Phosphorylation-contraction coupling in smooth muscle: role of caldesmon.
In intact smooth muscle strips from chicken gizzard, carbachol elicited brief, phasic contractions which were associated with a very rapid, transient phosphorylation of the 20 kDa myosin light chains. Phosphorylation was not significantly different from basal levels after 30 s while force still amounted to 50% of the peak value. The rate of tension decline could be increased by addition of atropine, even at apparently basal phosphorylation levels suggesting a phosphorylation independent regulation. The force, at a given level of phosphorylation, could also be modulated by addition of the actin binding, putative regulatory protein, caldesmon. Caldesmon, inhibits phosphorylation dependent force in skinned fiber bundles of chicken gizzard without affecting myosin light chain phosphorylation. This suggests that caldesmon might modulate contraction in smooth muscle. Moreover our results suggest that caldesmon does not function to maintain passive tension.
Pfitzer
G
G
II. Physiologisches Institut Universität Heidelberg, Germany.
Fischer
W
W
Chalovich
J M
JM
D000818:Animals; D002148:Calmodulin-Binding Proteins / Q000378:metabolism / Q000502:physiology*; D002217:Carbachol / Q000494:pharmacology; D002645:Chickens; D005895:Gizzard, Avian / Q000201:enzymology / Q000378:metabolism / Q000502:physiology; D009119:Muscle Contraction / Q000187:drug effects / Q000502:physiology; D009126:Muscle Relaxation / Q000502:physiology; D009130:Muscle, Smooth / Q000201:enzymology / Q000378:metabolism / Q000502:physiology*; D009219:Myosin-Light-Chain Kinase / Q000378:metabolism; D010766:Phosphorylation
D002148:Calmodulin-Binding Proteins; D002217:Carbachol; D009219:Myosin-Light-Chain Kinase