Literature DB >> 8806081

Syndecans, signaling, and cell adhesion.

J R Couchman1, A Woods.   

Abstract

Syndecans are transmembrane proteoglycans which can participate in diverse cell surface interactions, involving extracellular matrix macromolecules, growth factors, protease inhibitors, and even viral entry. Currently, all extracellular interactions are believed to be mediated by distinct structures within the heparan sulfate chains, leaving the roles of chondroitin sulfate chains and extracellular portion of the core proteins to be elucidated. Evidence that syndecans are a class of receptor involved in cell adhesion is mounting, and their small cytoplasmic domains may link with the microfilament cytoskeleton, thereby mediating signaling events. The molecular details are unknown, but the conservation of regions of syndecan cytoplasmic domains, and a strong tendency for homotypic association, support the idea that the ligand-induced clustering may be a discrete source of specific transmembrane signaling from matrix to cytoskeleton, as proposed for other classes of adhesion receptors.

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Year:  1996        PMID: 8806081     DOI: 10.1002/(sici)1097-4644(19960616)61:4<578::aid-jcb11>3.0.co;2-c

Source DB:  PubMed          Journal:  J Cell Biochem        ISSN: 0730-2312            Impact factor:   4.429


  19 in total

1.  Regulated expression and subcellular localization of syndecan heparan sulfate proteoglycans and the syndecan-binding protein CASK/LIN-2 during rat brain development.

Authors:  Y P Hsueh; M Sheng
Journal:  J Neurosci       Date:  1999-09-01       Impact factor: 6.167

2.  Basic fibroblast growth factor does not prevent heparan sulphate proteoglycan catabolism in intact cells, but it alters the distribution of the glycosaminoglycan degradation products.

Authors:  S Tumova; B A Hatch; D J Law; K J Bame
Journal:  Biochem J       Date:  1999-02-01       Impact factor: 3.857

3.  A practical approach to the detection of prognostically significant genomic aberrations in multiple myeloma.

Authors:  Zhong Chen; Bonnie Issa; Shiang Huang; Emily Aston; Jia Xu; Margaret Yu; Arthur R Brothman; Martha Glenn
Journal:  J Mol Diagn       Date:  2005-11       Impact factor: 5.568

Review 4.  Myofibroblast differentiation and survival in fibrotic disease.

Authors:  Kornelia Kis; Xiaoqiu Liu; James S Hagood
Journal:  Expert Rev Mol Med       Date:  2011-08-23       Impact factor: 5.600

5.  CGM1a antigen of neutrophils, a receptor of gonococcal opacity proteins.

Authors:  T Chen; E C Gotschlich
Journal:  Proc Natl Acad Sci U S A       Date:  1996-12-10       Impact factor: 11.205

6.  Expression of glypican-4 in haematopoietic-progenitor and bone-marrow-stromal cells.

Authors:  B Siebertz; G Stöcker; Z Drzeniek; S Handt; U Just; H D Haubeck
Journal:  Biochem J       Date:  1999-12-15       Impact factor: 3.857

7.  Cysteine-rich domain of human ADAM 12 (meltrin alpha) supports tumor cell adhesion.

Authors:  K Iba; R Albrechtsen; B J Gilpin; F Loechel; U M Wewer
Journal:  Am J Pathol       Date:  1999-05       Impact factor: 4.307

8.  Structural and functional changes in heparan sulfate proteoglycan expression associated with the myofibroblastic phenotype.

Authors:  Gareth Thomas; Aled Clayton; Janet Thomas; Malcolm Davies; Robert Steadman
Journal:  Am J Pathol       Date:  2003-03       Impact factor: 4.307

9.  Loss of heparan sulfate glycosaminoglycan assembly in podocytes does not lead to proteinuria.

Authors:  Shoujun Chen; Deborah J Wassenhove-McCarthy; Yu Yamaguchi; Lawrence B Holzman; Toin H van Kuppevelt; Guido J Jenniskens; Tessa J Wijnhoven; Ann C Woods; Kevin J McCarthy
Journal:  Kidney Int       Date:  2008-05-14       Impact factor: 10.612

Review 10.  Functional aspects of the interaction between interleukin-8 and sulfated glycosaminoglycans.

Authors:  Annelie Pichert; Denise Schlorke; Sandra Franz; Juergen Arnhold
Journal:  Biomatter       Date:  2012 Jul-Sep
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