Summary
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.
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Abbreviations
- EGTA:
-
ethylene glycol bis (β-aminoethyl ether)-N, N, N′, N′-tetraacetic acid
- Tris:
-
tris (hydroxymethyl) aminomethane
- MLCK:
-
myosin light chain kinase
- MLCK:
-
Ca2+-independent form of MLCK
- SDS:
-
sodium dodecyl sulfate
- Vus :
-
velocity unloaded shortening
- Fo :
-
isometric force
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Mrwa, U., Güth, K., Rüegg, J.C. et al. Mechanical and biochemical characterization of the contraction elicited by a calcium-independent myosin light chain kinase in chemically skinned smooth muscle. Experientia 41, 1002–1006 (1985). https://doi.org/10.1007/BF01952121
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DOI: https://doi.org/10.1007/BF01952121