title: Increased spectrin proteolysis in the brindled mouse brain.
abstract: Proteolytically generated fragments of the microfilament anchoring protein brain spectrin were found to accumulate in brindled mouse brain. Proteolysis was most extensive in brain regions possessing high concentrations of N-methyl-D-aspartate (NMDA) receptors (e.g. cortex, striatum, hippocampus). The brindle mutation affects copper homeostasis and thus a variety of copper-dependent enzymes needed in intermediary metabolism. The altered mitochondria of these mice are suggested to less efficiently buffer NMDA receptor-gated calcium fluxes, thus promoting activation of calcium-activated proteases and subsequent degradation of the spectrin meshwork.
authors.affiliation: Bonney Center for the Neurobiology of Learning and Memory, University of California, Irvine 92717.
authors.forename: P
authors.initials: P
authors.lastname: Seubert
authors.forename: C
authors.initials: C
authors.lastname: Peterson
authors.forename: P
authors.initials: P
authors.lastname: Vanderklish
authors.forename: C
authors.initials: C
authors.lastname: Cotman
authors.forename: G
authors.initials: G
authors.lastname: Lynch
mesh_terms: D000375:Aging / Q000378:metabolism; D000818:Animals; D001921:Brain / Q000254:growth & development / Q000378:metabolism*; D003300:Copper / Q000172:deficiency / Q000378:metabolism / Q000502:physiology*; D008297:Male; D051379:Mice; D008817:Mice, Mutant Strains / Q000254:growth & development / Q000378:metabolism*; D008970:Molecular Weight; D013049:Spectrin / Q000378:metabolism*
chemical_list: D013049:Spectrin; D003300:Copper