The transfer of mannose to dolichol diphosphate oligosaccharides in pig liver endoplasmic reticulum

Oliver, G.J.A.; Hemming, Frank W.

doi:10.1042/bj1520191

Cited by 42 publications

(10 citation statements)

References 15 publications

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“…4) (Table I) produced by the particulate fractions from GDP-mannose or UDP-GlcNAc supports this concept. Lipid-linked oligosaccharides have been implicated as precursors of the glycosyl component of glycoproteins (14,20,21). The time course kinetic data ( Fig.…”

Section: Resultsmentioning

confidence: 99%

Glycoprotein Biosynthesis in Cotyledons of Pisum sativum L

Beevers¹,

Mense²

1977

Plant Physiol.

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The reserve globulins, legumin and vicilin, in the pea cotyledon are glycoproteins. Acid hydrolysis of these glycoproteins releases the amino-sugar glucosamine and neutral sugars, principally mannose (2). Similar glycosyl components occur in the glycoproteins from animal tissues (16,27). Studies with extracts from animal tissues have established that the glycosyl components in the glycoproteins are derived originally from nucleotide sugars. The glycosyl components from the nucleotide sugars are transferred to lipid (polyisoprenol) intermediates to form lipidlinked monosaccharides which serve as precursors for the formation of lipid-linked oligosaccharides. This oligosaccharidelipid serves as the carrier of the oligosaccharide chain which combines with the polypeptide to produce glycoproteins (14,17). Similar lipid intermediates have been implicated in the biosynthesis of glycoproteins in shoots of mung bean seedlings (1,7,11), cotton fibers (6), and cotyledons of Phaseolus vulgaris (5).As part of our continuing studies of protein synthesis in the Beckman L2-65B centrifuge. The supernatant from this centrifugation was discarded and the surface of the remaining pellet was washed with reaction medium. Pellets were suspended in 3 ml of reaction mixture which, unless stated otherwise, consisted of 50 mm tris-HCl (pH 7) containing 10 mm KCI, 10 mm MgCI2, and 5 mm 2-mercaptoethanol. This suspension of cellular particulates was used as the enzyme source. Corporation). After a 60-min incubation at 37 C the reaction was terminated by the addition of 0.7 ml of H20 and 2.5 ml of chloroform-methanol (2:1, v/v). After thorough mixing the phases were separated by centrifugation and the lower organic phase recovered. The upper aqueous layer and interphase were reextracted with 2.5 ml of 2:1 chloroform-methanol; the organic phase was collected and pooled with the previous extraction.These pooled 2:1 chloroform-methanol fractions were then washed twice with 2.5 ml of chloroform-methanol-water (3:48:47). At each extraction the upper phase was discarded.The recovered washed 2:1 chloroform-methanol fraction was placed in a scintillation vial, evaporated to dryness, and radioactivity determined upon the addition of scintillation fluid (8 g 2,5-diphenyloxazole [PPOt in 2 liters of toluene, 1 liter of Triton X-100).The aqueous phase and interphase remaining after chloro-

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Section: Resultsmentioning

confidence: 99%

Glycoprotein Biosynthesis in Cotyledons of Pisum sativum L

Beevers¹,

Mense²

1977

Plant Physiol.

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“…Cell pellets were delipidated according to the procedure of Oliver and Hemming (1975). Delipidated material was exhaustively digested for 72 hr with pronase according to Muramatsu et al (1973).…”

Section: Preparation Of Cellular Glycopeptidesmentioning

confidence: 99%

Altered glycosylation of membrane glycoproteins in human uroepithelial cell lines

Debray

Zhu

Delannoy

et al. 1986

Intl Journal of Cancer

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Total cellular glycopeptides of 7 human uroepithelial cell lines that differ in the grade of transformation (TGr) were analysed by gel filtration and affinity chromatography on immobilized lectins. The 4 cell lines that are tumorigenic in nude mice and invasive in vitro (TGr III) possess more highly branched, tri- and tetraantennary N-acetyllactosaminic glycans, with less biantennary glycans than the 2 non-tumorigenic, noninvasive (TGr II) cell lines examined. The only exception to this general pattern is the third cell line, which is classified as TGr II. The cellular glycopeptide distribution pattern in this cell line is similar to that of the TGr III cells. The possible relationship between altered glycosylation of membrane glycoproteins and the expression of a malignant phenotype is discussed.

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“…This glycolipid was presumptively similar to that obtained by Brett and Leloir in plants [60] by elongation of a lipid 'pentasaccharide'. Oliver and Hemming [61] also described a 14C-labeled oligosaccharide corresponding in mobility to maltooligosaccharides of 8 -10 units. There is relatively more synthesis of lipid-bound trisaccharide and 'tetrasaccharide' in our system than in liver [8,11], aorta [62] and plants [I 5,59,60].…”

Section: Discussionmentioning

confidence: 99%

Lipid‐Bound Oligosaccharides in Insects

Allué

Belocopitow

1978

European Journal of Biochemistry

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Membrane preparations from immature stages of the fruit fly Ceratitis capitata catalyze the transfer of mannose from GDP-['4C]mannose into lipid-linked oligosaccharides. These compounds behave as polyprenyl derivatives and their formation is stimulated by the addition of an acidic glycolipid fraction isolated from insects.The mannose-labeled oligosaccharides are attached to the poly-isoprenol by a pyrophosphoryl linkage and can be released by mild acid hydrolysis. The trisaccharide lipid has been partially characterized. The results indicate that the compound is polyprenyl-pyrophosphate-N,N'-diacetylchitobiose-mannose.Incubation of dolichyl phosphate [14C]mannose or lower 14C-labeled oligosaccharide lipids with unlabeled GDP-mannose and the insect enzyme leads to the labeling of a higher lipid-bound oligosaccharide.When UDP-N-a~etyl['~C]glucosamine was incubated with insect membranes a '4C-labeled chitobiosyl lipid was synthesized. If unlabeled GDP-mannose was also present, the I4C label appeared in the trisaccharide and higher oligosaccharide lipids.Preliminary evidence indicates that the insect polyprenyl oligosaccharides described here might participate in glycoprotein biosynthesis.The role of polyprenylphosphates as glycosyl carriers in eucaryotic tissues is now well established [l-61. Evidence is being accumulated showing that dolichyl-bound saccharides are intermediates in the glycosylation of proteins in vertebrate [7 -141 plant [15,16] and fungal [17-211 systems. First, GlcNAc from UDP-GlcNAc is transferred to dolichyl-P. Then, N-acetylglucosamine and mannose are sequentially added from their respective sugar nucleotides yielding Dol-P-P-(GlcNAc)2-Man [22] which can undergo additional mannosylations [S, 11,221. Some of these mannose residues probably came from Dol-PMan which, in turn, is formed through the reaction of dolichyl-P with GDP-Man 123 -251. The last step is the transfer of the oligosaccharide from dolichyl-P-P derivatives to the polypeptide chains. The transfer of ['4C]mannose-labeled oligosaccharides has been described in yeast [26] and in vertebrate systems [8 -l l , 27,281.The amino acid involved in the protein-saccharide linkage is presumably asparagine because the sequence N,N'-diacetylchitobiose-mannose has always been found linked to it [29]. ~_ _ _Abbreviations. GlcNAc, N-acetylglucosamine; Dol, dolichyl ; Man, mannose; dolichyl-P. dolichyl moiiophosphate; dolichyl-P-P, dolichyl diphosphate.Enzyme. Streptomyes griseus protease or streptococcal proteinase (EC 3.4.22.10).It has been recently reported that dolichol [30,31], dolichyl phosphate [32] and dolichyl derivatives [33,34] occur in pluricellular invertebrates, but little is known about the mechanisms involved in protein glycosylation in those metazoan phyla [35].We previously reported the transfer of glucose, mannose and N-acetylglucosamine from their respective nucleotides to an endogenous polyprenyl phosphate catalyzed ip2 vitro by an insect extract [33,36]. These reactions could be stimulated by the addition of insect or pig li...

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The transfer of mannose to dolichol diphosphate oligosaccharides in pig liver endoplasmic reticulum

Cited by 42 publications

References 15 publications

Glycoprotein Biosynthesis in Cotyledons of Pisum sativum L

Glycoprotein Biosynthesis in Cotyledons of Pisum sativum L

Altered glycosylation of membrane glycoproteins in human uroepithelial cell lines

Lipid‐Bound Oligosaccharides in Insects

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