HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Weitzhandler, M. Articles by Bernfield, M. Search for Related Content PubMed PubMed Citation Articles by Weitzhandler, M. Articles by Bernfield, M. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 263, Issue 15, 6949-6952, 05, 1988

The cell surface proteoglycan of mouse mammary epithelial cells. The extracellular domain contains N terminus and a peptide sequence present in a conditioned medium proteoglycan

M Weitzhandler, HB Streeter, WJ Henzel and M Bernfield
Department of Pediatrics, Stanford University School of Medicine, California 94305.

The cell surface proteoglycan of mouse mammary epithelial (NMuMG) cells behaves as a receptor for interstitial matrix materials and consists of a membrane-associated domain and an extracellular domain (ectodomain). The ectodomain can be released intact from the cell surface by mild trypsin treatment and appears to be shed from the cells into the culture medium by cleavage from the membrane-associated domain. We have examined the chemical relationship between the trypsin-released proteoglycan and shed proteoglycan to assess their relationship to each other and to the cell surface. Purification and amino acid sequencing of the ectodomain released by mild trypsin treatment resulted in no clear signal until the protein was cleaved by CNBr treatment, suggesting that its N terminus is blocked and oriented extracellularly. The amino acid sequence identified in the trypsin-released ectodomain is present near the N terminus of the shed proteoglycan purified from conditioned medium, indicating that both forms possess closely related (if not identical) core proteins. The sequence reveals a pentapeptide identical to one near the C terminus of the rat hepatic lectin (RHL-1, rat asialoglycoprotein receptor). The medium proteoglycan, which migrates as a smear on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (between 93 and 200 kDa), is heterogeneous due to varying amounts of glycosaminoglycan and substituted O-linked oligosaccharide present on an approximately 46-kDa polypeptide.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				I. C. Dews and K. R. MacKenzie Transmembrane domains of the syndecan family of growth factor coreceptors display a hierarchy of homotypic and heterotypic interactions PNAS, December 26, 2007; 104(52): 20782 - 20787. [Abstract] [Full Text] [PDF]