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Publication : Sequence and tissue-dependent RNA expression of mouse FAD-linked glycerol-3-phosphate dehydrogenase.

First Author  Koza RA Year  1996
Journal  Arch Biochem Biophys Volume  336
Issue  1 Pages  97-104
PubMed ID  8951039 Mgi Jnum  J:36995
Mgi Id  MGI:84401 Doi  10.1006/abbi.1996.0536
Citation  Koza RA, et al. (1996) Sequence and tissue-dependent RNA expression of mouse FAD-linked glycerol-3-phosphate dehydrogenase. Arch Biochem Biophys 336(1):97-104
abstractText  A 2432-bp cDNA for mouse FAD-linked glycerol-3-phosphate dehydrogenase, a nuclear-encoded enzyme associated with the inner mitochondrial membrane, was isolated from a Lambda ZAP phage library generated from brown adipocyte mRNA The amino acid sequence was 95 and 93% homologous to the rat and human enzymes. PvuII and SacI polymorphisms between Mus spretus and C57BL/6J were used to map the mouse FAD-linked glycerol-3-phosphate dehydrogenase gene (Gdm1) to chromosome 2, 33 cM from the centromere. Northern blot analysis showed that brown adipose tissue predominantly expressed a 6.5-kb mRNA with lower expression of 4.5- and 2.4-kb forms, whereas brain and pancreatic islets almost exclusively expressed a 6.5-kb transcript, muscle expressed a 4.5-kb transcript, and testis expressed a 2.4-kb RNA form. Analysis of poly(A)(+) RNA hom brown adipose tissue suggested that all RNA forms are polyadenylated. Among the tissues examined, FAD-linked glycerol-3-phosphate dehydrogenase protein levels and enzyme activity were highest in brown adipose tissue, and a consistent correlation between protein levels and enzyme activity in all tissues was observed. RNA levels corresponded to protein levels in all tissues except testis, where high levels of 2.4-kb mRNA and relatively low protein were expressed. Exposing mice to cold temperatures induced the 6.5-kb mRNA and enzyme activity only in brown adipose tissue, suggesting a role for thermogenesis in this tissue. Although the molecular basis for the formation of the 6.5- and 4.5-kb mRNA's is not known, data suggest that the regulation of FAD-linked glycerol-3-phosphate dehydrogenase is complex and tissue- specific. (C) 1996 Academic Press, Inc.
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