Calreticulin is a binding protein for muramyl dipeptide and peptidoglycan in RK13 cells.
Biochemistry
; 43(37): 11796-801, 2004 Sep 21.
Article
em En
| MEDLINE
| ID: mdl-15362864
ABSTRACT
Calreticulin (CRT) was isolated and identified as a protein in rabbit kidney RK(13) cells that binds the apoptogenic bacterial cell wall (BCW) components, muramyl dipeptide (MDP) and peptidoglycan (PG). Mannan-agarose purified RK(13) cell CRT (rCRT) selectively bound sepharose-immobilized L,D-MDP and PG, but not L,L-MDP or D,D-MDP. Purified rCRT and bovine CRT (bCRT) also bound free PG and L,D-MDP demonstrated in bioassays of RK(13) cell apoptosis. The results suggest that, in RK(13) cells, (a) CRT is a specific binding protein for both L,D-MDP and PG and (b) CRT binding L,D-MDP or PG is dependent on the stereoisomeric configuration of the dipeptide (L-alanyl-D-isoglutamine) moiety. In addition, the results also suggest that, in RK(13) cells, the binding of L,D-MDP, L,L-MDP, D,D-MDP, or PG to CRT correlates with their capacities of inducing apoptosis.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peptidoglicano
/
Acetilmuramil-Alanil-Isoglutamina
/
Calreticulina
Limite:
Animals
Idioma:
En
Ano de publicação:
2004
Tipo de documento:
Article