Proteoglycans: pericellular and cell surface multireceptors that integrate external stimuli in the mammary gland.

2.50
Hdl Handle:
http://hdl.handle.net/10541/85569
Title:
Proteoglycans: pericellular and cell surface multireceptors that integrate external stimuli in the mammary gland.
Authors:
Delehedde, Maryse; Lyon, Malcolm; Sergeant, Nicolas; Rahmoune, Hassan; Fernig, David G
Abstract:
Proteoglycans consist of a core protein and an associated glycosaminoglycan (GAG) chain of heparan sulfate, chondroitin sulfate, dermatan sulfate or keratan sulfate, which are attached to a serine residue. The core proteins of cell surface proteoglycans may be transmembrane, e.g., syndecan, or GPI-anchored, e.g., glypican. Many different cell surface and matrix proteoglycan core proteins are expressed in the mammary gland and in mammary cells in culture. The level of expression of these core proteins, the structure of their GAG chains, and their degradation are regulated by many of the effectors that control the development and function of the mammary gland. Regulatory proteins of the mammary gland that bind GAG include many growth factors and morphogens (fibroblast growth factors, hepatocyte growth factor/scatter factor, members of the midkine family, wnts), matrix proteins (collagen, fibronectin, and laminin), enzymes (lipoprotein lipase) and microbial surface proteins. Structural diversity within GAG chains ensures that each protein-GAG interaction is as specific as necessary and a number of sequences of saccharides that recognize individual proteins have been elucidated. The GAG-protein interactions serve to regulate the signal output of growth factor receptor tyrosine kinase and hence cell fate as well as the storage and diffusion of extracellular protein effectors. In addition, GAGs clearly coordinate stromal and epithelial development, and they are active participants in mediating cell-cell and cell-matrix interactions. Since a single proteoglycan, even if it carries a single GAG chain, can bind multiple proteins, proteoglycans are also likely to act as multireceptors which promote the integration of cellular signals.
Affiliation:
School of Biological Sciences, University of Liverpool, United Kingdom.
Citation:
Proteoglycans: pericellular and cell surface multireceptors that integrate external stimuli in the mammary gland. 2001, 6 (3):253-73 J Mammary Gland Biol Neoplasia
Journal:
Journal of Mammary Gland Biology and Neoplasia
Issue Date:
Jul-2001
URI:
http://hdl.handle.net/10541/85569
PubMed ID:
11547896
Type:
Article
Language:
en
ISSN:
1083-3021
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorDelehedde, Maryseen
dc.contributor.authorLyon, Malcolmen
dc.contributor.authorSergeant, Nicolasen
dc.contributor.authorRahmoune, Hassanen
dc.contributor.authorFernig, David Gen
dc.date.accessioned2009-11-06T15:23:03Z-
dc.date.available2009-11-06T15:23:03Z-
dc.date.issued2001-07-
dc.identifier.citationProteoglycans: pericellular and cell surface multireceptors that integrate external stimuli in the mammary gland. 2001, 6 (3):253-73 J Mammary Gland Biol Neoplasiaen
dc.identifier.issn1083-3021-
dc.identifier.pmid11547896-
dc.identifier.urihttp://hdl.handle.net/10541/85569-
dc.description.abstractProteoglycans consist of a core protein and an associated glycosaminoglycan (GAG) chain of heparan sulfate, chondroitin sulfate, dermatan sulfate or keratan sulfate, which are attached to a serine residue. The core proteins of cell surface proteoglycans may be transmembrane, e.g., syndecan, or GPI-anchored, e.g., glypican. Many different cell surface and matrix proteoglycan core proteins are expressed in the mammary gland and in mammary cells in culture. The level of expression of these core proteins, the structure of their GAG chains, and their degradation are regulated by many of the effectors that control the development and function of the mammary gland. Regulatory proteins of the mammary gland that bind GAG include many growth factors and morphogens (fibroblast growth factors, hepatocyte growth factor/scatter factor, members of the midkine family, wnts), matrix proteins (collagen, fibronectin, and laminin), enzymes (lipoprotein lipase) and microbial surface proteins. Structural diversity within GAG chains ensures that each protein-GAG interaction is as specific as necessary and a number of sequences of saccharides that recognize individual proteins have been elucidated. The GAG-protein interactions serve to regulate the signal output of growth factor receptor tyrosine kinase and hence cell fate as well as the storage and diffusion of extracellular protein effectors. In addition, GAGs clearly coordinate stromal and epithelial development, and they are active participants in mediating cell-cell and cell-matrix interactions. Since a single proteoglycan, even if it carries a single GAG chain, can bind multiple proteins, proteoglycans are also likely to act as multireceptors which promote the integration of cellular signals.en
dc.language.isoenen
dc.subject.meshBreast-
dc.subject.meshCell Communication-
dc.subject.meshCell Line-
dc.subject.meshCell Membrane-
dc.subject.meshFemale-
dc.subject.meshGrowth Substances-
dc.subject.meshHumans-
dc.subject.meshProteoglycans-
dc.subject.meshReceptors, Cell Surface-
dc.titleProteoglycans: pericellular and cell surface multireceptors that integrate external stimuli in the mammary gland.en
dc.typeArticleen
dc.contributor.departmentSchool of Biological Sciences, University of Liverpool, United Kingdom.en
dc.identifier.journalJournal of Mammary Gland Biology and Neoplasiaen
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