Cross-linking of CD4 induces cytoskeletal association of CD4 and p56lck
Experimental & Molecular Medicine
;
: 18-22, 2000.
Artículo
en Inglés
| WPRIM
| ID: wpr-16700
ABSTRACT
A membrane glycoprotein CD4 functions as a co-receptor of a T lymphocyte. The co-receptor function has been attributed to a protein tyrosine kinase, p56lck, which is activated upon CD4 binding to MHC molecule. In this study, we present evidences that one of the pathways through which CD4 transmits its signal is cytoskeleton association of p56lck tyrosine kinase as well as CD4 itself. Cytoskeletal association of both proteins is inhibited by a tyrosine kinase inhibitor, genistein, indicating that tyrosine protein kinase activation is important for cytoskeletal association of CD4 and p56lck. Cytoskeletal association of these proteins by CD4 cross-linking is not affected by inhibitors of protein kinase C nor PI3-kinase. Taken together, these results suggest that CD4 cross-linking activates a tyrosine kinase which then induces the simultaneous association of CD4 and p56lck with cytoskeleton.
Texto completo:
Disponible
Índice:
WPRIM (Pacífico Occidental)
Asunto principal:
Fosforilación
/
Unión Proteica
/
Tirosina
/
Citoesqueleto
/
Acetato de Tetradecanoilforbol
/
Células Tumorales Cultivadas
/
Antígenos CD4
/
Regulación hacia Abajo
/
Genisteína
/
Proteína Tirosina Quinasa p56(lck) Específica de Linfocito
Límite:
Humanos
Idioma:
Inglés
Revista:
Experimental & Molecular Medicine
Año:
2000
Tipo del documento:
Artículo
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