Gymnastik- och idrottshögskolan, GIH

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Defects in Galactose Metabolism and Glycoconjugate Biosynthesis in a UDP-Glucose Pyrophosphorylase-Deficient Cell Line Are Reversed by Adding Galactose to the Growth Medium.
Université de Paris, France.
Hannover Medical School, Germany.
Université de Paris, France.
Université Paris Decartes, Sorbonnes Paris Cité, Institut Imagine, France.
Vise andre og tillknytning
2020 (engelsk)Inngår i: International Journal of Molecular Sciences, ISSN 1661-6596, E-ISSN 1422-0067, Vol. 21, nr 6, artikkel-id E2028Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

UDP-glucose (UDP-Glc) is synthesized by UGP2-encoded UDP-Glc pyrophosphorylase (UGP) and is required for glycoconjugate biosynthesis and galactose metabolism because it is a uridyl donor for galactose-1-P (Gal1P) uridyltransferase. Chinese hamster lung fibroblasts harboring a hypomrphic UGP(G116D) variant display reduced UDP-Glc levels and cannot grow if galactose is the sole carbon source. Here, these cells were cultivated with glucose in either the absence or presence of galactose in order to investigate glycoconjugate biosynthesis and galactose metabolism. The UGP-deficient cells display < 5% control levels of UDP-Glc/UDP-Gal and > 100-fold reduction of [6-3H]galactose incorporation into UDP-[6-3H]galactose, as well as multiple deficits in glycoconjugate biosynthesis. Cultivation of these cells in the presence of galactose leads to partial restoration of UDP-Glc levels, galactose metabolism and glycoconjugate biosynthesis. The Vmax for recombinant human UGP(G116D) with Glc1P is 2000-fold less than that of the wild-type protein, and UGP(G116D) displayed a mildly elevated Km for Glc1P, but no activity of the mutant enzyme towards Gal1P was detectable. To conclude, although the mechanism behind UDP-Glc/Gal production in the UGP-deficient cells remains to be determined, the capacity of this cell line to change its glycosylation status as a function of extracellular galactose makes it a useful, reversible model with which to study different aspects of galactose metabolism and glycoconjugate biosynthesis.

sted, utgiver, år, opplag, sider
MDPI, 2020. Vol. 21, nr 6, artikkel-id E2028
Emneord [en]
UDP-galactose, UDP-glucose, UGP2, congenital disorders of glycosylation (CDGs), developmental epileptic encephalopathies (DEEs), galactose, glycosphingolipid, prion protein, protein glycosylation
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URN: urn:nbn:se:gih:diva-6377DOI: 10.3390/ijms21062028PubMedID: 32188137OAI: oai:DiVA.org:gih-6377DiVA, id: diva2:1501623
Tilgjengelig fra: 2020-11-17 Laget: 2020-11-17 Sist oppdatert: 2022-02-10bibliografisk kontrollert

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