Impairment of IGF-I gene splicing and MGF expression associated with muscle wasting.
INT J BIOCHEM CELL B
2012 - 2022.
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-, NO3- 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. (c) 2005 Published by Elsevier Ltd.
|Title:||Impairment of IGF-I gene splicing and MGF expression associated with muscle wasting|
|Keywords:||MGF, IGF-I, muscle cachexia, satellite cells, sarcopenia, CONTRACTION-INDUCED INJURY, AGE-ASSOCIATED CHANGES, HUMAN SKELETAL-MUSCLE, RESISTANCE EXERCISE, SATELLITE CELL, GROWTH-HORMONE, MYOSTATIN GENE, TRANSGENIC MDX, STEM-CELLS, MICE|
|UCL classification:||UCL > School of Life and Medical Sciences
UCL > School of Life and Medical Sciences > Faculty of Medical Sciences
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