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Breast carcinoma epithelial cells express a very low density lipoprotein receptor variant lacking the olinked glycosylation domain encoded by exon 16, but with normal binding activity for serine proteinase/serpin complexes and m, 40,000 receptor associated protein

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  • Pia M. Martensen
  • Peter M. Rettenberger, Univ of Arhus
  • ,
  • Anni Christensen
  • Kazuhiro Oka, Baylor College of Medicine
  • ,
  • Lise Christensen, Rigshospitalet
  • ,
  • Helle H. Petersen, Aarhus University
  • ,
  • Lawrence Chan, Baylor College of Medicine
  • ,
  • Christian W. Heegaard
  • Peter A. Andreasen

Very low density lipoprotein receptor (VLDLR) belongs to the low density lipoprotein receptor family of endocytosis receptors. It binds a variety of different ligands, including apolipoprotein E, M, 40,000 receptor-associatedprotein (RAP), and some serine proteinase/serpin complexes, including uPA/PAI-1 and uPA/PN-1. Two forms of VLDLR with M, 105,000 and M, 130,000 have been found by SDS-PAGE These two forms correspond to forms with the absence (type-II) and presence (type-I) of the O-linked glycosylation domain encoded by exon 16, respectively. We show that the two forms have the same binding affinity to RAP and serine proteinase/serpin complexes. Using RTPCR we demonstrate that the splice variation giving rise to the two forms is highly cell specific. In particular, we demonstrate that human breast carcinomas express predominantly or exclusively the variant lacking exon 16. By immunohistochemistry, we demonstrate that VLDLR is mainly expressed by the epithelial cancer cells in these carcinomas. The VLDLR variant expressed by epithelial cancer cells could function in the clearance of cell-surface associated serine-proteinase/serpin complexes in breast carcinomas.

Original languageEnglish
JournalFibrinolysis and Proteolysis
IssueSUPPL. 3
Number of pages1
Publication statusPublished - 1 Dec 1997

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