Binding and endocytosis of 39 kDa protein by mdbk cells

Kim Vettenranta, Guojun Bu, Alan L. Schwartz

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

A 39 kDa protein copurifies with the low density lipoprotein receptor‐related protein (LRP) and regulates ligand interactions with LRP. In our recent studies on the clearance of the 39 kDa protein in vivo, we demonstrated that once the liver LRP receptors were saturated, the kidney necame the major organ responsible for the 39 kDa protein clearance (Warshawsky et al., 1993, J. Clin. Invest., 92:937‐944). The current study was undertaken in order to investigate the potential binding and cellular processing of the 39 kDa protein by kidney‐derived MDBK cells. Herein we demonstrate specific, high‐affinity, saturable, and Ca2+‐dependent binding of the 125I‐39 kDa protein to MDBK cells (Kd ∼ 10‐15 nM, 50‐70,000 bindings sites per cell). Cellular uptake and degradation of the 125I‐39 kDa protein by MDBK cells was also demonstrated with kinetics typical of receptor‐mediated endocytosis. Using chemical crosslinking we show that LRP in part mediates the binding of 125I‐39 kDa protein to the MDBK cell surface. In addition, the presence of functional LRP on the MDBK cell surface was confirmed by the specific binding of activated α2‐macroglobulin, another ligand of LRP. Our data thus demonstrate the ability of kidney‐derived MDBK cells to specifically bind, endocytose, and degrade the 39 kDa protein. © 1995 Wiley‐Liss, Inc.

Original languageEnglish (US)
Pages (from-to)441-447
Number of pages7
JournalJournal of Cellular Physiology
Volume164
Issue number2
DOIs
StatePublished - Aug 1995

ASJC Scopus subject areas

  • Physiology
  • Clinical Biochemistry
  • Cell Biology

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