Ignet

Gene Information

Gene symbol: JAK3

Gene name: Janus kinase 3

HGNC ID: 6193

Synonyms: L-JAK, JAKL, LJAK, JAK3_HUMAN, JAK-3

Related Genes

#	Gene Symbol	Number of hits
1	CCND1	1 hits
2	CCND3	1 hits
3	CD247	1 hits
4	CD8A	1 hits
5	GZMB	1 hits
6	IL12A	1 hits
7	IL2	1 hits
8	IL2RG	1 hits
9	JAK1	1 hits
10	JAK2	1 hits
11	MAPK1	1 hits
12	MAPK14	1 hits
13	PLA2G1B	1 hits
14	PLA2G4A	1 hits
15	PTGS2	1 hits
16	STAT6	1 hits

Related Sentences

#	PMID	Sentence
1	12349944	P3CSK4 activates the expression of tumor suppressor protein p53 (p53), c-rel, inhibitor of nuclear factor kappa B (NFkappaB) alpha (IkappaB alpha), type 2 (inducible) nitric oxide (NO) synthase (iNOS), CD40-LR, intercellular adhesion molecule-1 (ICAM-1) and interleukin 1/6/15 (IL-1/6/15).
2	12349944	We detected no activation of heat shock protein (HSP) 27, 60, 84 and 86, osmotic stress protein 94 (Osp 94), IL-12, extracellular signal-regulated protein kinase 1 (ERK1), p38 mitogen activated protein (MAP)-kinase (p38), c-Jun NH2-terminal kinase (JNK), signal transducer and activator of transcription 1 (STAT1), CD14 and caspase genes.
3	12349944	Furthermore, we monitored inhibition of STAT6, Janus kinase 3 (Jak3) and cyclin D1/D3 gene transcription after stimulating bone marrow-derived macrophages (BMDM) with lipopeptide.
4	15655551	Using cultured T cells, 'exosomes' were evaluated for suppression of CD3-zeta and JAK 3 expressions and induction of apoptosis, measured by DNA fragmentation.
5	15655551	'Exosomes' expressed class I MHC, placental alkaline phosphatase, B23/nucleophosmin, and FasL.
6	15655551	'Exosomes' suppressed expression of T-cell activation signalling components, CD3-zeta and JAK 3 and induced apoptosis.
7	15655551	Using cultured T cells, 'exosomes' were evaluated for suppression of CD3-zeta and JAK 3 expressions and induction of apoptosis, measured by DNA fragmentation.
8	15655551	'Exosomes' expressed class I MHC, placental alkaline phosphatase, B23/nucleophosmin, and FasL.
9	15655551	'Exosomes' suppressed expression of T-cell activation signalling components, CD3-zeta and JAK 3 and induced apoptosis.
10	16424164	Key features of NK cell activity were inhibited, including release of perforin but not granzyme B, as well as the expression of cyclin D3 and activation of the Jak3-mediated pathways.
11	20372811	Interleukin-12-anchored exosomes increase cytotoxicity of T lymphocytes by reversing the JAK/STAT pathway impaired by tumor-derived exosomes.
12	20372811	We investigated whether interleukin-12 (IL-12)-anchored exosomes (EXO/IL-12) reverse tumor exosome-mediated inhibition of T-cell activation and cytotoxicity was associated with inhibition of JAK3 and p-STAT5.
13	20372811	A co-expression plasmid of pBudCE4.1/IL-12A/ IL-12B-GPI was constructed.
14	20372811	Expression of JAK2, JAK3 and p-STAT5 was detected by Western blotting.
15	20372811	Our results showed that EXO/IL-12 was much more efficient in induction of the proliferation, release of IFN-gamma and cytotoxic effect of T lymphocytes than conventional exosomes in vitro.
16	20372811	Exosomes inhibited the expression of JAK3 and phosphorylation of STAT5 in high doses in T-cells, but not JAK2, while EXO/IL-12 had much less attenuated reduction of the expression of p-STAT5.
17	20372811	The enhanced cytotoxic effects of T lymphocytes might partly depend on EXO/IL-12 reversing the suppressed expression of p-Stat5 by Jak2/Stat5 pathway.
18	20372811	Interleukin-12-anchored exosomes increase cytotoxicity of T lymphocytes by reversing the JAK/STAT pathway impaired by tumor-derived exosomes.
19	20372811	We investigated whether interleukin-12 (IL-12)-anchored exosomes (EXO/IL-12) reverse tumor exosome-mediated inhibition of T-cell activation and cytotoxicity was associated with inhibition of JAK3 and p-STAT5.
20	20372811	A co-expression plasmid of pBudCE4.1/IL-12A/ IL-12B-GPI was constructed.
21	20372811	Expression of JAK2, JAK3 and p-STAT5 was detected by Western blotting.
22	20372811	Our results showed that EXO/IL-12 was much more efficient in induction of the proliferation, release of IFN-gamma and cytotoxic effect of T lymphocytes than conventional exosomes in vitro.
23	20372811	Exosomes inhibited the expression of JAK3 and phosphorylation of STAT5 in high doses in T-cells, but not JAK2, while EXO/IL-12 had much less attenuated reduction of the expression of p-STAT5.
24	20372811	The enhanced cytotoxic effects of T lymphocytes might partly depend on EXO/IL-12 reversing the suppressed expression of p-Stat5 by Jak2/Stat5 pathway.
25	20372811	Interleukin-12-anchored exosomes increase cytotoxicity of T lymphocytes by reversing the JAK/STAT pathway impaired by tumor-derived exosomes.
26	20372811	We investigated whether interleukin-12 (IL-12)-anchored exosomes (EXO/IL-12) reverse tumor exosome-mediated inhibition of T-cell activation and cytotoxicity was associated with inhibition of JAK3 and p-STAT5.
27	20372811	A co-expression plasmid of pBudCE4.1/IL-12A/ IL-12B-GPI was constructed.
28	20372811	Expression of JAK2, JAK3 and p-STAT5 was detected by Western blotting.
29	20372811	Our results showed that EXO/IL-12 was much more efficient in induction of the proliferation, release of IFN-gamma and cytotoxic effect of T lymphocytes than conventional exosomes in vitro.
30	20372811	Exosomes inhibited the expression of JAK3 and phosphorylation of STAT5 in high doses in T-cells, but not JAK2, while EXO/IL-12 had much less attenuated reduction of the expression of p-STAT5.
31	20372811	The enhanced cytotoxic effects of T lymphocytes might partly depend on EXO/IL-12 reversing the suppressed expression of p-Stat5 by Jak2/Stat5 pathway.
32	23359502	IL-2 produced by CD8+ immune T cells can augment their IFN-γ production independently from their proliferation in the secondary response to an intracellular pathogen.
33	23359502	In the current study, we examined the role of IL-2 in IFN-γ production by CD8(+) immune T cells in their secondary responses using T. gondii-specific CD8(+) T cell hybridomas and splenic CD8(+) immune T cells from chronically infected mice.
34	23359502	The majority (92%) of CD8(+) T cell hybridomas produced large amounts of IFN-γ only when a low amount (0.5 ng/ml) of exogenous IL-2 was provided in combination with T. gondii Ags.
35	23359502	Inhibition of cell proliferation by mitomycin C did not affect the enhancing effect of IL-2 on the IFN-γ production, and significant increases in transcription factor T-bet expression were associated with the IL-2-mediated IFN-γ amplification.
36	23359502	Splenic CD8(+) immune T cells produced similar low levels of IL-2 in the secondary response to T. gondii, and a blocking of IL-2 signaling by anti-IL-2Rα Ab or inhibitors of JAK1 and JAK3 significantly reduced IFN-γ production of the T cells.
37	23359502	This IL-2-mediated upregulation of IFN-γ production was observed in mitomycin C-treated CD8(+) immune T cells, thus independent from their cell division.
38	23359502	Therefore, endogenous IL-2 produced by CD8(+) immune T cells can play an important autocrine-enhancing role on their IFN-γ production in the secondary responses to T. gondii, suggesting an importance of induction of CD8(+) immune T cells with an appropriate IL-2 production for vaccine development.
39	24343645	Janus kinase 3 activity is necessary for phosphorylation of cytosolic phospholipase A2 and prostaglandin E2 synthesis by macrophages infected with Francisella tularensis live vaccine strain.
40	24343645	The synthesis of PGE2 begins with the liberation of arachidonic acid (AA) from membrane phospholipids by cytosolic phospholipase A2 (cPLA2).
41	24343645	In this study, we show that cPLA2, p38 mitogen-activated protein kinase (MAPK), and Janus kinase 3 (JAK3) signaling are necessary for F. tularensis-induced PGE2 production.
42	24343645	Inhibition of JAK3 activity reduced the phosphorylation of cPLA2 and COX-2 protein levels.
43	24343645	In addition, JAK3 regulates cPLA2 phosphorylation independent of transcription.
44	24343645	Moreover, p38 MAPK activity is required for F. tularensis-induced COX-2 protein synthesis, but not for the phosphorylation of cPLA2.
45	24343645	This research highlights a unique signaling axis in which JAK3 and p38 MAPK regulate the activity of multiple enzymes of the PGE2-biosynthetic pathway in macrophages infected with F. tularensis.
46	24343645	Janus kinase 3 activity is necessary for phosphorylation of cytosolic phospholipase A2 and prostaglandin E2 synthesis by macrophages infected with Francisella tularensis live vaccine strain.
47	24343645	The synthesis of PGE2 begins with the liberation of arachidonic acid (AA) from membrane phospholipids by cytosolic phospholipase A2 (cPLA2).
48	24343645	In this study, we show that cPLA2, p38 mitogen-activated protein kinase (MAPK), and Janus kinase 3 (JAK3) signaling are necessary for F. tularensis-induced PGE2 production.
49	24343645	Inhibition of JAK3 activity reduced the phosphorylation of cPLA2 and COX-2 protein levels.
50	24343645	In addition, JAK3 regulates cPLA2 phosphorylation independent of transcription.
51	24343645	Moreover, p38 MAPK activity is required for F. tularensis-induced COX-2 protein synthesis, but not for the phosphorylation of cPLA2.
52	24343645	This research highlights a unique signaling axis in which JAK3 and p38 MAPK regulate the activity of multiple enzymes of the PGE2-biosynthetic pathway in macrophages infected with F. tularensis.
53	24343645	Janus kinase 3 activity is necessary for phosphorylation of cytosolic phospholipase A2 and prostaglandin E2 synthesis by macrophages infected with Francisella tularensis live vaccine strain.
54	24343645	The synthesis of PGE2 begins with the liberation of arachidonic acid (AA) from membrane phospholipids by cytosolic phospholipase A2 (cPLA2).
55	24343645	In this study, we show that cPLA2, p38 mitogen-activated protein kinase (MAPK), and Janus kinase 3 (JAK3) signaling are necessary for F. tularensis-induced PGE2 production.
56	24343645	Inhibition of JAK3 activity reduced the phosphorylation of cPLA2 and COX-2 protein levels.
57	24343645	In addition, JAK3 regulates cPLA2 phosphorylation independent of transcription.
58	24343645	Moreover, p38 MAPK activity is required for F. tularensis-induced COX-2 protein synthesis, but not for the phosphorylation of cPLA2.
59	24343645	This research highlights a unique signaling axis in which JAK3 and p38 MAPK regulate the activity of multiple enzymes of the PGE2-biosynthetic pathway in macrophages infected with F. tularensis.
60	24343645	Janus kinase 3 activity is necessary for phosphorylation of cytosolic phospholipase A2 and prostaglandin E2 synthesis by macrophages infected with Francisella tularensis live vaccine strain.
61	24343645	The synthesis of PGE2 begins with the liberation of arachidonic acid (AA) from membrane phospholipids by cytosolic phospholipase A2 (cPLA2).
62	24343645	In this study, we show that cPLA2, p38 mitogen-activated protein kinase (MAPK), and Janus kinase 3 (JAK3) signaling are necessary for F. tularensis-induced PGE2 production.
63	24343645	Inhibition of JAK3 activity reduced the phosphorylation of cPLA2 and COX-2 protein levels.
64	24343645	In addition, JAK3 regulates cPLA2 phosphorylation independent of transcription.
65	24343645	Moreover, p38 MAPK activity is required for F. tularensis-induced COX-2 protein synthesis, but not for the phosphorylation of cPLA2.
66	24343645	This research highlights a unique signaling axis in which JAK3 and p38 MAPK regulate the activity of multiple enzymes of the PGE2-biosynthetic pathway in macrophages infected with F. tularensis.
67	24343645	Janus kinase 3 activity is necessary for phosphorylation of cytosolic phospholipase A2 and prostaglandin E2 synthesis by macrophages infected with Francisella tularensis live vaccine strain.
68	24343645	The synthesis of PGE2 begins with the liberation of arachidonic acid (AA) from membrane phospholipids by cytosolic phospholipase A2 (cPLA2).
69	24343645	In this study, we show that cPLA2, p38 mitogen-activated protein kinase (MAPK), and Janus kinase 3 (JAK3) signaling are necessary for F. tularensis-induced PGE2 production.
70	24343645	Inhibition of JAK3 activity reduced the phosphorylation of cPLA2 and COX-2 protein levels.
71	24343645	In addition, JAK3 regulates cPLA2 phosphorylation independent of transcription.
72	24343645	Moreover, p38 MAPK activity is required for F. tularensis-induced COX-2 protein synthesis, but not for the phosphorylation of cPLA2.
73	24343645	This research highlights a unique signaling axis in which JAK3 and p38 MAPK regulate the activity of multiple enzymes of the PGE2-biosynthetic pathway in macrophages infected with F. tularensis.
74	24481607	Out of five male infants with T-B+NK- SCID phenotype, mutation analysis revealed interleukin-2 (common) gamma-chain receptor (IL2RG) mutations in 3 with positive X-linked family history, and Janus-kinase (JAK)-3 gene defects in the other two.
75	24481607	Six patients had T-B-NK+ SCID phenotype and further 6 features of OS, 11 of which had recombinase-activating gene (RAG1or RAG2) and 1 Artemis gene mutations.