The modulation of the calcium transport by skeletal muscle sarcoplasmic reticulum in the hibernating European hamster.
Calcium transport of skeletal muscle sarcoplasmic reticulum was comparatively studied in hibernating and summer active European hamsters (Cricetus cricetus L.). Crude homogenates from psoas, soleus and mixed skeletal muscles were used. Protein yield was strongly reduced in the muscle homogenates of hibernating hamsters. The calcium concentration in the muscle of hibernating hamsters was increased to a much higher content than in the serum. In the same animals the maximal rate of calcium uptake and the calcium storing capacity of sarcoplasmic reticulum were augmented by 43% and respectively 17%. Kinetic experiments with various concentrations of free calcium revealed in the hibernating animals higher uptake rates and a lower apparent calcium affinity than in the summer active hamsters. Some shift of calcium uptake rate and calcium affinity similar to that of a fast-twitch muscle was also observed in winter active animals kept at 22 degrees C under natural photoperiod. By contrast, the activity of the calcium dependent ATPase was not increased, suggesting a tighter coupling during hibernation between calcium dependent ATP-hydrolysis and calcium transport. No seasonal difference was observed in the calcium release by KCl-caffeine from calcium loaded vesicles of sarcoplasmic reticulum. Proportion and size of fibre types were studied with cold cross sections from psoas and soleus muscles. An average atrophy of about 25% was found during hibernation in both muscles. Cytochemistry revealed, however, a different reduction of cross area between type-I- and type-II-fibres, which reaches values up to 46% in the type-II-fast-fibres of the slow soleus muscle. Electron microscopy did not show any definite change in the distribution and amount of sarcoplasmic reticulum. The results suggest that during hibernation a modulation in the properties of calcium transport ATPase of sarcoplasmic reticulum occurs to better support the calcium transport function at low temperatures, which in turn warrants the restoration of ion homeostasis in the course of the arousal.
Agostini
B
B
Max-Planck-Institut für Medizinische Forschung, Heidelberg, Bundesrepublik Deutschland.
De Martino
L
L
Soltau
B
B
Hasselbach
W
W
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001143:Arousal; D002118:Calcium / Q000378:metabolism*; D006224:Cricetinae / Q000502:physiology*; D006605:Hibernation; D007700:Kinetics; D008297:Male; D009132:Muscles / Q000166:cytology / Q000378:metabolism* / Q000648:ultrastructure; D009928:Organ Specificity; D012519:Sarcoplasmic Reticulum / Q000378:metabolism* / Q000648:ultrastructure
D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D002118:Calcium