Structure of the lipid-linked oligosaccharides that accumulate in class E Thy-1-negative mutant lymphomas

Chapman, Ann E.; Trowbridge, Ian S.; Hyman, Robert; Kornfeld, Stuart

doi:10.1016/0092-8674(79)90259-9

Cited by 122 publications

(48 citation statements)

References 7 publications

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“…7e). The elution volumes of both these oligosaccharides correspond closely to those reported for similar lipid-linked saccharides from other mammalian cells (6,19,23).…”

Section: Methodssupporting

confidence: 81%

Involvement of Lipid-linked Oligosaccharides in Synthesis of Storage Glycoproteins in Soybean Seeds

Bailey

Deluca²,

Dürr³

et al. 1980

Plant Physiol.

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Membrane preparations from developing soybean (var. Prize) cotyledon tissue, at the time of synthesis of storage glycoproteins, catalyze the sequential assembly of lipid-linked oligosaccharides from uridine-5'-diphospho-N-acetyl-E-16_3Hlglucosamine and guanosine-5'-diphospho-n-IU-14Clmannose. The maximum size of lipid-linked oligosaccharide that accumulates contains the equivalent of 10 saccharide units on the basis of Bio-Gel P-2 gel filtration studies. These lipid-linked oligosaccharides show similar characteristics to polyisoprenyl diphosphate derivatives on diethylaminoethyl-cellulose chromatography and are potential intermediates in glycoprotein biosynthesis in this tissue. These glycolipids do not appear to turn over in pulse-chase experiments and no completed storage glycoproteins were detected among the products of these incubations. (2) and french bean (9, 12, 13) cotyledon tissue. Dolichyl phosphate has been purified from soybean and shown to act as an effective acceptor for glycosyl transfer from sugar nucleotides (5,22).Evidence that lipid-linked oligosaccharides can be assembled in a sequential manner from UDP-GlcNAc and GDP-mannose by membrane preparations from developing soybean cotyledons and that some of these, as in mammalian systems, may be involved in the synthesis of endogenous storage glycoproteins is presented here. Earlier studies in these laboratories have been concerned mainly with the assembly of glycolipids in growing tissue (pea stem) where glycoproteins do not accumulate (1, 10), and it was of particular interest to employ similar techniques with a tissue where a major part of metabolism is geared to the synthesis and deposition of glycoprotein. MATERIALS AND METHODSPlant Material. Soybean (Glycine max. var. Prize) was grown in Vermiculite with a 12-h photoperiod at 28 C (daytime) and 22 C (night). Plants were inoculated with Rhizobium japonicum and watered with N-free medium as described previously (27). Cotyledons were harvested when their fresh weight was between 100 and 250 mg.Membrane Isolation and Incubation. A membrane preparation was obtained from developing soybean cotyledons by modification of the method previously used in studies with pea stem tissue (1). The cotyledons were homogenized with a mortar and pestle at 4 C in 0.1 M Tris-HCl (pH 7.4) containing 5 mm dithioerythritol, 10 mM MgCl2 and 0.4 M sucrose, and the brei was filtered through Miracloth (Calbiochem). The filtrate was centrifuged at low speed (lOOOg for 10 min) and the pellet was dispersed for 20 s using a tissue homogenizer (Polytron, Brinkmann Instruments, at halfmaximum force). The homogenate was recentrifuged (lOOOg for 10 min) and the supernatant was combined with that from the previous centrifugation. A total membrane preparation was obtained from this supernatant by centrifugation at high speed (48,000g for 60 min).

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“…7e). The elution volumes of both these oligosaccharides correspond closely to those reported for similar lipid-linked saccharides from other mammalian cells (6,19,23).…”

Section: Methodssupporting

confidence: 81%

Involvement of Lipid-linked Oligosaccharides in Synthesis of Storage Glycoproteins in Soybean Seeds

Bailey

Deluca²,

Dürr³

et al. 1980

Plant Physiol.

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“…Because Con A appears to have a greater specificity for simple oligosaccharides (l8), the mutation conferring Con A resistance might involve some biosynthetic step exclusive for the mannose-rich chains . In fact, a similar phenomenon has been observed in the case of class E Thy 1 lymphoma cell mutants, in which an inability to synthesize mannosyldolicholphosphate results in abnormal lipid-linked oligosaccharide and resistance to Con A (7,8). When Sindbis virus (which contains both simple and complex oligosaccharides) was grown in these cells, only the 232 TIil JOURNAL Or CELL BIOLOGY " VOLUME 89, 1981 high mannose residues were affected (51).…”

Section: Infection Ofmentioning

confidence: 55%

Glycosylation does not determine segregation of viral envelope proteins in the plasma membrane of epithelial cells.

Green¹,

Meiss²,

Rodríguez-Boulan³

1981

The Journal of Cell Biology

106

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Enveloped viruses are excellent tools for the study of the biogenesis of epithelial polarity, because they bud asymmetrically from confluent monolayers of epithelial cells and because polarized budding is preceded by the accumulation of envelope proteins exclusively in the plasma membrane regions from which the viruses bud. In this work, three different experimental approaches showed that the carbohydrate moieties do not determine the final surface localization of either influenza (WSN strain) or vesicular stomatitis virus (VSV) envelope proteins in infected Madin-Darby Canine Kidney (MDCK) cells, as determined by immunofluorescence and immunoelectron microscopy, using ferritin as a marker. Infected concanavalin A- and ricin 1-resistant mutants of MDCK cells, with alterations in glycosylation, exhibited surface distributions of viral glycoproteins identical to those of the parental cell line, i.e., influenza envelope proteins were exclusively found in the apical surface, whereas VSV G protein was localized only in the basolateral region. MDCK cells treated with tunicamycin, which abolishes the glycosylation of viral glycoproteins, exhibited the same distribution of envelope proteins as control cells, after infection with VSF or influenza. A temperature-sensitive mutant of influenza WSN, ts3, which, when grown at the nonpermissive temperature of 39.5 degrees C, retains the sialic acid residues in the envelope glycoproteins, showed, at both 32 degrees C (permissive temperature) and 39.5 degrees C, budding polarity and viral glycoprotein distribution identical to those of the parental WSN strain, when grown in MDCK cells. These results demonstrate that carbohydrate moieties are not components of the addressing signals that determine the polarized distribution of viral envelope proteins, and possibly of the intrinsic cellular plasma membrane proteins, in the surface of epithelial cells.

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“…[2]. In this proposal, a structural characterization of the lipidlinked (Man)9(GlcNAc)z intermediate was not reported.…”

Section: 121mentioning

confidence: 94%

“…G l~~M a n~( G l c N A c )~ appears to serve a similar function in an alternative or a bypass pathway of biosynthesis 12-51. Both of the precursors have been structurally characterized [6,7] and an ordered sequence for their assembly in vivo was proposed [2]. However, several intermediates for the assembly of Glc3Man9(GlcNAc)2, when isolated from incubations of bovine mammary microsomes in vitro, were found to contain multiple isomers [8,9].…”

mentioning

confidence: 99%

Biosynthesis of Mammary Glycoproteins

Vijay

Perdew

1982

European Journal of Biochemistry

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The lipid-linked glucosyloligosaccharide intermediates for the biosynthesis of asparagine-linked glycoproteins in the lactating bovine mammary tissue were isolated from incubations of microsomes of this tissue with labeled sugar-nucleotides. These were shown to have the general structure (Glc)~ -3(Man)9(GlcNAc)z. A structural characterization indicated that glucose residues in these oligosaccharides are linked as Glcctl-+ 3, Glcal -+ 3Glcal --t 3, and Glcl-+ 2Glcal-+ 3Glcal-+ 3, to the tetramannosyl branch of (Man)9(GlcNAc)2 portion previously characterized as Manal + 2Manal+ 2Manal+ 3(Manal + 2Manixl+ 6[Manixl+ 2Manal+ 31-Manal

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Structure of the lipid-linked oligosaccharides that accumulate in class E Thy-1-negative mutant lymphomas

Cited by 122 publications

References 7 publications

Involvement of Lipid-linked Oligosaccharides in Synthesis of Storage Glycoproteins in Soybean Seeds

Involvement of Lipid-linked Oligosaccharides in Synthesis of Storage Glycoproteins in Soybean Seeds

Glycosylation does not determine segregation of viral envelope proteins in the plasma membrane of epithelial cells.

Biosynthesis of Mammary Glycoproteins

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