AJP - Cell Physiology, Vol 249, Issue 5 464-C470, Copyright © 1985 by American Physiological Society

ARTICLES

Skeletal muscle protein synthesis and degradation in vitro: effects of temperature

D. A. Essig, S. S. Segal and T. P. White

We compared the structure, function, protein synthesis, and degradation of 70- to 95-mg rat soleus muscles during 120 min of incubation at 20 and 37 degrees C. At 37 degrees C, muscles were characterized by a damaged central core region and a decline of isometric tension development during incubation. Protein synthesis in the core region at 37 degrees C was depressed relative to the peripheral region. At 20 degrees C, developed tension remained constant during incubation, and synthesis rates in the core region were not different from the peripheral region. Compared with fresh muscle, ATP concentration after incubation was not affected by temperature. After equilibration of phenylalanine specific activity between extracellular and intracellular spaces (60 min at 20 degrees C; 30 min at 37 degrees C), rates of protein synthesis at 20 [0.048 nmol tyrosine (Tyr) X mg wet mass-1 X 2 h-1] and 37 degrees C (0.160 nmol Tyr X mg wet mass-1 X 2 h-1) were linear up to 180 and 120 min, respectively. Rates of protein degradation at 20 (0.076 nmol Tyr X mg wet mass-1 X 2 h-1) and 37 degrees C (0.248 nmol Tyr X mg wet mass-1 X 2 h-1) measured after 60 min were linear up to 180 and 120 min, respectively. Incubation at 20 degrees C offers an approach to study 70- to 95-mg muscles in vitro without compromising structure and function.