Differential fate of glycoproteins carrying a monoglucosylated form of truncated N-glycan in a new CHO line, MadIA214214, selected for a thermosensitive secretory defect

QUICK SEARCH:

[advanced]

	Author:		Keyword(s):

Home Help Feedback Subscriptions Archive Search Table of Contents

This Article

	Summary
	Full Text (PDF)
	Alert me when this article is cited
	Alert me if a correction is posted

Services

	Email this article to a friend
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new issues of the journal
	Download to citation manager


Citing Articles

	Citing Articles via HighWire
	Citing Articles via Google Scholar

Google Scholar

	Articles by Ermonval, M.
	Articles by Buttin, G.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Ermonval, M.
	Articles by Buttin, G.


Social Bookmarking

	What's this?

Allen, S., Naim, H. Y. and Bulleid, N. J (1995). Intracellular folding of tissue-type plasminogen activator. Effects of disulfide bond formation on N-linked glycosylation and secretion. J. Biol. Chem 270, 4797-4804.[Abstract/Free Full Text]

Ballow, J. P., Weissman, J. D. and Kearse, K. P (1995). Unique expression of major histocompatibility complex class I proteins in the absence of glucose trimming and calnexin association. J. Biol. Chem 270, 29025-29029.[Abstract/Free Full Text]

Beck, P. J., Gething, M. J., Sambrook, J. and Lehrman, M. A (1990). Complementing mutant alleles define three loci involved in mannosylation of Man5-GlcNAc2-P-P-dolichol in Chinese hamster ovary cells. Somatic Cell Mol. Genet 16, 539-548.[Medline]

Bellio, M., Lone, Y. C., Calle-Martin, O. d. l., Malissen, B., Abastado, J. B. and Kourilsky, P (1994). The V beta complementarity determining region 1 of major histocompatibility complex (MHC) class I-restricted T cell receptor is involved in the recognition of peptide/MHC I and superantigen/MHC II comlplex. J. Exp. Med 179, 1087-1097.[Abstract/Free Full Text]

Berger, J., Hauber, J., Hauber, R., Geiger, R. and Cullen, B. R (1988). Secreted placental alkaline phosphatase: a powerful new quantitative indicator of gene expression in eukaryotic cells. Gene 66, 1-10.[Medline]

Bonifacino, J. S. and Lippincott-Schwartz, J (1991). Degradation of proteins within the endoplasmic reticulum. Curr. Opin. Cell Biol 3, 592-600.[Medline]

Br\212ndli, A. W (1991). Mammalian glycosylation mutants as tools for the analysis and reconstitution of protein transport. Biochem. J 276, 1-12.

Cacan, R., Villers, C., Belard, M., Kaiden, A., Krag, S. S. and Verbert, A (1992). Different fates of the oligosaccharide moieties of lipid intermediates. Glycobiology 2, 127-136.[Abstract/Free Full Text]

Cacan, R., Labiau, O., Mir, A. M. and Verbert, A (1993). Effect of cell attachment and growth on the synthesis and fate of dolichol-linked oligosaccharides in Chinese hamster ovary cells. Eur. J. Biochem 215, 873-881.[Medline]

Casanova, J.-L., Cerottini, J.-C., Matthes, M., Necker, A., Gourmier, H., Barra, C., Wiedman, C., MacDonald, H. R., Lemonnier, F., Malissen, B. et al (1992). H-2 restricted cytolytic T lymphocytes specific for HLA display T cell receptors of limited diversity. J. Exp. Med 176, 439-447.[Abstract/Free Full Text]

Chapman, A., Fujimoto, K. and Kornfeld, S (1980). The primary glycosylation defect in class E Thy-1-negative mutant mouse lymphoma cells is an inability to synthesize dolichol-P-mannose. J. Biol. Chem 255, 4441-4446.[Free Full Text]

Doms, R. W., Russ, G. and Yewdell, J. W (1989). Brefeldin A redistributes resident and itinerant Golgi proteins to the endoplasmic reticulum. J. Cell Biol 109, 61-72.[Abstract/Free Full Text]

Fiedler, K. and Simons, K (1995). The role of N-glycans in the secretory pathway. Cell 81, 309-312.[Medline]

Gorgas, K (1985). Serial section analysis of mouse hepatic peroxisomes. Anat. Embryol 172, 21-32.[Medline]

Hammond, C., Braakman, I. and Helenius, A (1994). Role of N-linked oligosaccharide recognition, glucose trimming and calnexin in glycoprotein folding and quality control. Proc. Nat. Acad. Sci. USA 91, 913-917.[Abstract/Free Full Text]

Hammond, C. and Helenius, A (1994). Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment and Golgi apparatus. J. Cell Biol 126, 41-52.[Abstract/Free Full Text]

Hammond, C. and Helenius, A (1994). Folding of VSV G protein: sequential interaction with BiP and calnexin. Science 266, 456-458.[Abstract/Free Full Text]

Hearing, J., Gething, M.-J. and Sambrook, J (1989). Addition of truncated oligosaccharides to influenza virus hemagglutinin results in its temperature-conditional cell surface expression. J. Cell Biol 108, 355-365.[Abstract/Free Full Text]

Hirschberg, C. B. and Snider, M. D (1987). Topography of glycosylation in the rough endoplasmic reticulum and Golgi apparatus. Annu. Rev. Biochem 56, 63-87.[Medline]

Huffaker, T. C. and Robbins, P. W (1983). Yeast mutants deficient in protein glycosylation. Proc. Nat. Acad. Sci. USA 80, 7466-7470.[Abstract/Free Full Text]

Jaulin, C., Casanova, J.-L., Romero, P., Luescher, I., Cordey, A.-S., Maryanski, J. L. and Kourilsky, P (1992). Highly diverse T cell recognition of a single Plasmodium berghei peptide presented by a series of mutant H-2Kdmolecules. J. Immunol 149, 3990-3994.[Abstract]

Johannsson, A., Ellis, D. H., Bates, D. L., Plumb, A. M. and Stanley, C. J (1986). Enzyme amplification for immunoassays: detection limit of one hundredth of an attomole. J. Immunol. Meth 87, 7-11.[Medline]

Kim, P. S. and Arvan, P (1995). Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum. J. Cell Biol 128, 29-38.[Abstract/Free Full Text]

Kmiecik, D., Herman, V., Stroop, C. J. M., Michalski, J.-C., Mir, A.-M., Labiau, O., Verbert, A. and Cacan, R (1995). Catabolism of glycan moieties of lipid intermediates leads to a single Man5GlcNAc oligosaccharide isomer: a study with permeabilized CHO cells. Glycobiology 5, 483-494.[Abstract/Free Full Text]

Knittler, M. R. and Haas, I. G (1992). Interaction of BiP with newly synthesized immunoglobulin light chain molecules: cycles of sequential binding and release. EMBO J 11, 1573-1581.[Medline]

Knittler, M. R., Dirks, S. and Haas, I. G (1995). Molecular chaperones involved in protein degradation in the endoplasmic reticulum: Quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum. Proc. Nat. Acad. Sci. USA 92, 1764-1768.[Abstract/Free Full Text]

Kornfeld, R. and Kornfeld, S (1985). Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem 54, 631-664.[Medline]

Krasnewich, D. M., Holt, G. D., Brantly, M., Skovby, F., Redwine, J. and Gahl, W. A (1995). Abnormal synthesis of dolichol-linked oligosaccharides in carbohydrate-deficient glycoprotein syndrome. Glycobiology 5, 503-510.[Abstract/Free Full Text]

Landegren, U (1984). Measurement of cell numbers by means of the endogenous enzyme hexosaminidase. Applications for detection of lymphokines and cell surface antigens. J. Immunol. Meth 67, 379-388.[Medline]

Lehrman, M. A. and Zeng, Y (1989). Pleiotropic resistance to glycoprotein processing inhibitors in Chinese hamster ovary cells. J. Biol. Chem 264, 1584-1593.[Abstract/Free Full Text]

Lubas, W. A. and Spiro, R. G (1987). Golgi endo--D-mannosidase from rat liver, a novel N-linked carbohydrate unit processing enzyme. J. Biol. Chem 262, 3775-3781.[Abstract/Free Full Text]

Marquardt, T., Ulrich, K., Zimmer, P., Asilik, A., Deufel, T. and Harms, E (1995). Carbohydrate-deficient glycoprotein syndrome (CDGS)-glycosylation, folding and intracellular transport of newly synthesized glycoproteins. Eur. J. Cell Biol 66, 268-273.[Medline]

Orlean, P (1992). Enzymes that recognize dolichols participate in three glycosylation pathways and are required for protein secretion. Biochem. Cell Biol 70, 438-447.[Medline]

Ozato, K. and Sachs, D. H (1981). Monoclonal antibodies to mouse MHC antigens. J. Immunol 126, 317-.[Abstract]

Pelham, H. R. B (1989). Control of protein exit from the endoplasmic reticulum. Annu. Rev. Cell Biol 5, 1-23.

Plutner, H., Davidson, H. W., Saraste, J. and Balch, W. E (1992). Morphological analysis of protein transport from the ER to Golgi membranes in digitonin-permeabilized cells: role of P58 containing compartment. J. Cell Biol 119, 1097-1116.[Abstract/Free Full Text]

Rock, K. L., Gramm, C. and Benacerraf, B (1991). Low temperature and peptides favor the formation of class I heterodimers on RMA-S cells at the cell surface. Proc. Nat. Acad. Sci. USA 88, 4200-4204.[Abstract/Free Full Text]

Roos, J., Sternglanz, R. and Lennarz, W. J (1994). A screen for yeastmutants with defects in the dolichol-mediated pathway for N-glycosylation. Proc. Nat. Acad. Sci. USA 91, 1485-1489.[Abstract/Free Full Text]

Rose, J. K. and Doms, R. W (1988). Regulation of protein export from the endoplasmic reticulum. Annu. Rev. Cell Biol 4, 257-288.

Rosenwald, A. G. and Krag, S. S (1990). Lec9 CHO glycosylation mutants are defective in the synthesis of dolichol. J. Lipid Res 31, 523-533.[Abstract]

Rothman, J. E (1994). Mechanisms of intracellular protein transport. Nature 372, 55-63.[Medline]

Rubocki, R. J., Connolly, J. M., Hansen, T. D., Melvold, R. W., Kim, B. S., Hildebrand, W. H. and Martinko, J (1991). Mutation at amino acid position 133 of H-2Kdprevents2microglobulin association and immune recognition but not surface expression. J. Immunol 146, 2352-2357.[Abstract]

Self, C. H (1985). Enzyme amplification- a general method applied to provide an immunoassisted assay for placental alkaline phosphatase. J. Immunol. Meth 76, 389-393.[Medline]

Sitia, R. and Meldolesi, J (1992). Endoplasmic reticulum: a dynamic patchwork of specialized subregions. Mol. Biol. Cell 3, 1067-1072.[Medline]

Sousa, M. and Parodi, A. J (1995). The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc: glycoprotein glucosyltransferase. EMBO J 14, 4196-4203.[Medline]

Stanley, P (1987). Glycosylation mutants and the functions of mammalian carbohydrates. Trends Genet 3, 77-81.

Stoll, J., Robbins, A. R. and Krag, S. S (1982). Mutant of Chinese hamster ovary cells with altered mannose 6-phosphate receptor activity is unable to synthesize mannosylphosphoryldolichol. Proc. Nat. Acad. Sci. USA 79, 2296-2300.[Abstract/Free Full Text]

Thomas, P. J., Qu, B.-H. and Pedersen, P. L (1995). Defective protein folding as a basis of human disease. Trends Biochem. Sci 20, 456-459.[Medline]

Towsend, A. T., Eliott, T., Cerundolo, V., Foster, I., Barber, B. and Tse, A (1990). Assembly of MHC class I molecules analyzed in vitro. Cell 62, 285-295.[Medline]

Varki, A (1993). Biological roles of oligosaccharides: all of the theories are correct. Glycobiol 3, 97-130.[Abstract/Free Full Text]

Villers, C., Cacan, R., Mir, A.-M., Labiau, O. and Verbert, A (1994). Release of oligomannoside-type glycans as a marker of the degradation of newly synthesized glycoproteins. Biochem. J 298, 135-142.

Ware, F. E., Vassilakos, A., Peterson, P. A., Jackson, M. R., Lehrman, M. A. and Williams, D. B (1995). The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins. J. Biol. Chem 270, 4697-4704.[Abstract/Free Full Text]

Ware, F. E. and Lehrman, M. A (1996). Expression cloning of a novel suppressor of the Lec15 and Lec35 glycosylation mutations of Chinese hamster ovary cells. J. Biol. Chem 271, 13935-13938.[Abstract/Free Full Text]

Yamashita, K., Ideo, H., Ohkura, T., Fukushima, K., Yuasa, I., Ohno, K. and Takeshita, K (1993). Sugar chains of serum transferrin from patients with carbohydrate deficient glycoprotein syndrome. J. Biol. Chem 268, 5783-5789.[Abstract/Free Full Text]

Zeng, Y. C. and Lehrman, M. A (1990). A block at Man5GlcNAc2-pyrophosphoryldolichol in intact but not disrupted castanospermine and swainsonine-resistant Chinese hamster ovary cells. J. Biol. Chem 265, 2296-2305.[Abstract/Free Full Text]

CiteULike

Complore

Connotea

Del.icio.us Add to Digg

Digg

Technorati

Twitter What's this?

This article has been cited by other articles:

X. Wang, R. P. Rao, T. Kosakowska-Cholody, M. A. Masood, E. Southon, H. Zhang, C. Berthet, K. Nagashim, T. K. Veenstra, L. Tessarollo, et al.
Mitochondrial degeneration and not apoptosis is the primary cause of embryonic lethality in ceramide transfer protein mutant mice
J. Cell Biol., January 12, 2009; 184(1): 143 - 158.
[Abstract] [Full Text] [PDF]

M. Henquet, L. Lehle, M. Schreuder, G. Rouwendal, J. Molthoff, J. Helsper, S. van der Krol, and D. Bosch
Identification of the Gene Encoding the {alpha}1,3-Mannosyltransferase (ALG3) in Arabidopsis and Characterization of Downstream N-Glycan Processing
PLANT CELL, June 1, 2008; 20(6): 1652 - 1664.
[Abstract] [Full Text] [PDF]

H. Ashida, Y. Maeda, and T. Kinoshita
DPM1, the Catalytic Subunit of Dolichol-phosphate Mannose Synthase, Is Tethered to and Stabilized on the Endoplasmic Reticulum Membrane by DPM3
J. Biol. Chem., January 13, 2006; 281(2): 896 - 904.
[Abstract] [Full Text] [PDF]

E. S. Trombetta
The contribution of N-glycans and their processing in the endoplasmic reticulum to glycoprotein biosynthesis
Glycobiology, September 1, 2003; 13(9): 77R - 91R.
[Abstract] [Full Text] [PDF]

S. Duvet, A. Op De Beeck, L. Cocquerel, C. Wychowski, R. Cacan, and J. Dubuisson
Glycosylation of the hepatitis C virus envelope protein E1 occurs posttranslationally in a mannosylphosphoryldolichol-deficient CHO mutant cell line
Glycobiology, February 1, 2002; 12(2): 95 - 101.
[Abstract] [Full Text] [PDF]

M. Ermonval, C. Kitzmuller, A. M. Mir, R. Cacan, and N. E. Ivessa
N-glycan structure of a short-lived variant of ribophorin I expressed in the MadIA214 glycosylation-defective cell line reveals the role of a mannosidase that is not ER mannosidase I in the process of glycoprotein degradation
Glycobiology, July 1, 2001; 11(7): 565 - 576.
[Abstract] [Full Text] [PDF]

M. Anand, J. S. Rush, S. Ray, M.-A. Doucey, J. Weik, F. E. Ware, J. Hofsteenge, C. J. Waechter, and M. A. Lehrman
Requirement of the Lec35 Gene for All Known Classes of Monosaccharide-P-Dolichol-dependent Glycosyltransferase Reactions in Mammals
Mol. Biol. Cell, February 1, 2001; 12(2): 487 - 501.
[Abstract] [Full Text]

C. A. Jakob, P. Burda, J. Roth, and M. Aebi
Degradation of Misfolded Endoplasmic Reticulum Glycoproteins in Saccharomyces cerevisiae Is Determined by a Specific Oligosaccharide Structure
J. Cell Biol., September 7, 1998; 142(5): 1223 - 1233.
[Abstract] [Full Text] [PDF]

M. de Virgilio, H. Weninger, and N. E. Ivessa
Ubiquitination Is Required for the Retro-translocation of a Short-lived Luminal Endoplasmic Reticulum Glycoprotein to the Cytosol for Degradation by the Proteasome
J. Biol. Chem., April 17, 1998; 273(16): 9734 - 9743.
[Abstract] [Full Text] [PDF]

This Article

Summary

Full Text (PDF)

Alert me when this article is cited

Alert me if a correction is posted

Services

Email this article to a friend

Similar articles in this journal

Similar articles in PubMed

Alert me to new issues of the journal

Download to citation manager

Citing Articles

Citing Articles via HighWire

Citing Articles via Google Scholar

Google Scholar

Articles by Ermonval, M.

Articles by Buttin, G.

Search for Related Content

PubMed

PubMed Citation

Articles by Ermonval, M.

Articles by Buttin, G.

Social Bookmarking

What's this?

				M. Henquet, L. Lehle, M. Schreuder, G. Rouwendal, J. Molthoff, J. Helsper, S. van der Krol, and D. Bosch Identification of the Gene Encoding the {alpha}1,3-Mannosyltransferase (ALG3) in Arabidopsis and Characterization of Downstream N-Glycan Processing PLANT CELL, June 1, 2008; 20(6): 1652 - 1664. [Abstract] [Full Text] [PDF]

				H. Ashida, Y. Maeda, and T. Kinoshita DPM1, the Catalytic Subunit of Dolichol-phosphate Mannose Synthase, Is Tethered to and Stabilized on the Endoplasmic Reticulum Membrane by DPM3 J. Biol. Chem., January 13, 2006; 281(2): 896 - 904. [Abstract] [Full Text] [PDF]

				E. S. Trombetta The contribution of N-glycans and their processing in the endoplasmic reticulum to glycoprotein biosynthesis Glycobiology, September 1, 2003; 13(9): 77R - 91R. [Abstract] [Full Text] [PDF]

				S. Duvet, A. Op De Beeck, L. Cocquerel, C. Wychowski, R. Cacan, and J. Dubuisson Glycosylation of the hepatitis C virus envelope protein E1 occurs posttranslationally in a mannosylphosphoryldolichol-deficient CHO mutant cell line Glycobiology, February 1, 2002; 12(2): 95 - 101. [Abstract] [Full Text] [PDF]

				M. Ermonval, C. Kitzmuller, A. M. Mir, R. Cacan, and N. E. Ivessa N-glycan structure of a short-lived variant of ribophorin I expressed in the MadIA214 glycosylation-defective cell line reveals the role of a mannosidase that is not ER mannosidase I in the process of glycoprotein degradation Glycobiology, July 1, 2001; 11(7): 565 - 576. [Abstract] [Full Text] [PDF]

				M. Anand, J. S. Rush, S. Ray, M.-A. Doucey, J. Weik, F. E. Ware, J. Hofsteenge, C. J. Waechter, and M. A. Lehrman Requirement of the Lec35 Gene for All Known Classes of Monosaccharide-P-Dolichol-dependent Glycosyltransferase Reactions in Mammals Mol. Biol. Cell, February 1, 2001; 12(2): 487 - 501. [Abstract] [Full Text]

				C. A. Jakob, P. Burda, J. Roth, and M. Aebi Degradation of Misfolded Endoplasmic Reticulum Glycoproteins in Saccharomyces cerevisiae Is Determined by a Specific Oligosaccharide Structure J. Cell Biol., September 7, 1998; 142(5): 1223 - 1233. [Abstract] [Full Text] [PDF]

				M. de Virgilio, H. Weninger, and N. E. Ivessa Ubiquitination Is Required for the Retro-translocation of a Short-lived Luminal Endoplasmic Reticulum Glycoprotein to the Cytosol for Degradation by the Proteasome J. Biol. Chem., April 17, 1998; 273(16): 9734 - 9743. [Abstract] [Full Text] [PDF]