Glycolytic, pentose-phosphate shunt and transaminase enzymes in gastrocnemius muscle, liver, heart, and brain of two mouse mutants, 129 J-dy and A2g-adr, with abnormal muscle function.
Aldolase and phosphoglycerate kinase activity were markedly reduced in muscle from two mouse mutants, 129 J-dy and A2G-adr, with abnormal muscle development. The pentose-phosphate shunt enzymes, glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase, were both greatly increased in the gastrocnemius of 129 J-dy mice, but only the former was slightly increased in A2G-adr muscle. Alanine and aspartate aminotransferase activities were normal or low in 129 J-dy muscle but increased to approximately 200% in A2G-adr muscle. Liver from 129 J-dy mice showed increased activity of glucose-6-phosphate dehydrogenase. These findings are compatible with the well-recognised lipid involvement in the 129 J-dy mutant but indicate that an abnormality of amino acid metabolism in relation to energy supply is probably more important in the A2G-adr mutant.
D000818:Animals; D001921:Brain / Q000378:metabolism*; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism; D005954:Glucosephosphate Dehydrogenase / Q000378:metabolism; D006019:Glycolysis; D008099:Liver / Q000378:metabolism*; D051379:Mice; D008817:Mice, Mutant Strains; D009132:Muscles / Q000378:metabolism*; D009135:Muscular Diseases / Q000235:genetics / Q000378:metabolism*; D009206:Myocardium / Q000378:metabolism*; D009928:Organ Specificity; D010428:Pentosephosphates / Q000378:metabolism*; D010734:Phosphogluconate Dehydrogenase / Q000378:metabolism; D010735:Phosphoglycerate Kinase / Q000378:metabolism; D013045:Species Specificity; D000637:Transaminases / Q000378:metabolism*
D010428:Pentosephosphates; D010734:Phosphogluconate Dehydrogenase; D005954:Glucosephosphate Dehydrogenase; D000637:Transaminases; D010735:Phosphoglycerate Kinase; D005634:Fructose-Bisphosphate Aldolase