Synthesis and Spectral Studies of 4h-1,4-Benzothiazine S,s-Dioxides (Sulfones)

Gupta, Kalpana Das; Rathore, Bhawani Singh; Gupta, R.; Gupta, Vandana; Kumar, M.

doi:10.1515/hc.2003.9.4.381

Cited by 28 publications

(43 citation statements)

References 4 publications

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“…The activation of downstream signaling events, including the Ras/Raf/MAP kinase pathway, the phosphatidylinositol pathway, and the phosphatidylinositol 3-kinase pathway, was shown to be dependent upon protein-tyrosine kinase functions (39,49). Thus, we studied first the ability of purinoreceptors to mediate intracellular signaling in response to extracellular ATP by incubating Jurkat cells with various concentrations of ATP for different time intervals and evaluating the phosphorylation of protein-tyrosine kinases.…”

Section: Extracellular Atp Induces Activation Of P56mentioning

confidence: 99%

Signaling through P2X7 Receptor in Human T Cells Involves p56 , MAP Kinases, and Transcription Factors AP-1 and NF-κB

Budagian¹,

Bulanova²,

Brovko³

et al. 2003

Journal of Biological Chemistry

103

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ATP-gated ion channel P2X receptors are expressed on the surface of most immune cells and can trigger multiple cellular responses, such as membrane permeabilization, cytokine production, and cell proliferation or apoptosis. Despite broad distribution and pleiotropic activities, signaling pathways downstream of these ionotropic receptors are still poorly understood. Here, we describe intracellular signaling events in Jurkat cells treated with millimolar concentrations of extracellular ATP. Within minutes, ATP treatment resulted in the phosphorylation and activation of p56 lck kinase, extracellular signalregulated kinase (ERK), and c-Jun N-terminal kinase but not p38 kinase. These effects were wholly dependent upon the presence of extracellular Ca 2؉ ions in the culture medium. Nevertheless, calmodulin antagonist calmidazolium and CaM kinase inhibitor KN-93 both had no effect on the activation of p56 lck and ERK, whereas a pretreatment of Jurkat cells with MAP kinase kinase inhibitor P098059 was able to abrogate phosphorylation of ERK. Extracellular ATP and other nucleotides act through specific cell surface receptors and can regulate a variety of cellular responses in many cell types and tissues (1-7). Among them are such different phenomena as platelet aggregation, smooth muscle contractility, excitatory transmitter function, mitogenic stimulation, or induction of cell death (reviewed in Refs. 1 and 8). The biological effects of extracellular nucleotides are mediated via stimulation of two primary classes of purinergic receptors, P1 and P2. The P1 receptors are responsive to adenosine, whereas the P2 receptors respond to a variety of nucleotides, including ATP (7, 9). The P2 receptors are subdivided in two mechanistically distinct subclasses, the metabotropic G protein-coupled P2Y receptors (P2Y1, P2Y2, P2Y4, P2Y6, and P2Y11-13) and the ionotropic ligand-gated channel P2X receptors (P2X1-7) (9 -12). Activation of the P2Y receptors generally induces downstream signaling through the G protein-coupled activation of phospholipase C, followed by Ca 2ϩ mobilization from intracellular stores (13,14). The P2Y11 also activates adenylyl cyclase, whereas the P2Y12 inhibits it (15). The seven subunits of the ionotrophic ATP-gated P2X receptor family comprise a different subclass, ranging from 379 to 595 amino acids in length and regulating the intracellular level of Ca 2ϩ by ligand-stimulated increase in cell membrane permeability for extracellular Ca 2ϩ ions (7,16,17). The P2X7 receptor is a 595-amino acid polypeptide and has a structure similar to that of other P2X receptors with two membrane-spanning domains, a large extracellular loop, and intracellular N-and C-terminal domains (18,19). In contrast to other P2X receptors, the P2X7 C-terminal intracellular chain is about 200 amino acids longer (20,21). The P2X7 has a pharmacological profile similar to the receptor previously designated as P2Z, with prominent expression in many immune cells (lymphocytes, monocytes/macrophages, dendritic, mesangial, and microglial cells) (...

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Section: Extracellular Atp Induces Activation Of P56mentioning

confidence: 99%

Signaling through P2X7 Receptor in Human T Cells Involves p56 , MAP Kinases, and Transcription Factors AP-1 and NF-κB

Budagian¹,

Bulanova²,

Brovko³

et al. 2003

Journal of Biological Chemistry

103

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“…T-cell antigen receptor ligation of an Lck-deficient Jurkat mutant, J.CaM1, failed to induce tyrosine phosphorylation and activation of p42 MAPK upon anti-CD3 or monoclonal anti-T-cell antigen receptor ␤ antibody treatment. The same stimuli activated p42 MAPK in J.CaM1 cells transfected with p56 lck , demonstrating that Lck plays an important role in MAP kinase activation (11).…”

mentioning

confidence: 82%

Tyrosine Kinase, p56 -induced Cell Motility, and Urokinase-type Plasminogen Activator Secretion Involve Activation of Epidermal Growth Factor Receptor/Extracellular Signal Regulated Kinase Pathways

Mahabeleshwar

Das

Kundu

2004

Journal of Biological Chemistry

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“…Although accentuation of the CD4 Ϫ CD8 Ϫ T cell developmental block in Lck Ϫ/Ϫ mice by concurrent Fyn-deficiency suggests partial redundancy, Fyn does not restore peripheral T cell activation in Lck Ϫ/Ϫ mice, thus indicating an essential, nonredundant role of Lck in T cell activation (3)(4)(5).…”

mentioning

confidence: 95%

Negative regulation of Lck by Cbl ubiquitin ligase

Rao

Miyake

Reddi

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

120

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The Cbl-family ubiquitin ligases function as negative regulators of activated receptor tyrosine kinases by facilitating their ubiquitination and subsequent targeting to lysosomes. Cbl associates with the lymphoid-restricted nonreceptor tyrosine kinase Lck, but the functional relevance of this interaction remains unknown. Here, we demonstrate that T cell receptor and CD4 coligation on human T cells results in enhanced association between Cbl and Lck, together with Lck ubiquitination and degradation.

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Synthesis and Spectral Studies of 4h-1,4-Benzothiazine S,s-Dioxides (Sulfones)

Cited by 28 publications

References 4 publications

Signaling through P2X7 Receptor in Human T Cells Involves p56 , MAP Kinases, and Transcription Factors AP-1 and NF-κB

Signaling through P2X7 Receptor in Human T Cells Involves p56 , MAP Kinases, and Transcription Factors AP-1 and NF-κB

Tyrosine Kinase, p56 -induced Cell Motility, and Urokinase-type Plasminogen Activator Secretion Involve Activation of Epidermal Growth Factor Receptor/Extracellular Signal Regulated Kinase Pathways

Negative regulation of Lck by Cbl ubiquitin ligase

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