Literature DB >> 2658987

O-glycosylation pathway for mucin-type glycoproteins.

K L Carraway, S R Hull.   

Abstract

O-glycosylation is the post-translational process whereby carbohydrate is added to hydroxylated amino acids of proteins. The major O-glycosylation pathway in animal cells is involved in the synthesis of oligosaccharides linked by N-acetylgalactosamine to serine or threonine residues in 'mucin-type' proteins or their analogs. In this review, we discuss the evidence for the cellular localization of the biosynthetic steps in this pathway and propose a simplified, consensus version. We also propose variations of the simple pathway to account for its heterogeneity and variability in different cell types and differentiation states.

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Year:  1989        PMID: 2658987     DOI: 10.1002/bies.950100406

Source DB:  PubMed          Journal:  Bioessays        ISSN: 0265-9247            Impact factor:   4.345


  17 in total

Review 1.  Mammalian glycosylation mutants as tools for the analysis and reconstitution of protein transport.

Authors:  A W Brändli
Journal:  Biochem J       Date:  1991-05-15       Impact factor: 3.857

Review 2.  Structure, evolution, and biology of the MUC4 mucin.

Authors:  Pallavi Chaturvedi; Ajay P Singh; Surinder K Batra
Journal:  FASEB J       Date:  2007-11-16       Impact factor: 5.191

3.  Biochemical analysis of a bladder-cancer-associated mucin: structural features and epitope characterization.

Authors:  A Bergeron; H LaRue; Y Fradet
Journal:  Biochem J       Date:  1997-02-01       Impact factor: 3.857

Review 4.  The intrinsic disorder alphabet. III. Dual personality of serine.

Authors:  Vladimir N Uversky
Journal:  Intrinsically Disord Proteins       Date:  2015-03-17

Review 5.  Current status of mucins in the diagnosis and therapy of cancer.

Authors:  Satyanarayana Rachagani; Maria P Torres; Nicolas Moniaux; Surinder K Batra
Journal:  Biofactors       Date:  2009 Nov-Dec       Impact factor: 6.113

Review 6.  Review of the adenocarcinoma cell surface receptor for human alpha-fetoprotein; proposed identification of a widespread mucin as the tumor cell receptor.

Authors:  G J Mizejewski
Journal:  Tumour Biol       Date:  2013-02-28

7.  Polypeptide N-acetylgalactosaminyltransferase activity in tracheal epithelial microsomes.

Authors:  J M Cottrell; R L Hall; R G Sturton; P W Kent
Journal:  Biochem J       Date:  1992-04-01       Impact factor: 3.857

8.  Endoplasmic reticulum-through-Golgi transport assay based on O-glycosylation of native glycophorin in permeabilized erythroleukemia cells: role for Gi3.

Authors:  B S Wilson; G E Palade; M G Farquhar
Journal:  Proc Natl Acad Sci U S A       Date:  1993-03-01       Impact factor: 11.205

9.  Purification and characterization of two forms of beta-D-galactosidase from rat epididymal luminal fluid: evidence for their role in the modification of sperm plasma membrane glycoprotein(s).

Authors:  D R Tulsiani; M D Skudlarek; Y Araki; M C Orgebin-Crist
Journal:  Biochem J       Date:  1995-01-01       Impact factor: 3.857

Review 10.  Polymorphisms in mucin genes in the development of gastric cancer.

Authors:  Rong Wen; Fang Gao; Cheng-Jiang Zhou; Yan-Bin Jia
Journal:  World J Gastrointest Oncol       Date:  2015-11-15
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