Identification of clusterin sequences mediating renal tubular cell interactions

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Expression of the glycoprotein clusterin is markedly increased following tissue injury. One function of clusterin is to promote cell interactions which are perturbed in these pathologic settings. Clusterin causes cell aggregation and adhesion in vitro yet the molecular mechanism for this effect is not known. In order to identify the active site(s) of clusterin, 34 peptides, each 15 amino acid residues in length, were synthesized from hydrophilic regions of human clusterin. When studied individually, none of the peptides caused aggregation of LLC-PK1 cells, a porcine renal epithelial cell line. However, two out of the 34 peptides inhibited clusterin-induced cell aggregation in a dose-dependent manner. Scrambled versions of these two 'active' peptides did not inhibit cell aggregation. Seven peptides promoted cell adhesion. In conclusion, these findings provide evidence for novel amino acid sequences mediating clusterin-induced renal cell interactions.

Original languageEnglish (US)
Pages (from-to)449-457
Number of pages9
JournalJournal of Peptide Research
Volume54
Issue number5
DOIs
StatePublished - Nov 4 1999

Fingerprint

Clusterin
Cell Communication
Kidney
Cell Aggregation
Agglomeration
Peptides
Cell Adhesion
LLC-PK1 Cells
Amino Acids
Cell adhesion
Amino Acid Sequence
Catalytic Domain
Glycoproteins
Swine
Adhesion
Epithelial Cells
Tissue
Cell Line
Wounds and Injuries

Keywords

  • Adhesion
  • Aggregation
  • Apolipoprotein
  • Apolipoprotein J
  • Clusterin
  • Injury

Cite this

Identification of clusterin sequences mediating renal tubular cell interactions. / Silkensen, J. R.; Skubitz, A. P.N.; Skubitz, K. M.; Rosenberg, M. E.

In: Journal of Peptide Research, Vol. 54, No. 5, 04.11.1999, p. 449-457.

Research output: Contribution to journalArticle

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