Signaling through intercellular adhesion molecule 1 (ICAM-1) in a B cell lymphoma line: The activation of Lyn tyrosine kinase and the mitogen-activated protein kinase pathway

J Holland, T Owens

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

Udgivelsesdato: 1997-Apr-4
OriginalsprogEngelsk
TidsskriftJournal of Biological Chemistry
Vol/bind272
Udgave nummer14
Sider (fra-til)9108-12
Antal sider4
ISSN0021-9258
StatusUdgivet - 4. apr. 1997

Fingeraftryk

B-Cell Lymphoma
Intercellular Adhesion Molecule-1
Mitogen-Activated Protein Kinases
Protein-Tyrosine Kinases
Chemical activation
Cells
Cell Line
Lymphocyte Function-Associated Antigen-1
Phosphotransferases
Phosphorylation
Molecules
T-cells
Lymphocytes
src-Family Kinases
Adhesives
Tyrosine
Immunoglobulins
Assays
Lymphoma
Up-Regulation

Citer dette

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title = "Signaling through intercellular adhesion molecule 1 (ICAM-1) in a B cell lymphoma line: The activation of Lyn tyrosine kinase and the mitogen-activated protein kinase pathway",
abstract = "Intercellular adhesion molecule 1 (ICAM-1) (CD54) is an adhesion molecule of the immunoglobulin superfamily. The interaction between ICAM-1 on B lymphocytes and leukocyte function-associated antigen 1 on T cells plays a major role in several aspects of the immune response, including T-dependent B cell activation. While it was originally believed that ICAM-1 played a purely adhesive role, recent evidence suggests that it can itself transduce biochemical signals. We demonstrate that cross-linking of ICAM-1 results in the up-regulation of class II major histocompatibility complex, and we investigate the biochemical mechanism for the signaling role of ICAM-1. We show that cross-linking of ICAM-1 on the B lymphoma line A20 induces an increase in tyrosine phosphorylation of several cellular proteins, including the Src family kinase p53/p56(lyn). In vitro kinase assays showed that Lyn kinase was activated within 1 min after ICAM-1 cross-linking. In addition, ICAM-1 cross-linking resulted in activation of Raf-1 and mitogen-activated protein kinases, as determined by gel mobility shift. Activation of these kinases may represent important components in the cascade of signals that link ICAM-1 to various ICAM-1-elicited cellular responses. These data confirm the important role of ICAM-1 as a signaling molecule in B cell activation.",
keywords = "Animals, Calcium-Calmodulin-Dependent Protein Kinases, Electrophoresis, Polyacrylamide Gel, Enzyme Activation, Intercellular Adhesion Molecule-1, Lymphocyte Activation, Lymphoma, B-Cell, Mice, Mitogen-Activated Protein Kinase 1, Mitogen-Activated Protein Kinase 3, Mitogen-Activated Protein Kinases, Oncogene Proteins, Viral, Protein-Serine-Threonine Kinases, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-raf, Rats, Signal Transduction, T-Lymphocytes, src-Family Kinases",
author = "J Holland and T Owens",
year = "1997",
month = "4",
day = "4",
language = "English",
volume = "272",
pages = "9108--12",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "14",

}

Signaling through intercellular adhesion molecule 1 (ICAM-1) in a B cell lymphoma line : The activation of Lyn tyrosine kinase and the mitogen-activated protein kinase pathway. / Holland, J; Owens, T.

I: Journal of Biological Chemistry, Bind 272, Nr. 14, 04.04.1997, s. 9108-12.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - Signaling through intercellular adhesion molecule 1 (ICAM-1) in a B cell lymphoma line

T2 - The activation of Lyn tyrosine kinase and the mitogen-activated protein kinase pathway

AU - Holland, J

AU - Owens, T

PY - 1997/4/4

Y1 - 1997/4/4

N2 - Intercellular adhesion molecule 1 (ICAM-1) (CD54) is an adhesion molecule of the immunoglobulin superfamily. The interaction between ICAM-1 on B lymphocytes and leukocyte function-associated antigen 1 on T cells plays a major role in several aspects of the immune response, including T-dependent B cell activation. While it was originally believed that ICAM-1 played a purely adhesive role, recent evidence suggests that it can itself transduce biochemical signals. We demonstrate that cross-linking of ICAM-1 results in the up-regulation of class II major histocompatibility complex, and we investigate the biochemical mechanism for the signaling role of ICAM-1. We show that cross-linking of ICAM-1 on the B lymphoma line A20 induces an increase in tyrosine phosphorylation of several cellular proteins, including the Src family kinase p53/p56(lyn). In vitro kinase assays showed that Lyn kinase was activated within 1 min after ICAM-1 cross-linking. In addition, ICAM-1 cross-linking resulted in activation of Raf-1 and mitogen-activated protein kinases, as determined by gel mobility shift. Activation of these kinases may represent important components in the cascade of signals that link ICAM-1 to various ICAM-1-elicited cellular responses. These data confirm the important role of ICAM-1 as a signaling molecule in B cell activation.

AB - Intercellular adhesion molecule 1 (ICAM-1) (CD54) is an adhesion molecule of the immunoglobulin superfamily. The interaction between ICAM-1 on B lymphocytes and leukocyte function-associated antigen 1 on T cells plays a major role in several aspects of the immune response, including T-dependent B cell activation. While it was originally believed that ICAM-1 played a purely adhesive role, recent evidence suggests that it can itself transduce biochemical signals. We demonstrate that cross-linking of ICAM-1 results in the up-regulation of class II major histocompatibility complex, and we investigate the biochemical mechanism for the signaling role of ICAM-1. We show that cross-linking of ICAM-1 on the B lymphoma line A20 induces an increase in tyrosine phosphorylation of several cellular proteins, including the Src family kinase p53/p56(lyn). In vitro kinase assays showed that Lyn kinase was activated within 1 min after ICAM-1 cross-linking. In addition, ICAM-1 cross-linking resulted in activation of Raf-1 and mitogen-activated protein kinases, as determined by gel mobility shift. Activation of these kinases may represent important components in the cascade of signals that link ICAM-1 to various ICAM-1-elicited cellular responses. These data confirm the important role of ICAM-1 as a signaling molecule in B cell activation.

KW - Animals

KW - Calcium-Calmodulin-Dependent Protein Kinases

KW - Electrophoresis, Polyacrylamide Gel

KW - Enzyme Activation

KW - Intercellular Adhesion Molecule-1

KW - Lymphocyte Activation

KW - Lymphoma, B-Cell

KW - Mice

KW - Mitogen-Activated Protein Kinase 1

KW - Mitogen-Activated Protein Kinase 3

KW - Mitogen-Activated Protein Kinases

KW - Oncogene Proteins, Viral

KW - Protein-Serine-Threonine Kinases

KW - Protein-Tyrosine Kinases

KW - Proto-Oncogene Proteins

KW - Proto-Oncogene Proteins c-raf

KW - Rats

KW - Signal Transduction

KW - T-Lymphocytes

KW - src-Family Kinases

M3 - Journal article

C2 - 9083038

VL - 272

SP - 9108

EP - 9112

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 14

ER -