Literature DB >> 3015940

Rous sarcoma virus-transformed baby hamster kidney cells express higher levels of asparagine-linked tri- and tetraantennary glycopeptides containing [GlcNAc-beta (1,6)Man-alpha (1,6)Man] and poly-N-acetyllactosamine sequences than baby hamster kidney cells.

M Pierce, J Arango.   

Abstract

The alterations in complex-type N-linked oligosaccharides that can occur when an animal cell line is transformed by two dissimilar viruses were examined by comparing the N-linked oligosaccharides of baby hamster kidney (BHK) cells, metabolically radiolabeled with [2-3H]mannose, to the same class of oligosaccharides from BHK cells separately transformed by Rous sarcoma virus (RS-BHK), an RNA retrovirus, and polyoma virus (PY-BHK), a DNA papovavirus. Based on experiments that utilized serial lectin affinity chromatography, glycosidase digestions, and methylation analyses, both RS-BHK and PY-BHK cells demonstrated a significant increase in the relative amounts of tri- and tetraantennary complex-type N-linked oligosaccharides containing the branching sequence, [GlcNAc-beta(1,6)Man-alpha(1,6)Man], compared to the nontransformed BHK cells. In addition, almost all of the poly-N-acetyllactosamine sequence, [GlcNAc-beta(1,3)-Gal-beta(1,4)], was expressed on the tri- and tetraantennary N-linked oligosaccharides from BHK and RS-BHK cells that contain the sequence, [GlcNAc-beta(1,6)Man-beta(1,6)Man]. The increase in the relative amounts of this latter sequence in the transformed cells, therefore, most likely results in an increase in the amount of poly-N-acetyllactosamine sequence on the N-linked glycopeptides of these cells. The analysis of the degree of sialylation of the complex-type N-linked oligosaccharides from BHK and RS-BHK cells by ion exchange chromatography revealed no apparent differences, and in both of these cell types approximately 3% of the glycopeptide fraction radiolabeled with mannose was recovered in a highly negatively charged fraction that was identified by keratanase digestion to be keratan sulfate.

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Year:  1986        PMID: 3015940

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  54 in total

1.  N-linked oligosaccharides and metastatic propensity in in vivo selected mouse mammary adenocarcinoma cells.

Authors:  P J Seberger; E M Scholar; L Kelsey; W G Chaney; J E Talmadge
Journal:  Clin Exp Metastasis       Date:  1999-07       Impact factor: 5.150

Review 2.  From glycophenotyping by (plant) lectin histochemistry to defining functionality of glycans by pairing with endogenous lectins.

Authors:  Herbert Kaltner; Gabriel García Caballero; Anna-Kristin Ludwig; Joachim C Manning; Hans-Joachim Gabius
Journal:  Histochem Cell Biol       Date:  2018-05-05       Impact factor: 4.304

3.  Protein glycosylation in cancer biology: an overview.

Authors:  F Dall'olio
Journal:  Clin Mol Pathol       Date:  1996-06

4.  NMR structural characterization of substrates bound to N-acetylglucosaminyltransferase V.

Authors:  Megan A Macnaughtan; Maria Kamar; Gerardo Alvarez-Manilla; Andre Venot; John Glushka; J Michael Pierce; James H Prestegard
Journal:  J Mol Biol       Date:  2006-12-12       Impact factor: 5.469

5.  Upregulated β1-6 branch N-glycan marks early gliomagenesis but exhibited biphasic expression in the progression of astrocytic glioma.

Authors:  Arshad Ahmed Padhiar; Jianhui Fan; Ying Tang; Juanhan Yu; Shujing Wang; Linhua Liu; Bachir Niang; Max Efui Annani-Akollor; Lifen Wang; Qi Wang; Jianing Zhang
Journal:  Am J Cancer Res       Date:  2015-02-15       Impact factor: 6.166

Review 6.  A retrospective and prospective view of glycopathology.

Authors:  A Kobata
Journal:  Glycoconj J       Date:  1998-04       Impact factor: 2.916

Review 7.  Recent progress in the molecular biology of the cloned N-acetylglucosaminyltransferases.

Authors:  N Taniguchi; Y Ihara
Journal:  Glycoconj J       Date:  1995-12       Impact factor: 2.916

Review 8.  Perspectives on the significance of altered glycosylation of glycoproteins in cancer.

Authors:  Y J Kim; A Varki
Journal:  Glycoconj J       Date:  1997-08       Impact factor: 2.916

9.  α2,6 sialylation associated with increased beta 1,6-branched N-oligosaccharides influences cellular adhesion and invasion.

Authors:  Amit Ranjan; Rajiv D Kalraiya
Journal:  J Biosci       Date:  2013-12       Impact factor: 1.826

10.  Control of carbohydrate processing: increased beta-1,6 branching in N-linked carbohydrates of Lec9 CHO mutants appears to arise from a defect in oligosaccharide-dolichol biosynthesis.

Authors:  A G Rosenwald; P Stanley; S S Krag
Journal:  Mol Cell Biol       Date:  1989-03       Impact factor: 4.272

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