodulin-dependent myosin light chain kinase by growth-hormone-releasing factor and vasoactive intestinal peptide

AU - Shiraga, H.

AU - Stallwood, D.

AU - Ebadi, M.

AU - Pfeiffer, Ronald

AU - Landers, D.

AU - Paul, S.

PY - 1994

Y1 - 1994

N2 - In view of the ability of calmodulin to bind vasoactive intestinal peptide (VIP) and growth-hormone-releasing factor (GRF) with high affinity, 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.

AB - In view of the ability of calmodulin to bind vasoactive intestinal peptide (VIP) and growth-hormone-releasing factor (GRF) with high affinity, 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.

UR - http://www.scopus.com/inward/record.url?scp=0028335014&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028335014&partnerID=8YFLogxK

M3 - Article

VL - 300

SP - 901

EP - 905

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 3

ER -