Galactose Metabolism in Mice with Galactose-1-Phosphate Uridyltransferase Deficiency: Sucklings and 7-Week-Old Animals Fed a High-Galactose Diet

2001 ◽  
Vol 72 (4) ◽  
pp. 306-315 ◽  
Author(s):  
Cong Ning ◽  
Robert Reynolds ◽  
Jie Chen ◽  
Claire Yager ◽  
Gerard T. Berry ◽  
...  
Keyword(s):  
Galactose Metabolism ◽  
Uridyltransferase Deficiency

scholarly journals Galactose Metabolism by the Mouse with Galactose-1-Phosphate Uridyltransferase Deficiency

2000 ◽  
Vol 48 (2) ◽  
pp. 211-217 ◽  
Author(s):  
Cong Ning ◽  
Robert Reynolds ◽  
Jie Chen ◽  
Claire Yager ◽  
Gerard T Berry ◽  
...  
Keyword(s):  
Galactose Metabolism ◽  
Uridyltransferase Deficiency

scholarly journals Current and Future Treatments for Classic Galactosemia

2021 ◽  
Vol 11 (2) ◽  
pp. 75 ◽  
Author(s):  
Britt Delnoy ◽  
Ana I. Coelho ◽  
Maria Estela Rubio-Gozalbo
Keyword(s):  
Standard Of Care ◽  
Type I ◽  
Therapeutic Approaches ◽  
Restricted Diet ◽  
Galactose Metabolism ◽  
Galt Activity ◽  
Classic Galactosemia ◽  
Pathogenic Factors ◽  
Future Treatments ◽  
Novel Therapeutic

Type I (classic) galactosemia, galactose 1-phosphate uridylyltransferase (GALT)-deficiency is a hereditary disorder of galactose metabolism. The current therapeutic standard of care, a galactose-restricted diet, is effective in treating neonatal complications but is inadequate in preventing burdensome complications. The development of several animal models of classic galactosemia that (partly) mimic the biochemical and clinical phenotypes and the resolution of the crystal structure of GALT have provided important insights; however, precise pathophysiology remains to be elucidated. Novel therapeutic approaches currently being explored focus on several of the pathogenic factors that have been described, aiming to (i) restore GALT activity, (ii) influence the cascade of events and (iii) address the clinical picture. This review attempts to provide an overview on the latest advancements in therapy approaches.

scholarly journals Inhibition of protein N-glycosylation by 2-deoxy-2-fluoro-d-galactose

1992 ◽  
Vol 285 (3) ◽  
pp. 821-826 ◽  
Author(s):  
V Gross ◽  
W E Hull ◽  
U Berger ◽  
T Andus ◽  
W Kreisel ◽  
...  
Keyword(s):  
Interleukin 6 ◽  
Ex Vivo ◽  
Primary Cultures ◽  
Blood Monocytes ◽  
Galactose Metabolism ◽  
Rat Hepatocyte ◽  
Peripheral Blood Monocytes ◽  
Efficient Inhibitor ◽  
Acid Glycoprotein ◽  
Alpha 1 Antitrypsin

The effects of 2-deoxy-2-fluoro-D-galactose (dGalF) on N- and O-glycosylation of proteins was studied in rat hepatocyte primary cultures and in human monocytes. In hepatocytes, dGalF at concentrations of 1 mM or higher completely inhibited N-glycosylation of alpha 1-antitrypsin and alpha 1-acid glycoprotein, whereas 4 mM-2-deoxy-D-galactose (dGal) only slightly impaired N-glycosylation. In monocytes, 1 mM- or 4 mM-dGalF blocked N-glycosylation of alpha 1-antitrypsin and of interleukin-6, while O-glycosylation of interleukin-6 remained unaffected. In monocytes, dGal had no effect on protein N-glycosylation. Addition of uridine effectively prevented the UTP deficiency induced by dGalF, but had no effect on the inhibition of protein N-glycosylation by dGalF. Using 19F-n.m.r. spectroscopy, 2-deoxy-2-fluoro-D-galactose 1-phosphate (dGalF-1-P), UDP-dGalF and UDP-dGlcF could be identified as the major metabolites of dGalF in hepatocytes as well as in monocytes. In conclusion, compared with dGal, dGalF is a more efficient inhibitor of protein N-glycosylation. The effect is not caused by the depletion of UTP induced by dGalF, but rather by metabolites of dGalF. dGalF is metabolized not only in hepatocytes but also in peripheral blood monocytes, which can be used for ex vivo studies of disturbances in D-galactose metabolism.

Congenital Galactosemia. A Single Enzymatic Block in Galactose Metabolism

PEDIATRICS ◽  
1956 ◽  
Vol 18 (2) ◽  
pp. 204-204
Keyword(s):  
Recent Work ◽  
Inborn Errors Of Metabolism ◽  
Galactose Metabolism ◽  
Inborn Errors ◽  
Therapeutic Applications ◽  
Metabolic Conversion

Four enzymes are involved in the metabolic conversion of galactose to glucose-l-phosphate. This paper presents final evidence that in congenital galactosemia one of these, phosphogalatose-uridyl transferase, is lacking. This leads to an accumulation galactose-1-phosphate in erythrocytes when galactose is administered to infants suffering from congenital galactosemia. References to recent work which have made this conclusion possible are given. It is not suggested that any immediate therapeutic applications may be made but it is through such elucidation that some of the so called inborn errors of metabolism may ultimately be corrected.

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