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    ASN Neuro. 2009 Aug 25;1(3). pii: e00014. doi: 10.1042/AN20090028.

    Different proteolipid protein mutants exhibit unique metabolic defects.

    Hüttemann M, Zhang Z, Mullins C, Bessert D, Lee I, Nave KA, Appikatla S, Skoff RP.

    *Center for Molecular Medicine and Genetics, Wayne State University School of Medicine, Detroit, MI 48201, U.S.A.

    PMD (Pelizaeus-Merzbacher disease), a CNS (central nervous system) disease characterized by shortened lifespan and severe neural dysfunction, is caused by mutations of the PLP1 (X-linked myelin proteolipid protein) gene. The majority of human PLP1 mutations are caused by duplications; almost all others are caused by missense mutations. The cellular events leading to the phenotype are unknown. The same mutations in non-humans make them ideal models to study the mechanisms that cause neurological sequelae. In the present study we show that mice with Plp1 duplications (Plp1tg) have major mitochondrial deficits with a 50% reduction in ATP, a drastically reduced mitochondrial membrane potential and increased numbers of mitochondria. In contrast, the jp (jimpy) mouse with a Plp1 missense mutation exhibits normal mitochondrial function. We show that PLP in the Plp1tg mice and in Plp1-transfected cells is targeted to mitochondria. PLP has motifs permissive for insertion into mitochondria and deletions near its N-terminus prevent its co-localization to mitochondria. These novel data show that Plp1 missense mutations and duplications of the native Plp1 gene initiate uniquely different cellular responses.

    PMID: 19663806 [PubMed - in process]

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