BIOMAT Database Logo BIOMAT Database Logo

Zinc signals promote IL-2-dependent proliferation of T cells. 2010

Jennifer Kaltenberg, and Laura M Plum, and Julia L Ober-Blöbaum, and Andrea Hönscheid, and Lothar Rink, and Hajo Haase
Institute of Immunology, Medical Faculty, RWTH Aachen University, Aachen, Germany.

Zinc signals, i.e. a change of the intracellular concentration of free zinc ions in response to receptor stimulation, are involved in signal transduction in several immune cells. Here, the role of zinc signals in T-cell activation by IL-2 was investigated in the murine cytotoxic T-cell line CTLL-2 and in primary human T cells. Measurements with the fluorescent dyes FluoZin-3 and Zinquin showed that zinc is released from lysosomes into the cytosol in response to stimulation of the IL-2-receptor. Activation of the ERK-pathway was blocked by chelation of free zinc with N,N,N',N'-tetrakis-2(pyridyl-methyl)ethylenediamine, whereas zinc was not required for STAT5 phosphorylation. In addition, the key signaling molecules MEK and ERK were activated in response to elevated free intracellular zinc, induced by incubation with zinc and the ionophore pyrithione. Downstream of ERK activation, ERK-specific gene expression of c-fos and IL-2-induced proliferation was found to depend on zinc. Further experiments indicated that inhibition of MEK and ERK-dephosphorylating protein phosphatases is the molecular mechanism for the influence of zinc on this pathway. In conclusion, an increase of cytoplasmic free zinc is required for IL-2-induced ERK signaling and proliferation of T cells.

UI MeSH Term Description Entries
D007376 Interleukin-2 A soluble substance elaborated by antigen- or mitogen-stimulated T-LYMPHOCYTES which induces DNA synthesis in naive lymphocytes. IL-2,Lymphocyte Mitogenic Factor,T-Cell Growth Factor,TCGF,IL2,Interleukin II,Interleukine 2,RU 49637,RU-49637,Ro-23-6019,Ro-236019,T-Cell Stimulating Factor,Thymocyte Stimulating Factor,Interleukin 2,Mitogenic Factor, Lymphocyte,RU49637,Ro 23 6019,Ro 236019,Ro236019,T Cell Growth Factor,T Cell Stimulating Factor
D007476 Ionophores Chemical agents that increase the permeability of biological or artificial lipid membranes to specific ions. Most ionophores are relatively small organic molecules that act as mobile carriers within membranes or coalesce to form ion permeable channels across membranes. Many are antibiotics, and many act as uncoupling agents by short-circuiting the proton gradient across mitochondrial membranes. Ionophore
D008213 Lymphocyte Activation Morphologic alteration of small B LYMPHOCYTES or T LYMPHOCYTES in culture into large blast-like cells able to synthesize DNA and RNA and to divide mitotically. It is induced by INTERLEUKINS; MITOGENS such as PHYTOHEMAGGLUTININS, and by specific ANTIGENS. It may also occur in vivo as in GRAFT REJECTION. Blast Transformation,Blastogenesis,Lymphoblast Transformation,Lymphocyte Stimulation,Lymphocyte Transformation,Transformation, Blast,Transformation, Lymphoblast,Transformation, Lymphocyte,Activation, Lymphocyte,Stimulation, Lymphocyte
D008247 Lysosomes A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured or undergoes MEMBRANE FUSION. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed). Autolysosome,Autolysosomes,Lysosome
D010749 Phosphoprotein Phosphatases A group of enzymes removing the SERINE- or THREONINE-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992) Phosphoprotein Phosphatase,Phosphoprotein Phosphohydrolase,Protein Phosphatase,Protein Phosphatases,Casein Phosphatase,Ecto-Phosphoprotein Phosphatase,Nuclear Protein Phosphatase,Phosphohistone Phosphatase,Phosphoprotein Phosphatase-2C,Phosphoseryl-Protein Phosphatase,Protein Phosphatase C,Protein Phosphatase C-I,Protein Phosphatase C-II,Protein Phosphatase H-II,Protein-Serine-Threonine Phosphatase,Protein-Threonine Phosphatase,Serine-Threonine Phosphatase,Threonine Phosphatase,Ecto Phosphoprotein Phosphatase,Phosphatase C, Protein,Phosphatase C-I, Protein,Phosphatase C-II, Protein,Phosphatase H-II, Protein,Phosphatase, Casein,Phosphatase, Ecto-Phosphoprotein,Phosphatase, Nuclear Protein,Phosphatase, Phosphohistone,Phosphatase, Phosphoprotein,Phosphatase, Phosphoseryl-Protein,Phosphatase, Protein,Phosphatase, Protein-Serine-Threonine,Phosphatase, Protein-Threonine,Phosphatase, Serine-Threonine,Phosphatase, Threonine,Phosphatase-2C, Phosphoprotein,Phosphatases, Phosphoprotein,Phosphatases, Protein,Phosphohydrolase, Phosphoprotein,Phosphoprotein Phosphatase 2C,Phosphoseryl Protein Phosphatase,Protein Phosphatase C I,Protein Phosphatase C II,Protein Phosphatase H II,Protein Phosphatase, Nuclear,Protein Serine Threonine Phosphatase,Protein Threonine Phosphatase,Serine Threonine Phosphatase
D011083 Polycyclic Compounds Compounds which contain two or more rings in their structure. Compounds, Polycyclic
D011725 Pyridines Compounds with a six membered aromatic ring containing NITROGEN. The saturated version is PIPERIDINES.
D002451 Cell Compartmentation A partitioning within cells due to the selectively permeable membranes which enclose each of the separate parts, e.g., mitochondria, lysosomes, etc. Cell Compartmentations,Compartmentation, Cell,Compartmentations, Cell
D002455 Cell Division The fission of a CELL. It includes CYTOKINESIS, when the CYTOPLASM of a cell is divided, and CELL NUCLEUS DIVISION. M Phase,Cell Division Phase,Cell Divisions,Division Phase, Cell,Division, Cell,Divisions, Cell,M Phases,Phase, Cell Division,Phase, M,Phases, M
D002460 Cell Line Established cell cultures that have the potential to propagate indefinitely. Cell Lines,Line, Cell,Lines, Cell

Related Publications

Jennifer Kaltenberg, and Laura M Plum, and Julia L Ober-Blöbaum, and Andrea Hönscheid, and Lothar Rink, and Hajo Haase
IL-4 inhibits IL-2 receptor expression and IL-2-dependent proliferation of human T cells.
March 1990, Journal of immunology (Baltimore, Md. : 1950),
Jennifer Kaltenberg, and Laura M Plum, and Julia L Ober-Blöbaum, and Andrea Hönscheid, and Lothar Rink, and Hajo Haase
IL-4 potentiates the IL-2-dependent proliferation of mouse cytotoxic T cells.
February 1990, Journal of immunology (Baltimore, Md. : 1950),
Jennifer Kaltenberg, and Laura M Plum, and Julia L Ober-Blöbaum, and Andrea Hönscheid, and Lothar Rink, and Hajo Haase
TLR signals promote IL-6/IL-17-dependent transplant rejection.
May 2009, Journal of immunology (Baltimore, Md. : 1950),
Jennifer Kaltenberg, and Laura M Plum, and Julia L Ober-Blöbaum, and Andrea Hönscheid, and Lothar Rink, and Hajo Haase
IL-2-dependent proliferation of thymic accessory cells.
February 1988, Journal of immunology (Baltimore, Md. : 1950),
Jennifer Kaltenberg, and Laura M Plum, and Julia L Ober-Blöbaum, and Andrea Hönscheid, and Lothar Rink, and Hajo Haase
IL-4 and IL-2 promote human T-cell proliferation through symmetrical but independent pathways.
September 1992, Clinical immunology and immunopathology,
Jennifer Kaltenberg, and Laura M Plum, and Julia L Ober-Blöbaum, and Andrea Hönscheid, and Lothar Rink, and Hajo Haase
Repletion of zinc in zinc-deficient cells strongly up-regulates IL-1β-induced IL-2 production in T-cells.
October 2012, Metallomics : integrated biometal science,
Jennifer Kaltenberg, and Laura M Plum, and Julia L Ober-Blöbaum, and Andrea Hönscheid, and Lothar Rink, and Hajo Haase
Mycophenolic acid inhibits IL-2-dependent T cell proliferation, but not IL-2-dependent survival and sensitization to apoptosis.
September 2002, Journal of immunology (Baltimore, Md. : 1950),
Jennifer Kaltenberg, and Laura M Plum, and Julia L Ober-Blöbaum, and Andrea Hönscheid, and Lothar Rink, and Hajo Haase
PGE2 inhibits IL-2 and IL-4-dependent proliferation of CTLL-2 and HT2 cells.
April 1998, Cytokine,
Jennifer Kaltenberg, and Laura M Plum, and Julia L Ober-Blöbaum, and Andrea Hönscheid, and Lothar Rink, and Hajo Haase
IL-2-dependent proliferation of murine T cells requires expression of both the p55 and p70 subunits of the IL-2 receptor.
December 1990, Journal of immunology (Baltimore, Md. : 1950),
Jennifer Kaltenberg, and Laura M Plum, and Julia L Ober-Blöbaum, and Andrea Hönscheid, and Lothar Rink, and Hajo Haase
Evidence for IL-2 independent proliferation in human T cells.
February 1988, Journal of immunology (Baltimore, Md. : 1950),
Copied contents to your clipboard!