Gz. Zhu et al., Fudenine, a C-terminal truncated rat homologue of mouse prominin, is bloodglucose-regulated and can up-regulate the expression of GAPDH, BIOC BIOP R, 281(4), 2001, pp. 951-956
Citations number
15
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Messenger RNA differential display was applied to screen for the blood gluc
ose regulated genes in SD rat skeletal muscle. The rat homologue of the mou
se prominin was thus identified. Comparing to its mouse and human homologue
s, fudenine was C-terminal truncated due to a single nucleotide deletion. H
owever, its mitochondrial energy transfer signature peptide PQDLVKKLI remai
ned intact. Fudenine, an 592-amino acid containing, 66-kDa glycoprotein, is
a novel plasma membrane protein with four transmembrane segments flanking
by two large glycosylated extracellular domains. Although it is devoid of t
he last transmembrane domain comparing to its homologues, fudenine also loc
ates in cell membrane by transfection of fusion plasmid pFudenine-EGFP into
CBRH7919 cell and L-6TG: cell. Overexpression of fudenine in CBRH7919 cell
line up-regulated the mRNA level of GAPDH (3-phosphate glyceraldehyde dehy
drogenase), while long-term glucose exposure resulted to reduced GAPDH expr
ession. Since high blood glucose level induced the expression of fudenine i
n skeletal muscle, which in turn up-regulated the expression of GAPDH, we p
ropose that fudenine might be a candidate gene for diabetes mellitus. (C) 2
001 Academic Press.