Temperature dependence of the inhibitory effects of orthovanadate on shortening velocity in fast skeletal muscle.
We have investigated the effects of the orthophosphate (P(i)) analog orthovanadate (Vi) on maximum shortening velocity (Vmax) in activated, chemically skinned, vertebrate skeletal muscle fibers. Using new "temperature-jump" protocols, reproducible data can be obtained from activated fibers at high temperatures, and we have examined the effect of increased [Vi] on Vmax for temperatures in the range 5-30 degrees C. We find that for temperatures < or = 20 degrees C, increasing [Vi] inhibits Vmax; for temperatures > or = 25 degrees C, increasing [Vi] does not inhibit Vmax. Attached cross-bridges bound to Vi are thought to be an analog of the weakly bound actin-myosin.ADP-P(i) state. The data suggest that the weakly bound Vi state can inhibit velocity at low temperature, but not at high temperature, with the transition occurring over a narrow temperature range of < 5 degrees C. This suggests a highly cooperative interaction. The data also define a Q10 for Vmax of 2.1 for chemically skinned rabbit psoas fibers over the temperature range of 5-30 degrees C.
Pate
E
E
Department of Pure and Applied Mathematics, Washington State University, Pullman 99164.
Wilson
G J
GJ
Bhimani
M
M
Cooke
R
R
D000199:Actins / Q000737:chemistry / Q000502:physiology; D000818:Animals; D001696:Biomechanical Phenomena; D055592:Biophysical Phenomena; D001703:Biophysics; D006358:Hot Temperature; D066298:In Vitro Techniques; D007551:Isotonic Contraction / Q000187:drug effects / Q000502:physiology; D007700:Kinetics; D015394:Molecular Structure; D009119:Muscle Contraction / Q000187:drug effects* / Q000502:physiology; D009218:Myosins / Q000737:chemistry / Q000502:physiology; D011817:Rabbits; D013696:Temperature; D014638:Vanadates / Q000494:pharmacology*
D000199:Actins; D014638:Vanadates; D009218:Myosins