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The degradation of human myelin basic protein peptide 43–88 by human renal neutral proteinase

Neurology and Research Services of the Memphis Veterans Medical Center and the Departments of Neurology and Anatomy, University of Tennessee Center for the Health Sciences, Memphis, TN

Normal human kidney contains a neutral endopeptidase that can degrade human myelin basic protein peptide 43–88. In the present study, renal homogenates prepared from postmortem tissue obtained from four persons with multiple sclerosis, two with amyotrophic lateral sclerosis, one each with olivopontocerebellar atrophy, subacute sclerosing panencephalitis, and Guillain-Barré syndrome, and four controls were analyzed for the enzymes present that degrade human myelin BP peptide 43–88. There was no evidence that the activity in renal tissue for degrading human BP peptide 43–88 is qualitatively different in persons with MS, other neurologic diseases, or controls. Gel filtration of digested peptide demonstrated the action of an endopeptidase cqable of hydrolyzing BP peptide 43–88 into large fragments.

Address correspondence and reprint requests to Dr. Whitaker, Neurology Service, Memphis Veterans Medical Center, 1030 Jefferson Avenue, Memphis, TN 38104.

This work was supported by the Research Program of the Veterans Administration and Grant No. 1111-B-4 from the National Multiple Sclerosis Society. Dr. Whitaker is a Medical Investigator of the Veterans Administration.

Accepted for publication October 20, 1982.

This article has been cited by other articles:

				J. N Whitaker Myelin basic protein in cerebrospinal fluid and other body fluids Multiple Sclerosis, February 1, 1998; 4(1): 16 - 21. [Abstract] [PDF]