Document Detail


The cellular microenvironment and cell adhesion: a role for O-glycosylation.
MedLine Citation:
PMID:  21265808     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Glycosylation is one of the most abundant protein modifications in Nature, having roles in protein stability, secretion and function. Alterations in mucin-type O-glycosylation are responsible for a number of human diseases and developmental defects, as well as associated with certain types of cancer. However, the mechanistic role of this form of glycosylation in many of these instances is unclear. Here we describe how one glycosyltransferase responsible for initiating mucin-type O-glycosylation (PGANT3), specifically modulates integrin-mediated cell adhesion by influencing the secretion and localization of an integrin ligand. The integrin ligand Tiggrin, is normally O-glycosylated and localized to the basal matrix, where adhesion of two opposing cell layers takes place. In pgant3 mutants, Tiggrin is no longer O-glycosylated and fails to be properly secreted to the basal cell layer interface, resulting in disruption of proper cell adhesion. pgant3-mediated effects are dependent on the enzymatic activity of PGANT3 and cannot be rescued by another pgant family member, indicating a unique role for this glycosyltransferase. These results provide in vivo evidence for the role of O-glycosylation in the secretion of specific extracellular matrix proteins, which thereby influences the composition of the cellular 'microenvironment' and modulates cell adhesion events. The studies described in this review provide insight into the long-standing association between aberrant O-glycosylation and tumorigenesis, as changes in tumour environment and cell adhesion are hallmarks of cancer progression.
Authors:
Liping Zhang; Kelly G Ten Hagen
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Intramural; Review    
Journal Detail:
Title:  Biochemical Society transactions     Volume:  39     ISSN:  1470-8752     ISO Abbreviation:  Biochem. Soc. Trans.     Publication Date:  2011 Jan 
Date Detail:
Created Date:  2011-01-26     Completed Date:  2011-04-26     Revised Date:  2013-06-30    
Medline Journal Info:
Nlm Unique ID:  7506897     Medline TA:  Biochem Soc Trans     Country:  England    
Other Details:
Languages:  eng     Pagination:  378-82     Citation Subset:  IM    
Affiliation:
Developmental Glycobiology Unit, NIDCR, National Institutes of Health, Bethesda, MD 20892-4370, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cell Adhesion / physiology*
Drosophila Proteins / chemistry,  genetics,  metabolism
Drosophila melanogaster / anatomy & histology,  physiology
Extracellular Matrix / metabolism
Extracellular Matrix Proteins / chemistry,  genetics,  metabolism
Glycosylation
Glycosyltransferases / genetics,  metabolism
Humans
Integrins / genetics,  metabolism
Mutation
N-Acetylgalactosaminyltransferases / genetics,  metabolism
Neoplasms / chemistry,  metabolism,  pathology
Transgenes
Wing / growth & development
Grant Support
ID/Acronym/Agency:
ZIA DE000713-07/DE/NIDCR NIH HHS
Chemical
Reg. No./Substance:
0/Drosophila Proteins; 0/Extracellular Matrix Proteins; 0/Integrins; 0/Tig protein, Drosophila; EC 2.4.-/Glycosyltransferases; EC 2.4.-/Pgant3 protein, Drosophila; EC 2.4.1.-/N-Acetylgalactosaminyltransferases
Comments/Corrections

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