TY - JOUR
T1 - Isolation, mapping, and functional expression of the mouse X chromosome glycerol kinase gene
AU - Mahbubul Huq, A. H.M.
AU - Lovell, Rhonda S.
AU - Sampson, Margaret J.
AU - Decker, William K.
AU - Dinulos, Mary Beth
AU - Disteche, Christine M.
AU - Craigen, William J.
N1 - Funding Information:
This work was supported in part by the Baylor College of Medicine Mental Retardation Research Center (NICHD 2P30-HD24064), Child Health Research Center (NICHD 1P30-HD27823), a March of Dimes Basil O'Connor Award (W.J.C.), NIH GM46883 (C.M.D.), March of Dimes Grant 1013 (C.M.D.), and NIH GM07454 (M.B.D.). Thanks to Lucy Rowe and Mary Barter at the Jackson Laboratory Panel Map Service.
PY - 1996/9/15
Y1 - 1996/9/15
N2 - Glycerol kinase (Gyk) participates in the metabolism of endogenously derived and dietary glycerol. Deficiency of the human enzyme activity is an X-linked recessive disorder with a clinical picture varying from childhood metabolic crisis to asymptomatic adults incidentally identified by hyperlipidemia screening (pseudohypertriglyceridemia). Gyk is a member of a small group of kinases termed ambiquitous enzymes that are found in the cytosol or as membrane-bound enzymes associated with the voltage-dependent anion channel of the mitochondrial outer membrane. It was recently reported that in humans there are X4inked and autosomal copies of Gyk sequences, both apparently functional genes and processed pseudogenes. To understand the role of Gyk in normal metabolism and the variable clinical features seen with Gyk deficiency, we have characterized the mouse Gyk gene. We present the sequence of a full-length mouse Gyk cDNA that is alternatively spliced in brain. The Gyk gene was mapped to the mouse X chromosome by both fluorescence in situ hybridization and an interspecies backcross panel, demonstrating conservation of synteny with dmd. To confirm the functional identity of the cDNA, transient transfection of the cDNA into COS7 cells was shown to cause a marked elevation in glycerol kinase activity.
AB - Glycerol kinase (Gyk) participates in the metabolism of endogenously derived and dietary glycerol. Deficiency of the human enzyme activity is an X-linked recessive disorder with a clinical picture varying from childhood metabolic crisis to asymptomatic adults incidentally identified by hyperlipidemia screening (pseudohypertriglyceridemia). Gyk is a member of a small group of kinases termed ambiquitous enzymes that are found in the cytosol or as membrane-bound enzymes associated with the voltage-dependent anion channel of the mitochondrial outer membrane. It was recently reported that in humans there are X4inked and autosomal copies of Gyk sequences, both apparently functional genes and processed pseudogenes. To understand the role of Gyk in normal metabolism and the variable clinical features seen with Gyk deficiency, we have characterized the mouse Gyk gene. We present the sequence of a full-length mouse Gyk cDNA that is alternatively spliced in brain. The Gyk gene was mapped to the mouse X chromosome by both fluorescence in situ hybridization and an interspecies backcross panel, demonstrating conservation of synteny with dmd. To confirm the functional identity of the cDNA, transient transfection of the cDNA into COS7 cells was shown to cause a marked elevation in glycerol kinase activity.
UR - http://www.scopus.com/inward/record.url?scp=0030587409&partnerID=8YFLogxK
U2 - 10.1006/geno.1996.0500
DO - 10.1006/geno.1996.0500
M3 - Article
C2 - 8884278
AN - SCOPUS:0030587409
VL - 36
SP - 530
EP - 534
JO - Genomics
JF - Genomics
SN - 0888-7543
IS - 3
ER -