Literature DB >> 15157607

Variant glycosylation: an underappreciated regulatory mechanism for beta1 integrins.

Susan L Bellis1.   

Abstract

Although it has been known for many years that beta1 integrins undergo differential glycosylation in accordance with changes in cell phenotype, the potential role of N-glycosylation as a modulator of integrin function has received little attention. One reason for the relatively limited interest in this topic likely relates to the fact that much of the prior research was correlative in nature. However, new results now bolster the hypothesis that there is a causal relationship between variant glycosylation and altered integrin activity. In this review, the evidence for variant glycosylation as a regulatory mechanism for beta1 integrins are summarized, with particular emphasis on: (1). outlining the instances in which cell phenotypic variation is associated with differential beta1 glycosylation, (2). describing the specific alterations in glycan structure that accompany phenotypic changes and (3). presenting potential mechanisms by which variant glycosylation might regulate integrin function.

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Year:  2004        PMID: 15157607     DOI: 10.1016/j.bbamem.2004.03.012

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  59 in total

1.  Role of altered sialylation of the I-like domain of beta1 integrin in the binding of fibronectin to beta1 integrin: thermodynamics and conformational analyses.

Authors:  Di Pan; Yuhua Song
Journal:  Biophys J       Date:  2010-07-07       Impact factor: 4.033

2.  BIG1, a brefeldin A-inhibited guanine nucleotide-exchange protein, is required for correct glycosylation and function of integrin beta1.

Authors:  Xiaoyan Shen; Myoung-Soon Hong; Joel Moss; Martha Vaughan
Journal:  Proc Natl Acad Sci U S A       Date:  2007-01-16       Impact factor: 11.205

Review 3.  LDL receptor-related protein 1: unique tissue-specific functions revealed by selective gene knockout studies.

Authors:  Anna P Lillis; Lauren B Van Duyn; Joanne E Murphy-Ullrich; Dudley K Strickland
Journal:  Physiol Rev       Date:  2008-07       Impact factor: 37.312

4.  Proteolytic shedding of ST6Gal-I by BACE1 regulates the glycosylation and function of alpha4beta1 integrins.

Authors:  Alencia V Woodard-Grice; Alexis C McBrayer; John K Wakefield; Ya Zhuo; Susan L Bellis
Journal:  J Biol Chem       Date:  2008-07-23       Impact factor: 5.157

5.  N-glycosylation of the I-like domain of beta1 integrin is essential for beta1 integrin expression and biological function: identification of the minimal N-glycosylation requirement for alpha5beta1.

Authors:  Tomoya Isaji; Yuya Sato; Tomohiko Fukuda; Jianguo Gu
Journal:  J Biol Chem       Date:  2009-03-04       Impact factor: 5.157

6.  The morphologies of breast cancer cell lines in three-dimensional assays correlate with their profiles of gene expression.

Authors:  Paraic A Kenny; Genee Y Lee; Connie A Myers; Richard M Neve; Jeremy R Semeiks; Paul T Spellman; Katrin Lorenz; Eva H Lee; Mary Helen Barcellos-Hoff; Ole W Petersen; Joe W Gray; Mina J Bissell
Journal:  Mol Oncol       Date:  2007-06       Impact factor: 6.603

7.  Altered eosinophil profile in mice with ST6Gal-1 deficiency: an additional role for ST6Gal-1 generated by the P1 promoter in regulating allergic inflammation.

Authors:  Mehrab Nasirikenari; E V Chandrasekaran; Khushi L Matta; Brahm H Segal; Paul N Bogner; Amit A Lugade; Yasmin Thanavala; James J Lee; Joseph T Y Lau
Journal:  J Leukoc Biol       Date:  2009-12-09       Impact factor: 4.962

8.  Sialylation of beta1 integrins blocks cell adhesion to galectin-3 and protects cells against galectin-3-induced apoptosis.

Authors:  Ya Zhuo; Roger Chammas; Susan L Bellis
Journal:  J Biol Chem       Date:  2008-08-08       Impact factor: 5.157

9.  Galectin-3 is an important mediator of VEGF- and bFGF-mediated angiogenic response.

Authors:  Anna I Markowska; Fu-Tong Liu; Noorjahan Panjwani
Journal:  J Exp Med       Date:  2010-08-16       Impact factor: 14.307

10.  An N-glycosylation site on the beta-propeller domain of the integrin alpha5 subunit plays key roles in both its function and site-specific modification by beta1,4-N-acetylglucosaminyltransferase III.

Authors:  Yuya Sato; Tomoya Isaji; Michiko Tajiri; Shumi Yoshida-Yamamoto; Tsuyoshi Yoshinaka; Toshiaki Somehara; Tomohiko Fukuda; Yoshinao Wada; Jianguo Gu
Journal:  J Biol Chem       Date:  2009-03-09       Impact factor: 5.157

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