title: The effects of temperature on relaxation in frog skeletal muscle: the role of parvalbumin.
abstract: Isolated muscle fibers from Rana temporaria tibialis anterior muscles were microinjected with aequorin. The force responses and the Ca2+ transients associated with twitch and tetanic contractions were studied at several temperatures. The declines of the Ca2+ transients were well described by single exponential equations and the effects of temperature were complex (multi-exponential). To determine if these temperature effects on the Ca2+ transients were influenced by the Ca2+ indicator itself, samples of the injected aequorin were studied in vitro using a Gibson stopped-flow apparatus. The quenching of aequorin luminescence with either EGTA or de-calcified Rana temporaria parvalbumin were mono-exponential. These overall quenching reactions had single exponential temperature dependencies. The effects of temperature on the declines of the single fiber Ca2+ transients did not appear to be influenced by the kinetics of the aequorin reaction. The disparity in the effects of temperature on the single fiber Ca2+ transients versus the in vitro quenching of aequorin luminescence with parvalbumin, were interpreted to indicate that in twitch and tetanic contractions of these fibers, it was unlikely that soluble Ca2+ binding proteins played a major role in the regulation of myoplasmic Ca2+.
authors.affiliation: Department of Pharmacology, Mayo Foundation, Rochester, MN 55905.
authors.forename: P A
authors.initials: PA
authors.lastname: Iaizzo
mesh_terms: D000818:Animals; D002118:Calcium / Q000378:metabolism; D009119:Muscle Contraction; D009124:Muscle Proteins / Q000502:physiology*; D009126:Muscle Relaxation; D009132:Muscles / Q000502:physiology; D010320:Parvalbumins / Q000502:physiology*; D011896:Rana temporaria; D013696:Temperature; D013977:Tibia / Q000033:anatomy & histology
chemical_list: D009124:Muscle Proteins; D010320:Parvalbumins; D002118:Calcium