Cross-linking of CD4 induces cytoskeletal association of CD4 and p56lck
Experimental & Molecular Medicine
;
: 18-22, 2000.
Artigo
em Inglês
| 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:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Fosforilação
/
Ligação Proteica
/
Tirosina
/
Citoesqueleto
/
Acetato de Tetradecanoilforbol
/
Células Tumorais Cultivadas
/
Antígenos CD4
/
Regulação para Baixo
/
Genisteína
/
Proteína Tirosina Quinase p56(lck) Linfócito-Específica
Limite:
Humanos
Idioma:
Inglês
Revista:
Experimental & Molecular Medicine
Ano de publicação:
2000
Tipo de documento:
Artigo
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