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Publication : Human and murine glycerol kinase: influence of exon 18 alternative splicing on function.

First Author  Ohira RH Year  2005
Journal  Biochem Biophys Res Commun Volume  331
Issue  1 Pages  239-46
PubMed ID  15845384 Mgi Jnum  J:97598
Mgi Id  MGI:3575881 Doi  10.1016/j.bbrc.2005.03.143
Citation  Ohira RH, et al. (2005) Human and murine glycerol kinase: Influence of exon 18 alternative splicing on function. Biochem Biophys Res Commun 331(1):239-46
abstractText  Glycerol kinase (GK) is a key enzyme in glycerol metabolism with two alternatively spliced forms-one with an 87bp insertion corresponding to exon 18 (GK+EX18), and one lacking exon 18 (GK-EX18). We report the expression of GK+/-EX18 in various tissues and cell lines, as well as their enzymatic characteristics and subcellular localization. RT-PCR revealed differential expression in tissues and cell lines. Northern blot analysis revealed that both forms of the murine ortholog, Gyk, were highly expressed in murine heart and increased during embryonic development. K(m) values for glycerol for GK+/-EX18 were not significantly different, although GK-EX18 had a higher V(max) for glycerol. GK-EX18 had a lower K(m) and V(max) for ATP than GK+EX18. Immunofluorescence experiments showed that GK+EX18 co-localized to the mitochondria and the perinuclear region while GK-EX18 had a diffuse expression pattern. These data suggest specific and divergent roles for GK+EX18 and GK-EX18 in cellular metabolism and development.
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