Degradation of myelin basic protein by a membrane-associated metalloprotease: Neural distribution of the enzyme |
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| Authors: | Andrew Chantry Norman Gregson Paul Glynn |
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| Affiliation: | (1) The Multiple Sclerosis Society Laboratory, Department of Neurochemistry, Institute of Neurology, WC1N 1PJ London;(2) Department of Anatomy, Guy's Hospital Medical School, SE1 9RT London, UK;(3) Present address: Medical Research Council Immunochemistry Unit, Department of Biochemistry, University of Oxford, OX1 3QU Oxford;(4) Medical Research Council Laboratories, Woodmansterne Road, SM5 4EF Carshalton, Surrey |
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| Abstract: | A metalloprotease activity associated with myelin membrane preparations degrades myelin basic protein (MBP), generating a characteristic fragment designated peptide C (MBP 74-170). Using an immunoblotting assay, peptide C-generating activity was detected in mammalian, avian, reptilian, and amphibian brains. The activity was present in rat brain as early as postnatal day 1 and also in adult rat peripheral nerve. Immunohistochemistry with a monoclonal antibody to the purified enzyme revealed that the metalloprotease was present in oligodendrocytes of optic nerve, of both white and grey matter of spinal cord, and also in the cytoplasm of both myelinating and non-myelinating Schwann cells of peripheral nerve.Special issue dedicated to Dr. Alan N. Davison |
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| Keywords: | Metalloprotease myelin basic protein peptide C |
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