Mechanical and biochemical characterization of the contraction elicited by a calcium-independent myosin light chain kinase in chemically skinned smooth muscle

Document Type

Article

Publication Date

1985

Abstract

The contraction induced by a Ca2+-independent myosin light chain kinase (MLCK-) was characterized in terms of isometric force (Fo), immediate elastic recoil (SE), unloaded shortening velocity (Vus), shortening under a constant load and ATPase activity of chemically skinned smooth muscle preparations. These parameters were compared to those measured in a Ca2+-induced contraction to assess the nature of cross bridge interaction in the MLCK-induced contraction. Fo developed in chicken gizzard fibers as well as SE were similar in contractions elicited by either agent. Vus in the contraction induced by MLCK-(0.36 mg/ml) was similar though averaged 39.3±8.9% less than Vus induced by Ca2+ (1.6x10-6M) in the control fibers. Addition of Ca2+ (1.6x10-6M) to a contraction induced by MLCK-resulted in small increases in both Fo and Vus. Shortening under a constant load was similar for both types of contractions. The contraction induced by MLCK-was accompanied by an increased rate of ATP hydrolysis. The MLCK-induced contraction is thus kinetically similar though not identical to a contraction induced by Ca2+. We conclude that with respect to actin-myosin interaction, MLCK- and Ca2+-induced contractions are similar.

Publication Title

Experientia

Volume

41

Issue

8

First Page

1002

Last Page

1006

Comments

This article was published in Experientia, Volume 41, Issue 8, Pages 1002-1006.

The published version is available at http://dx.doi.org/10.1007/BF01952121.

Copyright © 1985 Springer.

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