Cell surface proteoglycan of mouse mammary epithelial cells is shed by cleavage of its matrix-binding ectodomain from its membrane-associated domain

doi:10.1083/jcb.105.6.3087

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Cell surface proteoglycan of mouse mammary epithelial cells is shed by cleavage of its matrix-binding ectodomain from its membrane-associated domain

M Jalkanen, A Rapraeger, S Saunders and M Bernfield
Department of Pediatrics, Stanford University School of Medicine, California 94305.

The cell surface proteoglycan on normal murine mammary gland (NMuMG) epithelial cells consists of a lipophilic domain, presumably intercalated into the plasma membrane, and an ectodomain that binds via its glycosaminoglycan chains to matrix components, is released intact by proteases and is detected by monoclonal antibody 281-2. The antibody 281-2 also detects a proteoglycan in the culture medium conditioned by NMuMG cells. This immunoactive proteoglycan was purified to homogeneity using DEAE-cellulose chromatography, isopycnic centrifugation, and 281- 2 affinity chromatography. Comparison of the immunoreactive medium proteoglycan with the trypsin-released ectodomain revealed that these proteoglycans are indistinguishable by several criteria as both: (a) contain heparan sulfate and chondroitin sulfate chains; and (b) are similar in hydrodynamic size and buoyant density; (c) have the same size core protein (Mr approximately 53 kD); (d) are nonlipophilic as studied by liposomal intercalation and transfer to silicone-treated paper. Kinetic studies of the release of proteoglycan from the surface of suspended NMuMG cells are interpreted to indicate that the immunoreactive medium proteoglycan is derived directly from the cell surface proteoglycan. Suspension of the cells both augments the release and inhibits the replacement of cell surface proteoglycan. These results indicate that the cell surface proteoglycan of NMuMG cells can be shed by cleavage of its matrix-binding ectodomain from its membrane- associated domain, providing a mechanism by which the epithelial cells can loosen their proteoglycan-mediated attachment to the matrix.
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Brown, C. T., Nugent, M. A., Lau, F. W., Trinkaus-Randall, V. (1999). Characterization of Proteoglycans Synthesized by Cultured Corneal Fibroblasts in Response to Transforming Growth Factor beta �and Fetal Calf Serum. J. Biol. Chem. 274: 7111-7119 [Abstract] [Full Text]
Ott, V. L., Rapraeger, A. C. (1998). Tyrosine Phosphorylation of Syndecan-1 and -4�Cytoplasmic Domains in Adherent B82 Fibroblasts. J. Biol. Chem. 273: 35291-35298 [Abstract] [Full Text]
Larrucea, S., Gonzalez-Rubio, C., Cambronero, R., Ballou, B., Bonay, P., Lopez-Granados, E., Bouvet, P., Fontan, G., Fresno, M., Lopez-Trascasa, M. (1998). Cellular Adhesion Mediated by Factor J, a Complement Inhibitor. EVIDENCE FOR NUCLEOLIN INVOLVEMENT. J. Biol. Chem. 273: 31718-31725 [Abstract] [Full Text]
Miralem, T., Templeton, D. M. (1998). Inactivation of kinase cascades in mesangial cells grown on collagen type I. Am. J. Physiol. Renal Physiol. 275: F585-F594 [Abstract] [Full Text]
Kainulainen, V., Wang, H., Schick, C., Bernfield, M. (1998). Syndecans, Heparan Sulfate Proteoglycans, Maintain the Proteolytic Balance of Acute Wound Fluids. J. Biol. Chem. 273: 11563-11569 [Abstract] [Full Text]
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McFall, A. J., Rapraeger, A. C. (1997). Identification of an Adhesion Site within the Syndecan-4 Extracellular Protein Domain. J. Biol. Chem. 272: 12901-12904 [Abstract] [Full Text]
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Elenius, K, Jalkanen, M (1994). Function of the syndecans--a family of cell surface proteoglycans. J. Cell Sci. 107: 2975-2982
Uitto, V.-J., Larjava, H. (1991). Extracellular Matrix Molecules and their Receptors: An Overview with Special Emphasis on Periodontal Tissues. CROBM 2: 323-354 [Abstract] [Full Text]
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