Incorporation of D-xylose-C14 into glycoprotein by particles from hen oviduct

Grebner, Eugene E.; Hall, Clara W.; Neufeld, Elizabeth F.

doi:10.1016/0006-291x(66)90199-9

Cited by 60 publications

(11 citation statements)

References 11 publications

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“…In particular, transfer of radioactive xylose into trichloroacetic acid precipitable material by hen oviduct, murine mastocytoma and embryonic chicken cartilage extracts, as sources containing both enzyme and acceptor, was reported by the Neufeld [8,9] and Dorfman groups [10]. Subsequently Baker et al tested embryonic chicken cartilage as a source of xylosyltransferase with a number of different acceptor substrates, ranging from Smith-degraded (i.e.…”

Section: Defining Xylosyltransferase Acceptor Specificitymentioning

confidence: 95%

The never-ending story of peptide O -xylosyltransferase

Wilson

2004

Cellular and Molecular Life Sciences (CMLS)

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In a journey lasting 40 years from the first reports on its activity in the 1960s to its purification and the cloning of relevant complementary DNAs, peptide O-xylosyltransferase has finally arrived at the same point as many other enzymes. This enzyme, whose systematic name is UDP-alpha-D-xylose:proteoglycan core protein beta-D-xylosyltransferase (EC 2.4.2.26), catalyses the first step in the biosynthesis of chondroitin, dermatan and heparan sulphates in the endoplasmic reticulum and/or the cis-Golgi cisternae. Analyses of their primary structure show that peptide O-xylosyltransferases are members of glycosyltransferase family 14 and so are homologous to beta1,6- N-acetylglucosaminyltransferases involved in O-glycan and poly- N-acetyllactosamine branching. Furthermore, vertebrates appear to have two rather similar genes encoding xylosyltransferase I and xylosyltransferase II, but enzymatic activity was only detected for a recombinant form of the first isoform. On the other hand, Caenorhabditis and Drosophila have each only one peptide O-xylosyltransferase gene. In the worm sqv-6 mutant, a mutation of the xylosyltransferase gene is associated with defective vulval morphogenesis, indicative of the importance of the glycosaminoglycan chains of proteoglycans in animal development. There remain, however, open questions, for instance, on the enzyme's intracellular localisation and structure-function relationships.

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Section: Defining Xylosyltransferase Acceptor Specificitymentioning

confidence: 95%

The never-ending story of peptide O -xylosyltransferase

Wilson

2004

Cellular and Molecular Life Sciences (CMLS)

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“…This indicates that these radioactive substrates were incorporated into protein largely unchanged and that conversion to amino acids did not take place to any detectable extent. Based on previous work by others (20)(21)(22)(23), it is probable that the incorporation was through a nucleotide intermediate, but that these compounds were not detected by the isolation procedures used in this study.…”

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confidence: 78%

Alveolar cells: incorporation of carbohydrate into protein and evidence for intracellular protein transport

Massaro¹

1968

J. Clin. Invest.

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“…Such sites would include those that synthesized mucopolysaccharides: most steps of mucopolysaccharide synthesis proceed outside the mitochondria as well as outside of the liver (30). Furthermore, some critical biosynthetic steps require manganese (1)(2)(3)(4)(5)(6).…”

Section: Discussionmentioning

confidence: 99%

“…Enzymes critical to mucoprotein synthesis are activated by manganese (1)(2)(3), and, conversely, defective mucopolysaccharide synthesis is found in manganese deficient animals (4,5). These mechanisms underlie the gross mesenchymal aberrations which characterize manganese deficiency (6).…”

Section: Introductionmentioning

confidence: 99%

Slow turnover of manganese in active rheumatoid arthritis accelerated by prednisone

Cotzias¹,

Papavasiliou²,

Hughes³

et al. 1968

J. Clin. Invest.

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Total body and area counts of intravenously injected 54Mn were measured periodically in 29 in-patients. A heterogeneous group of 19 control patients showed fair reproducibility in the immediate distribution, and considerable individual variance in the subsequent loss of the isotope. Eight studies of the effects of feeding excesses of manganous sulfate to five patients showed acceleration of the rate of loss of the radioisotope from the whole body and the liver. These findings seem compatible with the presence of control mechanisms in man, operating to vary the metal's excretion, while tending to preserve constancy of its concentration in tissues.Slow turnover rates of the metal were demonstrated in seven out of eight patients with active rheumatoid arthritis, in one with hydralazine disease, but not in one arthritic undergoing an impressive, spontaneous remission. Statistically significant differences were encountered in the measurements of 54Mn turnover of the total body, the thyroid, and the liver.Administration of prednisone induced clinical improvement and significant acceleration of these turnovers. Slow turnovers are characteristic of nutritional manganese deficiency. Therefore, serum and blood manganese determinations were performed by neutron activation analysis on 14 control patients, and on six patients with active rheumatoid arthritis. A statistically significant elevation of the red cell manganese concentration was encountered in patients with rheumatoid arthritis. This argued against the presence of classical trace-

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Incorporation of D-xylose-C14 into glycoprotein by particles from hen oviduct

Cited by 60 publications

References 11 publications

The never-ending story of peptide O -xylosyltransferase

The never-ending story of peptide O -xylosyltransferase

Alveolar cells: incorporation of carbohydrate into protein and evidence for intracellular protein transport

Slow turnover of manganese in active rheumatoid arthritis accelerated by prednisone

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