Decrease in myosin light chain kinase activity of rabbit fast muscle by chronic stimulation

G. A. Klug; M. E. Houston; J. T. Stullo; D. Pette

doi:10.1016/0014-5793(86)81167-X

Decrease in myosin light chain kinase activity of rabbit fast muscle by chronic stimulation

G. A. Klug, M. E. Houston, J. T. Stullo, D. Pette

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

Abstract

Analysis of myosin light chain kinase (MLCK) activity in tibialis anterior muscles of the rabbit revealed that chronic stimulation at a frequency of 10 Hz for 24 h per day reduced the enzyme activity in a timedependent manner. Since fast twitch muscle contains significantly more myosin light chain kinase than slow twitch muscle, the observed reductions are consistent with the type of fast-to-slow transformation observed for other type-specific muscle characteristics. The present data also indicate that the stimulation-induced decrease in MLCK activity precedes the fast-to-slow conversion of the myosin molecule as judged by pyrophosphate-polyacrylamide gel electrophoresis.

Original language	English (US)
Pages (from-to)	352-354
Number of pages	3
Journal	FEBS Letters
Volume	200
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(86)81167-X
State	Published - May 12 1986

Keywords

(Skeletal muscle)
Chronic stimulation
Fast-to-slow conversion
Isomyosin
Myosin light chain kinase

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Access to Document

10.1016/0014-5793(86)81167-X

Cite this

@article{af26999b33ea4099bf48fe7d93115993,

title = "Decrease in myosin light chain kinase activity of rabbit fast muscle by chronic stimulation",

abstract = "Analysis of myosin light chain kinase (MLCK) activity in tibialis anterior muscles of the rabbit revealed that chronic stimulation at a frequency of 10 Hz for 24 h per day reduced the enzyme activity in a timedependent manner. Since fast twitch muscle contains significantly more myosin light chain kinase than slow twitch muscle, the observed reductions are consistent with the type of fast-to-slow transformation observed for other type-specific muscle characteristics. The present data also indicate that the stimulation-induced decrease in MLCK activity precedes the fast-to-slow conversion of the myosin molecule as judged by pyrophosphate-polyacrylamide gel electrophoresis.",

keywords = "(Skeletal muscle), Chronic stimulation, Fast-to-slow conversion, Isomyosin, Myosin light chain kinase",

author = "Klug, {G. A.} and Houston, {M. E.} and Stullo, {J. T.} and D. Pette",

note = "Funding Information: This study was supported by the Deutsche Forschungsgemeinschaft, Sonderforschungsbe-reich 156a nd by a stipendf rom the Alexanderv on Humboldt-Stiftung (G.A.K.). The authors gratefully acknowledge the excellent technical assistanceo f MS Elmi Leisner.",

year = "1986",

month = may,

day = "12",

doi = "10.1016/0014-5793(86)81167-X",

language = "English (US)",

volume = "200",

pages = "352--354",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "2",

}

TY - JOUR

T1 - Decrease in myosin light chain kinase activity of rabbit fast muscle by chronic stimulation

AU - Klug, G. A.

AU - Houston, M. E.

AU - Stullo, J. T.

AU - Pette, D.

N1 - Funding Information: This study was supported by the Deutsche Forschungsgemeinschaft, Sonderforschungsbe-reich 156a nd by a stipendf rom the Alexanderv on Humboldt-Stiftung (G.A.K.). The authors gratefully acknowledge the excellent technical assistanceo f MS Elmi Leisner.

PY - 1986/5/12

Y1 - 1986/5/12

N2 - Analysis of myosin light chain kinase (MLCK) activity in tibialis anterior muscles of the rabbit revealed that chronic stimulation at a frequency of 10 Hz for 24 h per day reduced the enzyme activity in a timedependent manner. Since fast twitch muscle contains significantly more myosin light chain kinase than slow twitch muscle, the observed reductions are consistent with the type of fast-to-slow transformation observed for other type-specific muscle characteristics. The present data also indicate that the stimulation-induced decrease in MLCK activity precedes the fast-to-slow conversion of the myosin molecule as judged by pyrophosphate-polyacrylamide gel electrophoresis.

AB - Analysis of myosin light chain kinase (MLCK) activity in tibialis anterior muscles of the rabbit revealed that chronic stimulation at a frequency of 10 Hz for 24 h per day reduced the enzyme activity in a timedependent manner. Since fast twitch muscle contains significantly more myosin light chain kinase than slow twitch muscle, the observed reductions are consistent with the type of fast-to-slow transformation observed for other type-specific muscle characteristics. The present data also indicate that the stimulation-induced decrease in MLCK activity precedes the fast-to-slow conversion of the myosin molecule as judged by pyrophosphate-polyacrylamide gel electrophoresis.

KW - (Skeletal muscle)

KW - Chronic stimulation

KW - Fast-to-slow conversion

KW - Isomyosin

KW - Myosin light chain kinase

UR - http://www.scopus.com/inward/record.url?scp=0022506895&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0022506895&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(86)81167-X

DO - 10.1016/0014-5793(86)81167-X

M3 - Article

C2 - 3754822

AN - SCOPUS:0022506895

SN - 0014-5793

VL - 200

SP - 352

EP - 354

JO - FEBS Letters

JF - FEBS Letters

IS - 2

ER -

Decrease in myosin light chain kinase activity of rabbit fast muscle by chronic stimulation

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this