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Am J Physiol Cell Physiol 274: C1411-C1416, 1998;
0363-6143/98 $5.00
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Vol. 274, Issue 5, C1411-C1416, May 1998

Alterations in AMP deaminase activity and kinetics in skeletal muscle of creatine kinase-deficient mice

Peter C. Tullson1, James W. E. Rush1, Bé Wieringa2, and R. L. Terjung1

1 Department of Physiology, State University of New York, Health Science Center at Syracuse, Syracuse, New York 13210; and 2 Department of Cell Biology and Histology, University of Nijmegen, 6500 HB Nijmegen, The Netherlands

Alterations in the competency of the creatine kinase system elicit numerous structural and metabolic compensations, including changes in purine nucleotide metabolism. We evaluated molecular and kinetic changes in AMP deaminase from skeletal muscles of mice deficient in either cytosolic creatine kinase alone (M-CK-/-) or also deficient in mitochondrial creatine kinase (CK-/-) compared with wild type. We found that predominantly fast-twitch muscle, but not slow-twitch muscle, from both M-CK-/- and CK-/- mice had much lower AMP deaminase; the quantity of AMP deaminase detected by Western blot was correspondingly lower, whereas AMP deaminase-1 (AMPD1) gene expression was unchanged. Kinetic analysis of AMP deaminase from mixed muscle revealed negative cooperativity that was significantly greater in creatine kinase deficiencies. Treatment of AMP deaminase with acid phosphatase abolished negative cooperative behavior, indicating that a phosphorylation-dephosphorylation cycle may be important in the regulation of AMP deaminase.

muscle energetics; adenine nucleotides; inosine monophosphate; enzyme kinetics; enzyme phosphorylation


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