A lymphocyte-specific protein tyrosine kinase, p56lck, regulates the PMA-induced internalization of CD4

Hiroki Yoshida, Yasuhiro Koga, Kazuhiko Nakamura, Genki Kimura, Kikuo Nomoto

研究成果: ジャーナルへの寄稿評論記事

7 引用 (Scopus)

抄録

p56lck, a member of the src family of non-receptor protein tyrosine kinases (PTKs), is expressed predominantly in T-lymphocytes. Association of p56lck with CD4 and CD8 T-cell receptor (TcR) accessory molecules suggests that p56lck may play a specialized role in antigen-induced T-cell activation. CD4 and CD8 molecules are known to stabilize the interaction between TcR and the major histocompatibility complex during T-cell activation. To examine the role of p56lck in the dynamics of the CD4 molecule, p56lck-expressing transfectant cell clones were prepared by the transfection of an lck-gene plasmid containing an inducible promoter into a CD4+lck- human monocytoid cell line. When these transfectant cells were stimulated with phorbol ester, CD4 internalization on these p56lck-expressing cell lines was selectively and markedly retarded, as compared to p56lck-negative control molecules were dissociated from p56lck whereas the surface-retained CD4 molecules were still associated with p56lck. Moreover, the dissociation of p56lck from CD4 appeared to occur prior to the PMA-induced internalization of CD4. These data indicate that p56lck regulates the PMA-induced internalization of CD4 possibly via its association with CD4. Treatment with genistein, a PTK inhibitor, revealed that the PTK activity of p56lck might not be involved in this regulatory effect of p56lck on CD4 internalization.

元の言語英語
ページ(範囲)321-330
ページ数10
ジャーナルBBA - Molecular Cell Research
1137
発行部数3
DOI
出版物ステータス出版済み - 11 17 1992

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CD4 Antigens
Protein-Tyrosine Kinases
Lymphocytes
T-Cell Antigen Receptor
CD27 Antigens
T-Lymphocytes
Cell Line
Genistein
Phorbol Esters
Protein Kinase Inhibitors
Major Histocompatibility Complex
Transfection
Plasmids
Clone Cells
Genes

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

これを引用

A lymphocyte-specific protein tyrosine kinase, p56lck, regulates the PMA-induced internalization of CD4. / Yoshida, Hiroki; Koga, Yasuhiro; Nakamura, Kazuhiko; Kimura, Genki; Nomoto, Kikuo.

:: BBA - Molecular Cell Research, 巻 1137, 番号 3, 17.11.1992, p. 321-330.

研究成果: ジャーナルへの寄稿評論記事

Yoshida, Hiroki ; Koga, Yasuhiro ; Nakamura, Kazuhiko ; Kimura, Genki ; Nomoto, Kikuo. / A lymphocyte-specific protein tyrosine kinase, p56lck, regulates the PMA-induced internalization of CD4. :: BBA - Molecular Cell Research. 1992 ; 巻 1137, 番号 3. pp. 321-330.
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abstract = "p56lck, a member of the src family of non-receptor protein tyrosine kinases (PTKs), is expressed predominantly in T-lymphocytes. Association of p56lck with CD4 and CD8 T-cell receptor (TcR) accessory molecules suggests that p56lck may play a specialized role in antigen-induced T-cell activation. CD4 and CD8 molecules are known to stabilize the interaction between TcR and the major histocompatibility complex during T-cell activation. To examine the role of p56lck in the dynamics of the CD4 molecule, p56lck-expressing transfectant cell clones were prepared by the transfection of an lck-gene plasmid containing an inducible promoter into a CD4+lck- human monocytoid cell line. When these transfectant cells were stimulated with phorbol ester, CD4 internalization on these p56lck-expressing cell lines was selectively and markedly retarded, as compared to p56lck-negative control molecules were dissociated from p56lck whereas the surface-retained CD4 molecules were still associated with p56lck. Moreover, the dissociation of p56lck from CD4 appeared to occur prior to the PMA-induced internalization of CD4. These data indicate that p56lck regulates the PMA-induced internalization of CD4 possibly via its association with CD4. Treatment with genistein, a PTK inhibitor, revealed that the PTK activity of p56lck might not be involved in this regulatory effect of p56lck on CD4 internalization.",
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T1 - A lymphocyte-specific protein tyrosine kinase, p56lck, regulates the PMA-induced internalization of CD4

AU - Yoshida, Hiroki

AU - Koga, Yasuhiro

AU - Nakamura, Kazuhiko

AU - Kimura, Genki

AU - Nomoto, Kikuo

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N2 - p56lck, a member of the src family of non-receptor protein tyrosine kinases (PTKs), is expressed predominantly in T-lymphocytes. Association of p56lck with CD4 and CD8 T-cell receptor (TcR) accessory molecules suggests that p56lck may play a specialized role in antigen-induced T-cell activation. CD4 and CD8 molecules are known to stabilize the interaction between TcR and the major histocompatibility complex during T-cell activation. To examine the role of p56lck in the dynamics of the CD4 molecule, p56lck-expressing transfectant cell clones were prepared by the transfection of an lck-gene plasmid containing an inducible promoter into a CD4+lck- human monocytoid cell line. When these transfectant cells were stimulated with phorbol ester, CD4 internalization on these p56lck-expressing cell lines was selectively and markedly retarded, as compared to p56lck-negative control molecules were dissociated from p56lck whereas the surface-retained CD4 molecules were still associated with p56lck. Moreover, the dissociation of p56lck from CD4 appeared to occur prior to the PMA-induced internalization of CD4. These data indicate that p56lck regulates the PMA-induced internalization of CD4 possibly via its association with CD4. Treatment with genistein, a PTK inhibitor, revealed that the PTK activity of p56lck might not be involved in this regulatory effect of p56lck on CD4 internalization.

AB - p56lck, a member of the src family of non-receptor protein tyrosine kinases (PTKs), is expressed predominantly in T-lymphocytes. Association of p56lck with CD4 and CD8 T-cell receptor (TcR) accessory molecules suggests that p56lck may play a specialized role in antigen-induced T-cell activation. CD4 and CD8 molecules are known to stabilize the interaction between TcR and the major histocompatibility complex during T-cell activation. To examine the role of p56lck in the dynamics of the CD4 molecule, p56lck-expressing transfectant cell clones were prepared by the transfection of an lck-gene plasmid containing an inducible promoter into a CD4+lck- human monocytoid cell line. When these transfectant cells were stimulated with phorbol ester, CD4 internalization on these p56lck-expressing cell lines was selectively and markedly retarded, as compared to p56lck-negative control molecules were dissociated from p56lck whereas the surface-retained CD4 molecules were still associated with p56lck. Moreover, the dissociation of p56lck from CD4 appeared to occur prior to the PMA-induced internalization of CD4. These data indicate that p56lck regulates the PMA-induced internalization of CD4 possibly via its association with CD4. Treatment with genistein, a PTK inhibitor, revealed that the PTK activity of p56lck might not be involved in this regulatory effect of p56lck on CD4 internalization.

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