Identification of simian cyclophilin A as a calreticulin-binding protein in yeast two-hybrid screen and demonstration of cyclophilin A interaction with calreticulin.
Int J Biol Macromol
; 25(4): 345-51, 1999 Aug.
Article
em En
| MEDLINE
| ID: mdl-10456775
ABSTRACT
Cyclophilin A (CyPA) was identified as one of the calreticulin (CR)-binding proteins in a yeast two-hybrid screen utilizing simian cDNA expression-library. The simian CyPA protein had 96% identity with that of human, differing only at eight amino acid residues. We further established CyPA-CR interaction by incubation of glutathione transferase-fused CyPA (GST-CyPA) and CR proteins with CV-1 cyto-lysates, followed by CR and CyPA-specific immuno-blot analysis. The immunosuppressive drug cyclosporin A, a CyPA ligand, did not inhibit CyPA-CR interaction. Our results established a new property of CyPA binding activity to CR. Since CR is a Ca2+-binding protein, CR-CyPA interactions may be important in signaling pathways for induction of Ca2+-dependent cellular processes.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Ribonucleoproteínas
/
Proteínas de Ligação ao Cálcio
/
Peptidilprolil Isomerase
Tipo de estudo:
Diagnostic_studies
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Int J Biol Macromol
Ano de publicação:
1999
Tipo de documento:
Article
País de afiliação:
Estados Unidos