Stimulatory effects of the protein tyrosine phosphatase inhibitor, pervanadate, on T-cell activation events.

Secrist, J. Paul; Burns, L A; Karnitz, Larry M.; Koretzky, Gary A.; Abraham, Robert T.

doi:10.1016/s0021-9258(18)53403-7

Cited by 286 publications

(39 citation statements)

References 58 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…H 2 O 2 was shown to induce tyrosine phosphorylation of multiple cellular proteins in different cell types, and its effects were attributed to either a capability to inhibit protein-tyrosine phosphatases or to activate tyrosine kinases (see Refs. [22][23][24][25][26][27][28][29][30][31][32][33][34][35][36][37]. An inhibitory effect of H 2 O 2 on the phosphatase activity of CD45 has been reported (24,32).…”

Section: Discussionmentioning

confidence: 99%

“…For example, H 2 O 2 , either alone or in combination with vanadate, enhances activities of receptor tyrosine kinases (see Refs. 22 and 23 and references quoted therein) and cytoplasmic tyrosine kinases such as p56 lck (24 -28), p59 fyn (24,25,27), p72 syk (29,30), and ZAP-70 (31). In addition, H 2 O 2 inhibits the protein-tyrosine phosphatase CD45 (24,32).…”

mentioning

confidence: 99%

“…22 and 23 and references quoted therein) and cytoplasmic tyrosine kinases such as p56 lck (24 -28), p59 fyn (24,25,27), p72 syk (29,30), and ZAP-70 (31). In addition, H 2 O 2 inhibits the protein-tyrosine phosphatase CD45 (24,32). It is likely that regulation of tyrosine kinases and phosphatases is responsible for the H 2 O 2 -induced phosphorylation of multiple cellular proteins, as well as specific substrates (33)(34)(35).…”

mentioning

confidence: 99%

See 2 more Smart Citations

Regulation of Src Family Tyrosine Kinase Activities in Adherent Human Neutrophils

Yan

Berton

1996

Journal of Biological Chemistry

View full text Add to dashboard Cite

Src family tyrosine kinases have been implicated in the adhesion-dependent activation of neutrophil functions (Yan, S. R., Fumagalli, L., and Berton, G. (1995) J. Inflamm. 45, 297-312; Lowell, C. A., Fumagalli, L., and Berton, G. (1996) J. Cell Biol. 133, 895-910). Because the activity of tyrosine kinases can be affected by oxidants, we investigated whether reactive oxygen intermediates (ROI) produced by adherent neutrophils regulate Src family kinase activities. Inhibition of ROI production by diphenylene iodonium, an inhibitor of NADPH oxidase, or degradation of H2O2 by exogenously added catalase inhibited the adhesion-stimulated activities of p58(c-fgr) and p53/56(lyn). In addition, adhesion-stimulated p58(c-fgr) and p53/56(lyn) activities were greatly reduced in neutrophils from patients with chronic granulomatous disease (CGD) that are deficient in the production of ROI. Exogenously added H2O2 increased p58(c-fgr) and p53/56(lyn) activities in nonadherent neutrophils. Although ROI regulated the activities of p58(c-fgr) and p53/56(lyn), they did not affect the redistribution of the two kinases to a Triton X-100-insoluble, cytoskeletal fraction that occurs in adherent neutrophils. Tyrosine phosphorylation of proteins in adherent, CGD neutrophils was only partially inhibited, suggesting that the full activation of p58(c-fgr) and p53/56(lyn), which depends on endogenously produced ROI, does not represent an absolute requirement for protein tyrosine phosphorylation. The adhesion-stimulated activity of the tyrosine kinase p72(syk) was not affected by catalase in normal neutrophils, and it was comparable in normal and CGD neutrophils. These findings suggest that ROI endogenously produced by adherent neutrophils regulate Src family kinases activity selectively and establish the existence of a cross-talk between reorganization of the cytoskeleton, production of ROI, and Src family tyrosine kinase activities in signaling by adhesion.

show abstract

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Regulation of Src Family Tyrosine Kinase Activities in Adherent Human Neutrophils

Yan

Berton

1996

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Although the sites and kinases have not been identified, phosphorylation appears to play Regulation of NF-B Activation by Tyrosine Phosphorylation a role in increasing the affinity of NF-B for its target sequences (Naumann and Scheidereit, 1994). cAMP-Inhibition of tyrosine phosphatases by pervanadate in Jurkat cells leads to a rapid increase in tyrosine phos-dependent phosphorylation events were reported to down-modulate NF-B activity in T cells (Serfling et al, phorylation of cellular proteins followed by triggering of the T cell activation cascade (Secrist et al, 1993;Imbert 1989). Most importantly, phosphorylation regulates activity of the inhibitor IB-␣, which sequesters NF-B et al, 1994).…”

Section: Many If Not All Activators Of Nf-b Have Been Reportedmentioning

confidence: 99%

Tyrosine Phosphorylation of IκB-α Activates NF-κB without Proteolytic Degradation of IκB-α

Imbert

Rupec

Livolsi

et al. 1996

Cell

661

502

View full text Add to dashboard Cite

The transcription factor NF-kappa B regulates genes participating in immune and inflammatory responses. In T lymphocytes, NF-kappa B is sequestered in the cytosol by the inhibitor I kappa B-alpha and released after serine phosphorylation of I kappa B-alpha that regulates its ubiquitin-dependent degradation. We report an alternative mechanism of NF-kappa B activation. Stimulation of Jurkat T cells with the protein tyrosine phosphatase inhibitor and T cell activator pervanadate led to NF-kappa B activation through tyrosine phosphorylation but not degradation of I kappa B-alpha. Pervanadate-induced I kappa B-alpha phosphorylation and NF-kappa B activation required expression of the T cell tyrosine kinase p56ick. Reoxygenation of hypoxic cells appeared as a physiological effector of I kappa B-alpha tyrosine phosphorylation. Tyrosine phosphorylation of I kappa B-alpha represents a proteolysis-independent mechanism of NF-kappa B activation that directly couples NF-kappa B to cellular tyrosine kinase.

show abstract

“…To evaluate ZAP-70 kinase activity in the absence of other kinases, we examined anti-ZAP-70 immunoprecipitates from CD4 ϩ CD8 ϩ thymocytes that had been stimulated with pervanadate, a membrane-permeable phosphatase inhibitor that results in potent activation of intracellular PTKs (O' Shea et al, 1992;Secrist et al, 1993). Pervanadate stimulation, like TCR ϩ CD4 cocrosslinking, induced tyrosine phosphorylation of the that regulates ZAP-70 kinase activity.…”

Section: Introductionmentioning

confidence: 99%

A Spontaneously Arising Mutation in the DLAARN Motif of Murine ZAP-70 Abrogates Kinase Activity and Arrests Thymocyte Development

et al. 1997

View full text Add to dashboard Cite

Development of immature CD4+ CD8+ thymocytes into functionally mature CD4+ and CD8+ T cells is driven by selection events that require signals transduced through the T cell antigen receptor (TCR). Transduction of TCR signals in the thymus involves tyrosine phosphorylation of the protein tyrosine kinase ZAP-70 by p56(lck) and results in induction of ZAP-70 enzymatic activity. We have identified a novel, spontaneously arising point mutation within a highly conserved motif (DLAARN) in the kinase domain of murine ZAP-70 that uncouples tyrosine phosphorylation of ZAP-70 from induction of ZAP-70 kinase activity. Mice homozygous for this mutation are devoid of mature T cells because thymocyte development is arrested at the CD4+ CD8+ stage of differentiation. The developmental arrest is due to the inability of CD4+ CD8+ thymocytes to propagate TCR signals in the absence of ZAP-70 kinase activity despite tyrosine phosphorylation of TCR-associated ZAP-70 molecules.

show abstract

Stimulatory effects of the protein tyrosine phosphatase inhibitor, pervanadate, on T-cell activation events.

Cited by 286 publications

References 58 publications

Regulation of Src Family Tyrosine Kinase Activities in Adherent Human Neutrophils

Regulation of Src Family Tyrosine Kinase Activities in Adherent Human Neutrophils

Tyrosine Phosphorylation of IκB-α Activates NF-κB without Proteolytic Degradation of IκB-α

A Spontaneously Arising Mutation in the DLAARN Motif of Murine ZAP-70 Abrogates Kinase Activity and Arrests Thymocyte Development

Contact Info

Product

Resources

About