Locomotion of tumor cells: a molecular comparison to migrating pre- and postmitotic leukocytes
Autor: | K. S. Zänker, F. Entschladen |
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Rok vydání: | 2000 |
Předmět: |
Cancer Research
biology Role of cell adhesions in neural development T-Lymphocytes Integrin T-cell receptor Mitosis CD28 General Medicine Receptor tyrosine kinase Cell biology Focal adhesion Oncology Cell Movement Neoplasms Cell Adhesion biology.protein Cytokines IL-2 receptor Chemokines Neoplasm Metastasis Signal transduction Cell Adhesion Molecules Signal Transduction |
Zdroj: | Journal of Cancer Research and Clinical Oncology. 126:671-681 |
ISSN: | 1432-1335 0171-5216 |
DOI: | 10.1007/s004320000143 |
Popis: | Increasing evidence has shown that the molecular regulation of active cell migration of slow-moving cells, e.g., tumor cells and fibroblasts, is different from fast-moving leukocytes, e.g., T lymphocytes and neutrophil granulocytes. Slow-moving cells develop focal adhesions as a crucial regulatory element during migration. These focal adhesions connect the extracellular matrix to the intracellular actin- and tubulin-cytoskeleton via integrins and enzymatically active proteins. Beside matrix-binding integrins, ligands of receptor tyrosine kinases and heterotrimeric G protein-coupled serpentine receptors initiate migration of slow-moving cells. Focal adhesions are not found in T lymphocytes and neutrophil granulocytes moving within three-dimensional matrices. In T lymphocytes, the T cell receptor is supposed to have a key regulatory function not only in antigen recognition, cell activation, and proliferation but also in cell migration. Regulatory molecules as well as the cytoskeleton are connected to the T cell receptor. The T cell receptor functionally combines elements of receptor tyrosine kinase signaling and of focal adhesions. In neutrophil granulocytes no multi-protein complexes regulating migration have been identified so far. Most potent activators of migration of neutrophil granulocytes, as those of T lymphocytes, are chemokines binding to heterotrimeric G protein-coupled serpentine receptors. |
Databáze: | OpenAIRE |
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