Exercising mammals synthesize stress proteins

Am J Physiol. 1990 Apr;258(4 Pt 1):C723-9. doi: 10.1152/ajpcell.1990.258.4.C723.

Abstract

Spleen cells, peripheral lymphocytes, and soleus muscles were removed from male Sprague-Dawley rats that had been run on a treadmill (24 m/min) for either 20, 40, or 60 min or to exhaustion (86 +/- 41 min) and were labeled in vitro with [35S]methionine at 37 degrees C. Similar tissues from nonrunning control rats were labeled in vitro at either 37 or 43 degrees C (heat shock). Fluorographic analyses of one- and two-dimensional polyacrylamide gel electrophoretic separations of the proteins from cells and tissues of exercised rats demonstrate the new or enhanced synthesis of proteins of approximately 65, 72, 90, and 100 kDa. Although synthesis of these proteins is low or not detectable in tissues from control rats labeled at 37 degrees C, they are prominent products of similar tissues labeled under heat-shock conditions (43 degrees C) and, in fact, correspond in Mr and pI with the so-called heat-shock proteins. These results suggest that exercise is a sufficient stimulus to induce or enhance the synthesis of heat shock and/or stress proteins in mammalian cells and tissues.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Body Temperature
  • Electrophoresis, Gel, Two-Dimensional
  • Glycogen / metabolism
  • Heat-Shock Proteins / biosynthesis*
  • Heat-Shock Proteins / isolation & purification
  • Liver Glycogen / metabolism
  • Male
  • Methionine / metabolism
  • Muscles / metabolism
  • Physical Exertion*
  • Radioisotope Dilution Technique
  • Rats
  • Rats, Inbred Strains
  • Spleen / metabolism
  • Sulfur Radioisotopes
  • Time Factors

Substances

  • Heat-Shock Proteins
  • Liver Glycogen
  • Sulfur Radioisotopes
  • Glycogen
  • Methionine