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A significant decrease in major urinary protein (MUP) in adult male Bar Harbor 129REJ dystrophic mice correlated with a marked decrease in the amount of translatable MUPmRNA in the liver. Previous investigations have shown that MUP synthesis is under complex multihormonal regulation suggesting that the dystrophic mouse may have a hormonal deficiency.

The protein composition of normal spinal roots and the partially myelinated spinal roots of Bar Harbor 129 ReJ dystrophic mice was analyzed by 2D-gel electrophoresis which resolved basic proteins. The normal roots contained proteins with mobilities identical to two of the three 18.5 kDa and two of the three 14 kDa myelin basic protein spots resolved in purified spinal cord myelin suggesting that normal root myelin may have some of the characteristics of CNS myelin. In contrast dystrophic roots contained spots with mobilities identical to only one of the spots resolved for each myelin basic protein. The possibility that the difference in microheterogeneity may be responsible for the decreased myelination is discussed.

Proteins of lumbosacral spinal roots and sciatic nerves of adult dystrophic mice (Bar Harbor 129REJ dydy) were analyzed by SDS gel electrophoresis to determine if identifiable proteins were affected. All peripheral nerve myelin proteins (P0 glycoprotein, P1 and Pr basic proteins, X protein and a high-molecular-weight protein) were decreased in the roots but not in the sciatic nerves. Central nervous system myelin proteins were not increased in either roots or sciatic nerves. Although dystrophic spinal roots and sciatic nerves contained less collagen, Type I, III and V collagens were present.