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Functions of proteoglycans at the cell surface.

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Functions of proteoglycans at the cell surface. / Höök, M; Woods, A; Johansson, S; Kjellén, L; Couchman, J R.

I: Novartis Foundation Symposium, Bind 124, 1986, s. 143-57.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Höök, M, Woods, A, Johansson, S, Kjellén, L & Couchman, JR 1986, 'Functions of proteoglycans at the cell surface.', Novartis Foundation Symposium, bind 124, s. 143-57.

APA

Höök, M., Woods, A., Johansson, S., Kjellén, L., & Couchman, J. R. (1986). Functions of proteoglycans at the cell surface. Novartis Foundation Symposium, 124, 143-57.

Vancouver

Höök M, Woods A, Johansson S, Kjellén L, Couchman JR. Functions of proteoglycans at the cell surface. Novartis Foundation Symposium. 1986;124:143-57.

Author

Höök, M ; Woods, A ; Johansson, S ; Kjellén, L ; Couchman, J R. / Functions of proteoglycans at the cell surface. I: Novartis Foundation Symposium. 1986 ; Bind 124. s. 143-57.

Bibtex

@article{eba5ce10598411dd8d9f000ea68e967b,
title = "Functions of proteoglycans at the cell surface.",
abstract = "Proteoglycans (primarily heparan sulphate proteoglycans) are found at the surface of most adherent eukaryotic cells. Earlier studies suggest that these molecules can be associated with the cell surface principally by two different mechanisms. Proteoglycans may occur as membrane-intercalated glycoproteins, where the core protein of the proteoglycan is anchored in the lipid interior of the plasma membrane, or they may be bound via the polysaccharide components of the molecule to specific anchoring proteins present at the cell surface. A number of functions have been proposed for cell surface-associated proteoglycans, including: regulation of cell-substrate adhesion; regulation of cell proliferation; participation in the binding and uptake of extracellular components; and participation in the regulation of extracellular matrix formation. Evidence is discussed suggesting that the cell-associated heparan sulphate helps to connect the intracellular cytoskeleton to the extracellular matrix in focal adhesions. This evidence includes: the co-localization of actin and heparan sulphate proteoglycan during the process of cell spreading, and in isolated focal adhesions; biochemical analyses of a hydrophobic heparan sulphate proteoglycan from isolated focal adhesions; and the formation of focal adhesions on substrates made from isolated fibronectin fragments requires the presence of a heparan sulphate-binding site.",
author = "M H{\"o}{\"o}k and A Woods and S Johansson and L Kjell{\'e}n and Couchman, {J R}",
note = "Keywords: Animals; Cell Adhesion; Cell Membrane; Humans; Proteoglycans",
year = "1986",
language = "English",
volume = "124",
pages = "143--57",
journal = "Novartis Foundation Symposium",
issn = "1528-2511",
publisher = "JohnWiley & Sons Ltd",

}

RIS

TY - JOUR

T1 - Functions of proteoglycans at the cell surface.

AU - Höök, M

AU - Woods, A

AU - Johansson, S

AU - Kjellén, L

AU - Couchman, J R

N1 - Keywords: Animals; Cell Adhesion; Cell Membrane; Humans; Proteoglycans

PY - 1986

Y1 - 1986

N2 - Proteoglycans (primarily heparan sulphate proteoglycans) are found at the surface of most adherent eukaryotic cells. Earlier studies suggest that these molecules can be associated with the cell surface principally by two different mechanisms. Proteoglycans may occur as membrane-intercalated glycoproteins, where the core protein of the proteoglycan is anchored in the lipid interior of the plasma membrane, or they may be bound via the polysaccharide components of the molecule to specific anchoring proteins present at the cell surface. A number of functions have been proposed for cell surface-associated proteoglycans, including: regulation of cell-substrate adhesion; regulation of cell proliferation; participation in the binding and uptake of extracellular components; and participation in the regulation of extracellular matrix formation. Evidence is discussed suggesting that the cell-associated heparan sulphate helps to connect the intracellular cytoskeleton to the extracellular matrix in focal adhesions. This evidence includes: the co-localization of actin and heparan sulphate proteoglycan during the process of cell spreading, and in isolated focal adhesions; biochemical analyses of a hydrophobic heparan sulphate proteoglycan from isolated focal adhesions; and the formation of focal adhesions on substrates made from isolated fibronectin fragments requires the presence of a heparan sulphate-binding site.

AB - Proteoglycans (primarily heparan sulphate proteoglycans) are found at the surface of most adherent eukaryotic cells. Earlier studies suggest that these molecules can be associated with the cell surface principally by two different mechanisms. Proteoglycans may occur as membrane-intercalated glycoproteins, where the core protein of the proteoglycan is anchored in the lipid interior of the plasma membrane, or they may be bound via the polysaccharide components of the molecule to specific anchoring proteins present at the cell surface. A number of functions have been proposed for cell surface-associated proteoglycans, including: regulation of cell-substrate adhesion; regulation of cell proliferation; participation in the binding and uptake of extracellular components; and participation in the regulation of extracellular matrix formation. Evidence is discussed suggesting that the cell-associated heparan sulphate helps to connect the intracellular cytoskeleton to the extracellular matrix in focal adhesions. This evidence includes: the co-localization of actin and heparan sulphate proteoglycan during the process of cell spreading, and in isolated focal adhesions; biochemical analyses of a hydrophobic heparan sulphate proteoglycan from isolated focal adhesions; and the formation of focal adhesions on substrates made from isolated fibronectin fragments requires the presence of a heparan sulphate-binding site.

M3 - Journal article

C2 - 3816416

VL - 124

SP - 143

EP - 157

JO - Novartis Foundation Symposium

JF - Novartis Foundation Symposium

SN - 1528-2511

ER -

ID: 5167517