Degradation of myelin basic protein by a membrane-associated metalloprotease: neural distribution of the enzyme.
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 nonmyelinating Schwann cells of peripheral nerve.
Chantry
A
A
Department of Neurochemistry, Institute of Neurology, London, UK.
Gregson
N
N
Glynn
P
P
D000818:Animals; D000911:Antibodies, Monoclonal; D007106:Immune Sera; D007124:Immunoenzyme Techniques; D008565:Membrane Proteins / Q000378:metabolism*; D008666:Metalloendopeptidases / Q000378:metabolism*; D004676:Myelin Basic Protein / Q000378:metabolism*; D009420:Nervous System / Q000201:enzymology*; D010455:Peptides / Q000276:immunology; D051381:Rats
D000911:Antibodies, Monoclonal; D007106:Immune Sera; D008565:Membrane Proteins; D004676:Myelin Basic Protein; D010455:Peptides; C050632:polypeptide C; D008666:Metalloendopeptidases