title: Zinc as an inhibitor of myelin basic protein proteolytic breakdown in the central nervous system.
abstract: It is known that central nervous system myelin contains proteolytic enzymes which degrade the myelin basic protein (MBP). We have found that zinc acetate is able to inhibit MBP cleavage at concentrations of 1 mM or higher. Furthermore, the Zn-inhibitable MBP-degrading activity was found to be water-soluble and able to recognize MBP also if this protein was protected by its lipidic environment in the native-like, lipid-bound form. Data presented here suggest a Zn-dependent metallo-protease which recognize MBP as a substrate probably even in the myelin sheath, when the protein is not yet released from the membrane.
authors.affiliation: Dipartimento di Biochimica e Biologia Molecolare, Università di Bari, Italy.
authors.forename: G M
authors.initials: GM
authors.lastname: Liuzzi
authors.forename: A
authors.initials: A
authors.lastname: Ventola
authors.forename: T
authors.initials: T
authors.lastname: Rizzo
authors.forename: P
authors.initials: P
authors.lastname: Riccio
authors.forename: E
authors.initials: E
authors.lastname: Quagliariello
mesh_terms: D000818:Animals; D001923:Brain Chemistry / Q000187:drug effects; D002417:Cattle; D002490:Central Nervous System / Q000187:drug effects / Q000378:metabolism*; D006868:Hydrolysis; D066298:In Vitro Techniques; D004676:Myelin Basic Protein / Q000378:metabolism*; D015032:Zinc / Q000494:pharmacology*
chemical_list: D004676:Myelin Basic Protein; D015032:Zinc