Agarose gel isoelectrofocusing of UDP-galactose pyrophosphorylase and galactose-1-phosphate uridyltransferase. Developmental aspect of UDP-galactose pyrophosphorylase

Shin, Yoon S.; Niedermeier, H.; Endres, W.; Schaub, J.; Weidinger, S.

doi:10.1016/0009-8981(87)90191-4

Cited by 24 publications

(11 citation statements)

References 12 publications

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“…The diagnosis of D-1 and D-2 variants was based on the presence of the N314D sequence change, on GALT activity levels of about 20% of normal in erythrocyte lysates of D-2/G patients and by increased GALT activity in erythrocyte lysates of the D-1 probands. The identity of the D-1 and D-2 alleles was further confirmed by isoelectric focusing of GALT activity in erythrocyte lysates (Shin et al, 1987) in the laboratory of Y.S. Shin, University of Munich, Germany.…”

Section: Materials and Methods Patientsmentioning

confidence: 78%

“…The most common variant form of the GALT enzyme, the Duarte variant (Beutler et al, 1966) exists as two different types: Duarte-1 (D-1) with normal or increased enzyme activity and Duarte-2 (D-2) with an enzyme activity reduced to about 35-45% of normal (Shin et al, 1987). Compound heterozygotes for one classical galactosemia allele (G) and one D-2 allele (D-2/G) have a GALT activity of about 25% of normal and only rarely develop clinical symptoms.…”

Section: Introductionmentioning

confidence: 99%

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Molecular heterogeneity of classical and duarte galactosemia: Mutation analysis by denaturing gradient gel electrophoresis

et al. 1997

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Section: Materials and Methods Patientsmentioning

confidence: 78%

Section: Introductionmentioning

confidence: 99%

Molecular heterogeneity of classical and duarte galactosemia: Mutation analysis by denaturing gradient gel electrophoresis

et al. 1997

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“…The Duarte variant (D or D2) has been defined biochemically by reduced enzyme activity and by an isoform distinguishable by native gel electrophoresis and isoelectric focusing [Beutler et al, 1965;Kelley et al, 1983;Shin et al, 1987]. Another GALT enzyme, the Los Angeles variant (LA or D1), exists with isoforms and immunochemical reactions identical to those of Duarte 2, except that it is associated with increased activity compared with controls [Ng et al, 1972].…”

Section: The Duarte Allelementioning

confidence: 98%

Classical galactosemia and mutations at the galactose-1-phosphate uridyl transferase (GALT) gene

et al. 1999

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“…UDPglucose is readily formed from uridine triphosphate and glucose-lphosphate by the action of UDPglucose pyrophosphorylase. In contrast, the formation of UDPgalactose from galactose-1-phosphate via UDPgalactose pyrophosphorylase is minimal (21). On the other hand, UDPgalactose is readily formed from UDPglucose via UDPgalactose-4-epimerase.…”

Section: Discussionmentioning

confidence: 95%

Uridine Diphosphate Hexoses in Leukocytes and Fibroblasts of Classic Galactosemics and Patients with Other Metabolic Diseases

et al. 1994

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To examine uridine diphosphate hexose (UDPhexose) content of cells that have more complete metabolic patterns than erythrocytes, which have been commonly used in the study of galactosemia, the concentrations of uridine diphosphate galactose (UDPgalactose) and uridine diphosphate glucose (UDPglucose) were determined in white blood cells (WBC) and fibroblasts cultured from skin biopsies. Leukocyte UDPgalactose and UDPglucose values were determined in 60 normal individuals, 14 classic galactosemics, and 18 patients with other metabolic diseases on protein-restricted and low-lactose diets. There was no difference in the average concentration of these compounds between any of these groups. There was no relationship between age and WBC UDPhexose content or correlation of WBC and erythrocyte UDPhexose levels in the same blood specimens. WBC from galactosemic individuals differ from their red blood cells because the former do not show the low average UDPgalactose levels and abnormal UDPglucose to UDPgalactose ratio previously reported for erythrocytes from galactose-1-phosphate uridyltransferase-deficient individuals. Fibroblast cell lines from 10 normal and 10 galactosemic individuals, cultured and grown to confluence in glucose medium, also showed no difference in nucleotide sugar concentrations. Thus far, of the cell types easily available, red blood cells appear to be unique in showing an abnormality in nucleotide sugar metabolism. The fact that galactosemic fibroblasts demonstrate no abnormality in the concentration of these compounds suggests that the defective galactosylation that has been observed in galactosemic fibroblasts is not due to (1) reported that UDPgalactose concentration was low in red blood cells, liver biopsies, and cultured fibroblasts of patients with classic galactosemia, much attention has been focused on cellular UDPhexose levels. It has been suggested that a deficiency of UDPgalactose, the obligate donor in galactosylation, could lead to a defect in this important cellular process. The postulate that impaired galactosylation may be the basis for the long-term complications seen in galactosemics,

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Agarose gel isoelectrofocusing of UDP-galactose pyrophosphorylase and galactose-1-phosphate uridyltransferase. Developmental aspect of UDP-galactose pyrophosphorylase

Cited by 24 publications

References 12 publications

Molecular heterogeneity of classical and duarte galactosemia: Mutation analysis by denaturing gradient gel electrophoresis

Molecular heterogeneity of classical and duarte galactosemia: Mutation analysis by denaturing gradient gel electrophoresis

Classical galactosemia and mutations at the galactose-1-phosphate uridyl transferase (GALT) gene

Uridine Diphosphate Hexoses in Leukocytes and Fibroblasts of Classic Galactosemics and Patients with Other Metabolic Diseases

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