Identification of clusterin sequences mediating renal tubular cell interactions

Identification of clusterin sequences mediating renal tubular cell interactions

: 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...

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Published in:The journal of peptide research Vol. 54; no. 5; pp. 449 - 457
Main Authors: Silkensen, J.R., Skubitz, K.M., Rosenberg, M.E., Skubitz, A. P. N.
Format: Journal Article
Language:English
Published: Copenhagen, Denmark Munksgaard International Publishers 01-11-1999
Subjects:
adhesion
aggregation
Animals
apolipoprotein
apolipoprotein J
Binding Sites
Cell Adhesion - drug effects
Cell Aggregation - drug effects
Cell Line
Cell Survival - drug effects
Clusterin
Glycoproteins - chemistry
Glycoproteins - pharmacology
Humans
injury
Kidney Tubules - metabolism
Molecular Chaperones
Peptide Fragments - chemical synthesis
Peptide Fragments - pharmacology
Sequence Homology, Amino Acid
Swine
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Summary:: 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.
Bibliography:istex:6933F644CD12DF7F5F65316C38E9F8FE0EBD800E
ArticleID:CBDD145
ark:/67375/WNG-00D991SD-9
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To cite this article
Identification of clusterin sequences mediating renal tubular cell interactions.
Silensen, J. R., Skubitz, A. M. P., Skubittz, K. M. & Rosenberg, M. E.
J. Peptide Res.
1999
54
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1397-002X
1399-3011
DOI:10.1034/j.1399-3011.1999.00145.x