Altered allosteric properties of cytoskeleton-bound phosphofructokinase in muscle from mice with X chromosome-linked muscular dystrophy (mdx).

Intracellular distribution of cytoskeleton-bound and soluble phosphofructokinase (PFK) (the rate-limiting enzyme in glycolysis) in mdx dystrophic muscle was the same as in control nondystrophic muscle. However, the allosteric activity of both bound and soluble PFK was reduced in mdx muscle, accompanied by a decrease in ATP level. In contrast to normal muscle, the cytoskeleton-bound PFK in mdx muscle was sensitive to allosteric regulation, like the soluble enzyme. This change in the properties of cytoskeletal PFK in mdx mice may result from the absence of dystrophin, believed to reside in the cytoskeleton. The findings that cytoskeletal PFK in mdx muscle, although altered, remains bound to cytoskeleton may play a role in muscle structure and function and the mild clinical symptoms in mdx mice.