MiR-10b Downregulates the Stress-Induced Cell Surface Molecule MICB, a Critical Ligand for Cancer Cell Recognition by Natural Killer Cells

2012 ◽  
Vol 72 (21) ◽  
pp. 5463-5472 ◽  
Author(s):  
Pinchas Tsukerman ◽  
Noam Stern-Ginossar ◽  
Chamutal Gur ◽  
Ariella Glasner ◽  
Daphna Nachmani ◽  
...  
Keyword(s):  
Natural Killer Cells ◽  
Cell Surface ◽  
Natural Killer ◽  
Cancer Cell ◽  
Cell Recognition ◽  
Surface Molecule ◽  
Cell Surface Molecule ◽  
Killer Cells

Association of Src-like protein tyrosine kinases with the CD2 cell surface molecule in rat T lymphocytes and natural killer cells

1992 ◽  
Vol 12 (12) ◽  
pp. 5548-5554
Author(s):  
G M Bell ◽  
J B Bolen ◽  
J B Imboden
Keyword(s):  
Natural Killer Cells ◽  
T Lymphocytes ◽  
Cell Surface ◽  
Natural Killer ◽  
Tyrosine Kinases ◽  
Protein Tyrosine Kinases ◽  
Surface Molecule ◽  
Cell Surface Molecule ◽  
Killer Cells ◽  
Protein Tyrosine

The cell surface molecule CD2 has a signaling role in the activation of T lymphocytes and natural killer cells. Because perturbation of CD2 leads to the appearance of tyrosine-phosphorylated proteins, we investigated the possibility that CD2 associates with cytoplasmic protein tyrosine kinases. As determined by in vitro kinase assays and phosphoamino acid analysis, protein tyrosine kinase activity coprecipitated with CD2 from rat T lymphocytes, T lymphoblasts, thymocytes, interleukin-2-activated natural killer cells, and RNK-16 cells (a rat natural killer cell line). In each case, both p56lck and p59fyn were identified in the CD2 immunoprecipitate. In the thymus, the association between CD2 and these kinases occurred predominately in a small subset of thymocytes that had the cell surface phenotype of mature T cells, indicating that the association is a regulated event and occurs late in T-cell ontogeny. The finding that CD2 is associated with p56lck and p59fyn in detergent lysates suggests that interactions with these Src-like protein kinases play a critical role in CD2-mediated signal transduction.

scholarly journals Association of Src-like protein tyrosine kinases with the CD2 cell surface molecule in rat T lymphocytes and natural killer cells.

1992 ◽  
Vol 12 (12) ◽  
pp. 5548-5554 ◽  
Author(s):  
G M Bell ◽  
J B Bolen ◽  
J B Imboden
Keyword(s):  
Natural Killer Cells ◽  
T Lymphocytes ◽  
Cell Surface ◽  
Natural Killer ◽  
Tyrosine Kinases ◽  
Protein Tyrosine Kinases ◽  
Surface Molecule ◽  
Cell Surface Molecule ◽  
Killer Cells ◽  
Protein Tyrosine

The cell surface molecule CD2 has a signaling role in the activation of T lymphocytes and natural killer cells. Because perturbation of CD2 leads to the appearance of tyrosine-phosphorylated proteins, we investigated the possibility that CD2 associates with cytoplasmic protein tyrosine kinases. As determined by in vitro kinase assays and phosphoamino acid analysis, protein tyrosine kinase activity coprecipitated with CD2 from rat T lymphocytes, T lymphoblasts, thymocytes, interleukin-2-activated natural killer cells, and RNK-16 cells (a rat natural killer cell line). In each case, both p56lck and p59fyn were identified in the CD2 immunoprecipitate. In the thymus, the association between CD2 and these kinases occurred predominately in a small subset of thymocytes that had the cell surface phenotype of mature T cells, indicating that the association is a regulated event and occurs late in T-cell ontogeny. The finding that CD2 is associated with p56lck and p59fyn in detergent lysates suggests that interactions with these Src-like protein kinases play a critical role in CD2-mediated signal transduction.

Natural killer cells in breast cancer cell growth and metastasis in SCID mice

2005 ◽  
Vol 59 ◽  
pp. S375-S379 ◽  
Author(s):  
Md.Z. Dewan ◽  
H. Terunuma ◽  
S. Ahmed ◽  
K. Ohba ◽  
M. Takada ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cell Growth ◽  
Natural Killer Cells ◽  
Natural Killer ◽  
Cancer Cell ◽  
Breast Cancer Cell ◽  
Scid Mice ◽  
Cancer Cell Growth ◽  
Killer Cells ◽  
Breast Cancer Cell Growth

Generation of Antibodies to Cell Surface Markers on Mature Natural Killer Cells

2003 ◽  
pp. 211-217 ◽  
Author(s):  
Wayne C. Lai ◽  
Ying Zhang ◽  
Thaddeus George ◽  
P. V. Sivakumar ◽  
Susan Stepp ◽  
...  
Keyword(s):  
Natural Killer Cells ◽  
Cell Surface ◽  
Natural Killer ◽  
Surface Markers ◽  
Cell Surface Markers ◽  
Killer Cells

Molecular basis of human natural killer cell recognition of HLA-E (human leucocyte antigen-E) and its relevance to clearance of pathogen-infected and tumour cells

2000 ◽  
Vol 99 (1) ◽  
pp. 9-17 ◽  
Author(s):  
Christopher A. O'CALLAGHAN
Keyword(s):  
Endoplasmic Reticulum ◽  
Natural Killer Cells ◽  
Natural Killer Cell ◽  
Cell Surface ◽  
Natural Killer ◽  
Human Leucocyte Antigen ◽  
Killer Cell ◽  
Tumour Cells ◽  
Leader Peptide ◽  
Killer Cells

HLA-E (human leucocyte antigen-E) is a conserved class I major histocompatibility molecule which has only limited polymorphism. It binds to the leader peptide derived from the polymorphic classical major histocompatibility molecules HLA-A, HLA-B and HLA-C. This peptide binding is highly specific and stabilizes the HLA-E protein, allowing it to migrate to the cell surface. A functioning TAP (transporter associated with antigen processing) molecule is required to transport these peptides into the endoplasmic reticulum, where they can interact with HLA-E. HLA-E then migrates to the cell surface, where it interacts with CD94/NKG2A receptors on natural killer cells. This interaction inhibits natural killer cell-mediated lysis of a cell displaying HLA-E. If the leader peptide is not present in the endoplasmic reticulum, HLA-E is unstable and is degraded before it reaches the cell surface. In damaged cells, such as virally infected or tumour cells, down-regulation of HLA-A, HLA-B and HLA-C production or inhibition of TAP prevents stabilization of HLA-E by the leader peptide. Under these circumstances, HLA-E does not reach the cell surface and the cell is then vulnerable to lysis by natural killer cells. The molecular mechanisms underlying this function of HLA-E have been revealed by crystallographic studies of the structure of HLA-E.

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