Proteoglycans: pericellular and cell surface multireceptors that integrate external stimuli in the mammary gland.
AffiliationSchool of Biological Sciences, University of Liverpool, United Kingdom.
MetadataShow full item record
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.
CitationProteoglycans: pericellular and cell surface multireceptors that integrate external stimuli in the mammary gland. 2001, 6 (3):253-73 J Mammary Gland Biol Neoplasia
JournalJournal of Mammary Gland Biology and Neoplasia
- Transforming growth factor (type beta) promotes the addition of chondroitin sulfate chains to the cell surface proteoglycan (syndecan) of mouse mammary epithelia.
- Authors: Rapraeger A
- Issue date: 1989 Nov
- Matrix glycosaminoglycans in the growth phase of fibroblasts: more of the story in wound healing.
- Authors: Kosir MA, Quinn CC, Wang W, Tromp G
- Issue date: 2000 Jul
- Chondroitin sulfate chains on syndecan-1 and syndecan-4 from normal murine mammary gland epithelial cells are structurally and functionally distinct and cooperate with heparan sulfate chains to bind growth factors. A novel function to control binding of midkine, pleiotrophin, and basic fibroblast growth factor.
- Authors: Deepa SS, Yamada S, Zako M, Goldberger O, Sugahara K
- Issue date: 2004 Sep 3
- Interactions of neural glycosaminoglycans and proteoglycans with protein ligands: assessment of selectivity, heterogeneity and the participation of core proteins in binding.
- Authors: Herndon ME, Stipp CS, Lander AD
- Issue date: 1999 Feb
- Differential expression of cell surface heparan sulfate proteoglycans in human mammary epithelial cells and lung fibroblasts.
- Authors: Lories V, Cassiman JJ, Van den Berghe H, David G
- Issue date: 1992 Jan 15