Src kinase, but not the Src kinase family member p56lck, mediates stromal cell-derived factor 1 α/CXCL12-induced chemotaxis of a T cell line

Seiichi Okabe, Seiji Fukuda, Hal Broxmeyer

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Stromal cell-derived factor 1 (SDF-1/CXCL12) is believed to mediate migration of leukocytes. To explore potential mechanisms, we evaluated the signal transduction pathways activated by SDF-1 in the Jurkat T cell line. Src kinase was phosphorylated and mitogen-activated protein kinase/extracellular signal-regulated kinase (MAPK/ERK) activated in a time-related fashion after SDF-1 stimulation. Chemotaxis of Jurkat cells was partially blocked by pretreatment with the src kinase inhibitor PP2 in a dose-dependent manner. Wiskott-Aldrich Syndrome Protein (WASP) regulates actin polymerization and cytoskeletal organization in T cells. We found WASP complexed to activated src after SDF-1 stimulation, suggesting a possible interacting role for src kinase and WASP in mediating SDF-1 action. J.CaM1.6 cells, which have lost expression of the src kinase p56lck (lck), responded to chemotaxis induced by SDF-1 as well as the parental Jurkat cells. Because J.CaM1.6 cells respond as well as the parental cells to SDF-1 in terms of ERK activation and tyrosine phosphorylation of WASP after SDF-1 stimulation, it appears that src kinase, but not the src kinase family member lck, mediates chemotaxis of Jurkat cells in response to SDF-1 induction and that src kinase may link with WASP in this effect.

Original languageEnglish
Pages (from-to)923-928
Number of pages6
JournalJournal of Hematotherapy and Stem Cell Research
Volume11
Issue number6
DOIs
StatePublished - Dec 2002

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Chemokine CXCL12
src-Family Kinases
Wiskott-Aldrich Syndrome Protein
Chemotaxis
Jurkat Cells
T-Lymphocytes
Cell Line
Extracellular Signal-Regulated MAP Kinases
Mitogen-Activated Protein Kinases
Polymerization
Tyrosine
Actins
Signal Transduction
Leukocytes
Phosphorylation

ASJC Scopus subject areas

  • Hematology
  • Immunology

Cite this

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abstract = "Stromal cell-derived factor 1 (SDF-1/CXCL12) is believed to mediate migration of leukocytes. To explore potential mechanisms, we evaluated the signal transduction pathways activated by SDF-1 in the Jurkat T cell line. Src kinase was phosphorylated and mitogen-activated protein kinase/extracellular signal-regulated kinase (MAPK/ERK) activated in a time-related fashion after SDF-1 stimulation. Chemotaxis of Jurkat cells was partially blocked by pretreatment with the src kinase inhibitor PP2 in a dose-dependent manner. Wiskott-Aldrich Syndrome Protein (WASP) regulates actin polymerization and cytoskeletal organization in T cells. We found WASP complexed to activated src after SDF-1 stimulation, suggesting a possible interacting role for src kinase and WASP in mediating SDF-1 action. J.CaM1.6 cells, which have lost expression of the src kinase p56lck (lck), responded to chemotaxis induced by SDF-1 as well as the parental Jurkat cells. Because J.CaM1.6 cells respond as well as the parental cells to SDF-1 in terms of ERK activation and tyrosine phosphorylation of WASP after SDF-1 stimulation, it appears that src kinase, but not the src kinase family member lck, mediates chemotaxis of Jurkat cells in response to SDF-1 induction and that src kinase may link with WASP in this effect.",
author = "Seiichi Okabe and Seiji Fukuda and Hal Broxmeyer",
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T1 - Src kinase, but not the Src kinase family member p56lck, mediates stromal cell-derived factor 1 α/CXCL12-induced chemotaxis of a T cell line

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AU - Fukuda, Seiji

AU - Broxmeyer, Hal

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AB - Stromal cell-derived factor 1 (SDF-1/CXCL12) is believed to mediate migration of leukocytes. To explore potential mechanisms, we evaluated the signal transduction pathways activated by SDF-1 in the Jurkat T cell line. Src kinase was phosphorylated and mitogen-activated protein kinase/extracellular signal-regulated kinase (MAPK/ERK) activated in a time-related fashion after SDF-1 stimulation. Chemotaxis of Jurkat cells was partially blocked by pretreatment with the src kinase inhibitor PP2 in a dose-dependent manner. Wiskott-Aldrich Syndrome Protein (WASP) regulates actin polymerization and cytoskeletal organization in T cells. We found WASP complexed to activated src after SDF-1 stimulation, suggesting a possible interacting role for src kinase and WASP in mediating SDF-1 action. J.CaM1.6 cells, which have lost expression of the src kinase p56lck (lck), responded to chemotaxis induced by SDF-1 as well as the parental Jurkat cells. Because J.CaM1.6 cells respond as well as the parental cells to SDF-1 in terms of ERK activation and tyrosine phosphorylation of WASP after SDF-1 stimulation, it appears that src kinase, but not the src kinase family member lck, mediates chemotaxis of Jurkat cells in response to SDF-1 induction and that src kinase may link with WASP in this effect.

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