Heparan sulfate chains from glypican and syndecans bind the Hep II domain of fibronectin similarly despite minor structural differences.

Research output: Contribution to journalJournal articleResearchpeer-review

Standard

Heparan sulfate chains from glypican and syndecans bind the Hep II domain of fibronectin similarly despite minor structural differences. / Tumova, S; Woods, A; Couchman, J R.

In: Journal of Biological Chemistry, Vol. 275, No. 13, 2000, p. 9410-7.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Tumova, S, Woods, A & Couchman, JR 2000, 'Heparan sulfate chains from glypican and syndecans bind the Hep II domain of fibronectin similarly despite minor structural differences.', Journal of Biological Chemistry, vol. 275, no. 13, pp. 9410-7.

APA

Tumova, S., Woods, A., & Couchman, J. R. (2000). Heparan sulfate chains from glypican and syndecans bind the Hep II domain of fibronectin similarly despite minor structural differences. Journal of Biological Chemistry, 275(13), 9410-7.

Vancouver

Tumova S, Woods A, Couchman JR. Heparan sulfate chains from glypican and syndecans bind the Hep II domain of fibronectin similarly despite minor structural differences. Journal of Biological Chemistry. 2000;275(13):9410-7.

Author

Tumova, S ; Woods, A ; Couchman, J R. / Heparan sulfate chains from glypican and syndecans bind the Hep II domain of fibronectin similarly despite minor structural differences. In: Journal of Biological Chemistry. 2000 ; Vol. 275, No. 13. pp. 9410-7.

Bibtex

@article{931159e0597011dd8d9f000ea68e967b,
title = "Heparan sulfate chains from glypican and syndecans bind the Hep II domain of fibronectin similarly despite minor structural differences.",
abstract = "Numerous functions of heparan sulfate proteoglycans are mediated through interactions between their heparan sulfate glycosaminoglycan chains and extracellular ligands. Ligand binding specificity for some molecules, including many growth factors, is determined by complex heparan sulfate fine structure, where highly sulfated, iduronate-rich domains alternate with N-acetylated domains. Syndecan-4, a cell surface heparan sulfate proteoglycan, has a distinct role in cell adhesion, suggesting its chains may differ from those of other cell surface proteoglycans. To determine whether the specific role of syndecan-4 correlates with a distinct heparan sulfate structure, we have analyzed heparan sulfate chains from the different surface proteoglycans of a single fibroblast strain and compared their ability to bind the Hep II domain of fibronectin, a ligand known to promote focal adhesion formation through syndecan-4. Despite distinct molecular masses of glypican and syndecan glycosaminoglycans and minor differences in disaccharide composition and sulfation pattern, the overall proportion and distribution of sulfated regions and the affinity for the Hep II domain were similar. Therefore, adhesion regulation requires core protein determinants of syndecan-4.",
author = "S Tumova and A Woods and Couchman, {J R}",
note = "Keywords: Animals; Cells, Cultured; Chromatography, Gel; Chromatography, High Pressure Liquid; Chromatography, Ion Exchange; Electrophoresis, Agar Gel; Fibroblasts; Fibronectins; Heparan Sulfate Proteoglycans; Heparitin Sulfate; Membrane Glycoproteins; Protein Binding; Protein Conformation; Proteoglycans; Rats; Syndecans",
year = "2000",
language = "English",
volume = "275",
pages = "9410--7",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "13",

}

RIS

TY - JOUR

T1 - Heparan sulfate chains from glypican and syndecans bind the Hep II domain of fibronectin similarly despite minor structural differences.

AU - Tumova, S

AU - Woods, A

AU - Couchman, J R

N1 - Keywords: Animals; Cells, Cultured; Chromatography, Gel; Chromatography, High Pressure Liquid; Chromatography, Ion Exchange; Electrophoresis, Agar Gel; Fibroblasts; Fibronectins; Heparan Sulfate Proteoglycans; Heparitin Sulfate; Membrane Glycoproteins; Protein Binding; Protein Conformation; Proteoglycans; Rats; Syndecans

PY - 2000

Y1 - 2000

N2 - Numerous functions of heparan sulfate proteoglycans are mediated through interactions between their heparan sulfate glycosaminoglycan chains and extracellular ligands. Ligand binding specificity for some molecules, including many growth factors, is determined by complex heparan sulfate fine structure, where highly sulfated, iduronate-rich domains alternate with N-acetylated domains. Syndecan-4, a cell surface heparan sulfate proteoglycan, has a distinct role in cell adhesion, suggesting its chains may differ from those of other cell surface proteoglycans. To determine whether the specific role of syndecan-4 correlates with a distinct heparan sulfate structure, we have analyzed heparan sulfate chains from the different surface proteoglycans of a single fibroblast strain and compared their ability to bind the Hep II domain of fibronectin, a ligand known to promote focal adhesion formation through syndecan-4. Despite distinct molecular masses of glypican and syndecan glycosaminoglycans and minor differences in disaccharide composition and sulfation pattern, the overall proportion and distribution of sulfated regions and the affinity for the Hep II domain were similar. Therefore, adhesion regulation requires core protein determinants of syndecan-4.

AB - Numerous functions of heparan sulfate proteoglycans are mediated through interactions between their heparan sulfate glycosaminoglycan chains and extracellular ligands. Ligand binding specificity for some molecules, including many growth factors, is determined by complex heparan sulfate fine structure, where highly sulfated, iduronate-rich domains alternate with N-acetylated domains. Syndecan-4, a cell surface heparan sulfate proteoglycan, has a distinct role in cell adhesion, suggesting its chains may differ from those of other cell surface proteoglycans. To determine whether the specific role of syndecan-4 correlates with a distinct heparan sulfate structure, we have analyzed heparan sulfate chains from the different surface proteoglycans of a single fibroblast strain and compared their ability to bind the Hep II domain of fibronectin, a ligand known to promote focal adhesion formation through syndecan-4. Despite distinct molecular masses of glypican and syndecan glycosaminoglycans and minor differences in disaccharide composition and sulfation pattern, the overall proportion and distribution of sulfated regions and the affinity for the Hep II domain were similar. Therefore, adhesion regulation requires core protein determinants of syndecan-4.

M3 - Journal article

VL - 275

SP - 9410

EP - 9417

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 13

ER -

ID: 5163590