Cross-linking of CD4 induces cytoskeletal association of CD4 and p56lck.
- Author:
Young Mie HA-LEE
1
;
Yoon Sil LEE
;
Young Kee KIM
;
Jeong Won SOHN
Author Information
1. Korea Nutrition Research Institute, Korea University, Seoul.
- Publication Type:Original Article ; Research Support, Non-U.S. Gov't
- Keywords:
T cells;
cytoskeletal association;
tyrosine kinase inhibition;
CD4;
p56 lck
- MeSH:
Antigens, CD4/metabolism*;
Antigens, CD4/drug effects;
Cross-Linking Reagents;
Cytoskeleton/metabolism*;
Down-Regulation (Physiology);
Enzyme Inhibitors/pharmacology;
Flow Cytometry;
Genistein/pharmacology;
Human;
Lymphocyte Specific Protein Tyrosine Kinase p56(lck)/metabolism*;
Lymphocyte Specific Protein Tyrosine Kinase p56(lck)/antagonists & inhibitors;
Phosphorylation/drug effects;
Protein Binding;
Tetradecanoylphorbol Acetate/pharmacology;
Tumor Cells, Cultured;
Tyrosine/metabolism
- From:Experimental & Molecular Medicine
2000;32(1):18-22
- CountryRepublic of Korea
- Language:English
-
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.
