Impairment of IGF-I gene splicing and MGF expression associated with muscle wasting.
An aminopeptidase was purified from bovine skeletal muscle by ammonium sulfate fractionation and by successive chromatographies of DEAE-cellulose, Sehacryl S-200, phenyl-sepharose CL-4B, hydroxyapatite and Hi-Trap chelating HP columns. The aminopeptidase was purified about 14-fold over the crude extract with a yield of 1.0% activity. The molecular mass of the enzyme was found to be 58 kDa on SDS-PAGE. The enzyme activity was enhanced by the addition of some anions, such as Cl(-), NO(3)(-) and SCN(-), which is the most unique property of this enzyme. While, the activity was strongly inhibited by bestatin, PMSF and puromycin, suggesting that it was a serine protease. In addition, this enzyme was identical with leukotriene (LT) A4 hydrolase, converting LTA4 to LTB4.
Goldspink
Geoffrey
G
Department of Surgery, Royal Free and University College Medical School, Royal Free Campus, Rowland Hill Street, London NW3 2PF, UK. ggoldspi@medsch.ucl.ac.uk
D000375:Aging; D000818:Animals; D004274:DNA, Recombinant / Q000235:genetics / Q000378:metabolism*; D005081:Exercise Therapy; D013006:Growth Hormone / Q000378:metabolism / Q000494:pharmacology; D006801:Humans; D007334:Insulin-Like Growth Factor I / Q000235:genetics* / Q000378:metabolism; D040542:Mechanotransduction, Cellular; D009133:Muscular Atrophy / Q000235:genetics / Q000378:metabolism*; D020033:Protein Isoforms / Q000235:genetics* / Q000378:metabolism; D051381:Rats; D032496:Satellite Cells, Skeletal Muscle
D004274:DNA, Recombinant; D020033:Protein Isoforms; D007334:Insulin-Like Growth Factor I; D013006:Growth Hormone