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Regulation of isometric force and isotonic shortening velocity by phosphorylation of 20000 dalton myosin light chain of rat uterine smooth muscle

, : Regulation of isometric force and isotonic shortening velocity by phosphorylation of 20000 dalton myosin light chain of rat uterine smooth muscle. Pfluegers Archiv European Journal of Physiology 403(2): 215-219

The regulation of isometric force maintenance and isotonic shortening velocity by phosphorylation of the 20,000 dalton L chain of myosin was examined for K-depolarized rat uterine smooth muscle. Following a transient peak in myosin L chain (LC20) phosphorylation at 20 s of contraction (0.46 mol PO4/mol LC20), phosphorylation declined to a steady-state by 2 min (0.28 mol PO4/mol LC20) with no significant change from 2-90 min of contraction. Isometric force developed more slowly, reaching a maximum at 2 min with no further change out to 90 min. Lightly-loaded (0.1 F0) shortening velocity like LC20 phosphorylation, increased initially to a peak of 0.034 L0/s at 20 s of contraction and then declined to 0.023 L0/s by 2 min. Unlike LC20 phosphorylation and isometric force, shortening velocity decreased .apprx. 4-fold from 0.023 L0/s at 2 min to 0.006 L0/s at 90 min of contraction. Graded activation with reduced extracellular Ca was associated with proportional changes in steady-state isometric force and LC20 phosphorylation. Shortening velocity was also decreased with reduced Ca, however, unlike LC20 phosphorylation the greatest changes in velocity occurred at low levels of developed force. In contrast to the large reductions in shortening velocity observed during 90 min contractions where force and LC20 phosphorylation were unchanged, similar reductions in shortening velocity did not occur with graded activation in spite of significant (> 3-fold) decreases in both force and LC20 phosphorylation. Factors other than L chain phosphorylation are involved in the regulation of isotonic shortening velocity during extended isometric contractions of uterine smooth muscle.

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