| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
CUTTING EDGE |
Immunobiology Department, DNAX Research Institute of Molecular and Cellular Biology, Palo Alto, CA 94304
T cell activation represents a balance between positive and negative signals delivered via distinct cell surface molecules. Many cytoplasmic protein tyrosine phosphatases are involved in regulating cellular responses by antagonizing the action of protein tyrosine kinases. CD148 is a receptor-type protein tyrosine phosphatase expressed by all human mononuclear cells. We have investigated the effect of CD148 on TCR-mediated activation of human T cells. Overexpression of wild-type, but not a phosphatase-deficient, CD148 in Jurkat T cells inhibited TCR-mediated activation, evidenced by reduced expression of the early activation Ag CD69, inhibition of tyrosine phosphorylation of many intracellular proteins including the critical protein tyrosine kinase ZAP-70, and impairment of mitogen-activated protein kinase activation. Taken together, these results suggest that CD148 is an important phosphatase involved in negatively regulating the proximal signaling events during activation of Ag-specific T cells.
This article has been cited by other articles:
|
|
 |
|
  T. Takahashi, K. Takahashi, R. L. Mernaugh, N. Tsuboi, H. Liu, and T. O. Daniel A monoclonal antibody against CD148, a receptor-like tyrosine phosphatase, inhibits endothelial-cell growth and angiogenesis Blood, August 15, 2006; 108(4): 1234 - 1242. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. Lin, J. W. Zhu, J. E. Baker, and A. Weiss Regulated Expression of the Receptor-Like Tyrosine Phosphatase CD148 on Hemopoietic Cells J. Immunol., August 15, 2004; 173(4): 2324 - 2330. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Kellie, G. Craggs, I. N. Bird, and G. E. Jones The tyrosine phosphatase DEP-1 induces cytoskeletal rearrangements, aberrant cell-substratum interactions and a reduction in cell proliferation J. Cell Sci., February 1, 2004; 117(4): 609 - 618. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 T. Ito, H. Okazawa, K. Maruyama, K. Tomizawa, S.-i. Motegi, H. Ohnishi, H. Kuwano, A. Kosugi, and T. Matozaki Interaction of SAP-1, a Transmembrane-type Protein-tyrosine Phosphatase, with the Tyrosine Kinase Lck: ROLES IN REGULATION OF T CELL FUNCTION J. Biol. Chem., September 12, 2003; 278(37): 34854 - 34863. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. Lin and A. Weiss The tyrosine phosphatase CD148 is excluded from the immunologic synapse and down-regulates prolonged T cell signaling J. Cell Biol., August 18, 2003; 162(4): 673 - 682. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. E. Baker, R. Majeti, S. G. Tangye, and A. Weiss Protein Tyrosine Phosphatase CD148-Mediated Inhibition of T-Cell Receptor Signal Transduction Is Associated with Reduced LAT and Phospholipase C{gamma}1 Phosphorylation Mol. Cell. Biol., April 1, 2001; 21(7): 2393 - 2403. [Abstract] [Full Text]
|
|
|
|
|
|
M. Kovalenko, K. Denner, J. Sandstrom, C. Persson, S. GroB, E. Jandt, R. Vilella, F. Bohmer, and A. Ostman Site-selective Dephosphorylation of the Platelet-derived Growth Factor beta -Receptor by the Receptor-like Protein-tyrosine Phosphatase DEP-1 J. Biol. Chem., May 26, 2000; 275(21): 16219 - 16226. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. Billard, S. Delaire, E. Raffoux, A. Bensussan, and L. Boumsell Switch in the protein tyrosine phosphatase associated with human CD100 semaphorin at terminal B-cell differentiation stage Blood, February 1, 2000; 95(3): 965 - 972. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
