The effect of caldesmon on actin-myosin interaction in skeletal muscle fibers.
The effects of caldesmon on structural and dynamic properties of phalloidin-rhodamine-labeled F-actin in single skeletal muscle fibers were investigated by polarized microphotometry. The binding of caldesmon to F-actin in glycerinated fibers reduced the alterations of thin filaments structure and dynamics that occur upon the transition of the fibers from rigor to relaxing conditions. In fibers devoid of myosin and regulatory proteins (ghost fibers) the binding of caldesmon to F-actin precluded structural changes in actin filaments induced by skeletal muscle myosin subfragment 1 and smooth muscle tropomyosin. These results suggest that the restraint for the alteration of actin structure and dynamics upon binding of myosin heads and/or tropomyosin evoked by caldesmon can be related to its inhibitory effect on actin-myosin interaction.
Institute of Cytology of the Academy of Sciences of U.S.S.R., Leningrad.
B
B
Gałazkiewicz
Y S
YS
Borovikov
R
R
Dabrowska
D000199:Actins / Q000378:metabolism*; D000818:Animals; D002148:Calmodulin-Binding Proteins / Q000494:pharmacology*; D002645:Chickens; D005454:Fluorescence Polarization; D005895:Gizzard, Avian / Q000032:analysis; D009132:Muscles / Q000187:drug effects* / Q000201:enzymology; D009218:Myosins / Q000378:metabolism*; D011817:Rabbits
D000199:Actins; D002148:Calmodulin-Binding Proteins; D009218:Myosins