Biosynthesis of glucosylated derivatives of dolichol: possible intermediates in the assembly of white matter glycoproteins

Scher, Malka G.; Jochen, Albert; Waechter, Charles J.

doi:10.1021/bi00642a015

Cited by 42 publications

(22 citation statements)

References 41 publications

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“…Upon incubation with radiolabeled DPG, UMP (but not UDP) was able to reverse the DPGS reaction up to 57% at 0.62 mM [76]. These results are consistent with previous observations for DPGS from mammalian [78], plant [79] and protozoan [80] cells. The role of nucleotides in the regulation of DPGS in vivo remains to be elucidated.…”

Section: Dp Glucose Synthasesupporting

confidence: 92%

Protein Glycosylation in Candida

et al. 2009

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Candidiasis is a significant cause of invasive human mycosis with associated mortality rates that are equivalent to, or worse than, those cited for most cases of bacterial septicemia. As a result, considerable efforts are being made to understand how the fungus invades host cells and to identify new targets for fungal chemotherapy. This has led to an increasing interest in Candida glycobiology, with an emphasis on the identification of enzymes essential for glycoprotein and adhesion metabolism, and the role of N- and O-linked glycans in host recognition and virulence. Here, we refer to studies dealing with the identification and characterization of enzymes such as dolichol phosphate mannose synthase, dolichol phosphate glucose synthase and processing glycosidases and synthesis, structure and recognition of mannans and discuss recent findings in the context of Candida albicans pathogenesis.

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Section: Dp Glucose Synthasesupporting

confidence: 92%

Protein Glycosylation in Candida

et al. 2009

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“…To evaluate the potential influence of sugar nucleotides on glycoprotein formation, two types of enzymes must be taken into account. For those responsible for the synthesis of the dolichol-linked saccharide intermediates involved in the assembly of the core portion of asparagine-bound carbohydrate units Km values of 10 7 mol/l have been reported for GDP-mannose [37] and UDPglucose [38]; even the very low concentrations of GDPmannose found in the tissues studied and the reduced level of UDP-glucose seen in liver and muscle are many times greater than the Km values for the dolichylphosphate monosaccharide synthesis. However, the enzymes involved in building carbohydrate units by adding sugars such as galactose, glucose, sialic acid or N-acetylglucosamine directly from the nucleotides have Km values of 10 -4 to 10 -5 tool/1 [17,39,40]; the Km values for sugar nucleotides of enzymes responsible for glycosaminoglycan [41,42] or glycolipid [43,44] synthesis similarly are approximately 10 4 tool/1.…”

Section: Discussionmentioning

confidence: 99%

Effect of diabetes on the sugar nucleotides in several tissues of the rat

Spiro

1984

Diabetologia

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Summary. Studies have been carried out to determine the effect of diabetes on the concentrations of sugar nucleotides in several tissues of the rat. This represents one aspect of an investigation aimed at evaluating the role which alterations in the metabolism of glycoproteins or other glycoconjugates may play in the development of the long-term complications of this disease. Measurements were made of the nucleotides of hexoses, N-acetylhexosamines, hexuronic acids, and sialic acid in liver, kidney, skeletal muscle, testis and heart of alloxan-diabetic rats and age-matched controls. Of the intermediates studied, only UDP-glucose and UDP-galactose showed significant alterations in diabetes. The direction of the changes depended on the tissue, with the levels in liver and skeletal muscle being decreased, those in kidney and testis increased and the concentrations in heart being unchanged. In the diabetic liver, the concentrations of UDP-glucose was reduced to 0.75 that of normal, while in skeletal muscle both UDP-glucose and UDP-galactose were significantly decreased (diabetic to normal ratios of 0.67 and 0.64, respectively). Kidney and testis, on the other hand, showed elevations of both UDP-glucose and UDP-galactose, with the diabetic levels being 1.2 to 1.3 those of normal levels. The direction of change in UDPglucose in a tissue appeared to reflect its known ability to synthesize glycogen in diabetes. The finding of elevated UDPglucose and UDP-galactose concentrations in diabetic kidney is considered to be potentially of great importance to the increased synthesis of basement membrane collagen by this tissue.

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“…The radiolabeled product formed by the UDP-glucose-dependent reaction had the same chromatographic mobility as authentic Glc-P-Do1 (lane D). The [ 3 2 P ] p h o~p h o g l~~~l i p i d was converted to Dold2P (lane C) by exposure to 0.1 M-HCI in 50% 1-propanol at 50" for 30 min, as observed for Glc-P-Do1 (Scher et al, 1977).…”

Section: Front-mentioning

confidence: 80%

“…Direct proof for the transfer of glucose from Glc-P-Do1 to dolicholbound oligosaccharides has also been obtained with membrane preparations from rat liver (Behrens et al, 1971), yeast (Parodi, 1976), Tetrahymena pyriformis (Keenan et al, 1975), and calf pancreas (Herscovics et al, 1977). Earlier in vitro studies have shown that the lipophilic glucosyl donor is formed by the reversible transfer of glucose from UDP-glucose to dolichyl monophosphate (Dol-P) in calf brain (Scher et al, 1977) as in extraneural tissues (Parodi and Leloir, 1979).…”

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confidence: 99%

Enzymatic Glucosylation of Dolichyl Monophosphate Formed Via Cytidine Triphosphate in Calf Brain Membranes

Scher

Burton

Waechter

1980

Journal of Neurochemistry

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When calf brain membrane preparations containing endogenous dolichyl [32P]monophosphate (Dol-32P), prelabeled enzymatically by [gamma-32P]-CTP, are incubated with unlabeled UDP-glucose, the formation of a mild acid-labile [32P]phosphoglucolipid is observed. The biosynthesis of the [32P]phosphoglucolipid is dependent on the concentration of UDP-glucose added, and no [32P]phosphoglycolipid appeared when UDP-glucose was replaced by ADP-glucose, UDP-xylose, UDP-galactose, UDP-mannose, or UDP-glucuronic acid. The 32P-labeled product formed by the UDP-glucose-dependent reaction is chemically and chromatographically identical to glucosylphosphoryldolichol. Several enzymatic parameters of the glucosylation of the specific pool of Dol-P, synthesized by the CTP-mediated kinase, and the total available pool of Dol-P have been compared by a double-label assay utilizing endogenous, prelabeled Dol-32P and UDP-[3H]glucose as substrates.

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Biosynthesis of glucosylated derivatives of dolichol: possible intermediates in the assembly of white matter glycoproteins

Cited by 42 publications

References 41 publications

Protein Glycosylation in Candida

Protein Glycosylation in Candida

Effect of diabetes on the sugar nucleotides in several tissues of the rat

Enzymatic Glucosylation of Dolichyl Monophosphate Formed Via Cytidine Triphosphate in Calf Brain Membranes

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