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J. Cell Biol. Sep (2006); 174(7):1097-106
Heparanase deglycanation of syndecan-1 is required for binding of the epithelial-restricted prosecretory mitogen lacritin-
Ma P, Beck SL, Raab RW, McKown RL, Coffman GL, Utani A, Chirico WJ, Rapraeger AC, Laurie GW
Department of Cell Biology, University of Virginia, Charlottesville, VA 22908, USA-
Abstract: Cell surface heparan sulfate -HS- proteoglycans are carbohydrate-rich regulators of cell migratory, mitogenic, secretory, and inflammatory activity that bind and present soluble heparin-binding growth factors -e-g-, fibroblast growth factor, Wnt, Hh, transforming growth factor beta, amphiregulin, and hepatocyte growth factor- to their respective signaling receptors- We demonstrate that the deglycanated core protein of syndecan-1 -SDC1- and not HS chains nor SDC2 or -4, appears to target the epithelial selective prosecretory mitogen lacritin- An important and novel step in this mechanism is that binding necessitates prior partial or complete removal of HS chains by endogenous heparanase- This limits lacritin activity to sites where heparanase appears to predominate, such as sites of exocrine cell migration, secretion, renewal, and inflammation- Binding is mutually specified by lacritin's C-terminal mitogenic domain and SDC1's N terminus- Heparanase modification of the latter transforms a widely expressed HS proteoglycan into a highly selective surface-binding protein- This novel example of cell specification through extracellular modification of an HS proteoglycan has broad implications in development, homeostasis, and disease-
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Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers.
Nucleic Acids Res. Jan 1;34:D535-9.