UDP-galactose:Glycoprotein galactosyltransferase activity in tissues of developing rat

Jato-Rodriguez, Juan J.; Mookerjea, Sailen

doi:10.1016/0003-9861(74)90127-1

Cited by 26 publications

(3 citation statements)

References 31 publications

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“…No evidence of enzyme heterogeneity could be found, and the Km values and other kinetic parameters of the galactokinase remain cotistant during development (WaIker-& Khan, 1968). Similar results are reported for the UDP-galactose 4-epimerase (Cohn & Segal, 1969) and UDP-galactoseglycoprotein galactosyltransferase (Jato-Rodriguez & Mookerjea, 1974), except that these enzymes show their highest-activities in the perinatal period and decrease rapidly within a few days. The Km Value of 554uM-LI]W-galactose for both foetal and adult liver galactosyltransferase does not differ from data obtained after partial hepatectomy.…”

Section: Discussionsupporting

confidence: 85%

Galactose metabolism in regenerating rat liver

Bauer¹,

Hassels²,

Reutter³

1976

Biochemical Journal

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1. Rats trained on a controlled lighting and feeding schedule were subjected to partial hepatectomy or sham operation. 2. After a large period of about 6h the activity of UDP-galactose 4-epimerase increased threefold, reaching a maximum 4 days after partial hepatectomy, and returned to normal values within a fortnight. 3. The enzyme pattern of the UDP-galactose-glycoprotein galactosyltransferase was biphasic, one peak appearing at 20 h, the second at 72 h after partial hepatectomy. 4. The rise in enzyme activities could be blocked by the injection of actinomycin D, and the Km values for UDP-glucose and UDP-galactose were nearly identical in regenerating and adult liver. It is therefore concluded that the increase in enzyme activity is due to synthesis de novo of enzyme protein.

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Section: Discussionsupporting

confidence: 85%

Galactose metabolism in regenerating rat liver

Bauer¹,

Hassels²,

Reutter³

1976

Biochemical Journal

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“…Several studies have demonstrated that changes in the surface glycoproteins occur in malignant cells (Meezan et al, 1969;Buck et al, 1971). The glycosyltransferase activities which regulate chain elongation of the oligosaccharide prosthetic groups of glycoproteins undergo changes when the cells are transformed by oncogenic viruses (Bosmann, 1972;Grimes, 1973), during the growth stage in the mitotic cycle of the cell (Bosmann, 1971) and in tissues during embryonic development (Carlson et al, 1973;Jato-Rodriguez & Mookerjea, 1974). Warren et al (1972) found an increase of specific sialyltransferases both in transformed and in dividing cells.…”

mentioning

confidence: 99%

Sialyltransferase activity in regenerating rat liver

Serafini‐Cessi¹

1977

Biochemical Journal

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Liver microsomal fractions catalyse the transfer of sialic acid from CMP-N-acetyl-neuraminic acid to various exogenous acceptors such as desialylated fetuin, desialylated human Tamm-Horsfall glycoprotein and desialylated bovine submaxillary-gland mucin. An increase in the rate of incorporation of sialic acid into desialylated glycoproteins was found after a lag period (7h) in regenerating liver. The increase was maximum 24h after partial hepatectomy for all acceptors tested. At later times after operation the sialyltransferase activity remained high only for desialylated fetuin. No soluble factors from liver or serum of partially hepatectomized animals influenced the activity of the sialyltransferases bound to the microsomal fraction. The sensitivity of sialyltransferases to activation by Triton X-100, added to the incubation medium, was unchanged in the microsomal preparation from animals 24h after sham operation or partial hepatectomy. The full activity of sialyltransferases towards the various desialylated acceptors showed some differences. Human Tamm-Horsfall glycoprotein was a good acceptor of sialic acid only when desialylated by mild acid hydrolysis. After this treatment, but not after enzymic hydrolysis, a decrease in molecular weight of human Tamm-Horsfall glycoprotein was observed. Further, the sialyltransferase activity as a function of incubation temperature gave different curves according to the acceptor used. The relationship between the biosynthesis of glycoproteins by regenerating liver and the sialyltransferase activity of microsomal fraction after partial hepatectomy is discussed.

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“…In this context, it is of interest that some glycosyltransferases unrelated to ABO bloodgroup synthesis are increased in embryonic chicken brain [3] and in the tissues of the embryonic and neonatal rat [1,7,9], Per haps some non-specific stimulating factor, possibly hormonal, is present in the embryo and neonate.…”

Section: Resultsmentioning

confidence: 99%

Human Blood-Group A- and H-Specified Glycosyltransferase Levels in the Sera of Newborn Infants and their Mothers

Tilley

Crookston

et al. 1978

Vox Sanguinis

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The level of blood-group A^1-specified α,3'-N-acetyl-D-galactosaminyl-transferase in the serum of recently-delivered women was found to be appreciably lower than the level of this enzyme in the serum of non-pregnant adults and of newborn infants ; a similar but less striking decrease was observed in the levels of the A^2-specified a,3'-N-acetyl-D-galactosaminyltransferase and the H-specified α,2'-L-fucosyltransferase. Although the red cells of newborn infants are known to have relatively few A and H antigen sites, the serum of neonates was found to have a level of A^1- and A^2-dependent N-acetylgalactosaminyltransferases and Hdependent fucosyltransferase as high as, if not higher than, the serum of non-pregnant adults. This finding is compatible with the fact that the haemopoietic tissue contributes only about 20% of the serum transferase level.

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UDP-galactose:Glycoprotein galactosyltransferase activity in tissues of developing rat

Cited by 26 publications

References 31 publications

Galactose metabolism in regenerating rat liver

Galactose metabolism in regenerating rat liver

Sialyltransferase activity in regenerating rat liver

Human Blood-Group A- and H-Specified Glycosyltransferase Levels in the Sera of Newborn Infants and their Mothers

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