IndraLab
Statements
sparser
"Mechanistic studies revealed that upon hypoxia‐induced activation, JAK2 phosphorylates STAT3, which then translocates into the nucleus, where it binds to the CCNA2 promoter to transcribe cyclin A2 expression, thereby promoting PASMC hyperplasia along with pulmonary vascular remodelling (Figure xref )."
reach
"Stat3 is frequently phosphorylated and activated in the majority of breast and ovarian cancers [XREF_BIBR], where cytokines and growth factors such as IL-6 bind to specific receptors and activate JAK2 which, in turn, phosphorylates Stat3 and prompts translocation of pStat3 to the nucleus."
sparser
"Furthermore, treatment of JAK2 clinical medicine AZD1480 to ESCC cells showed similar tendency with Lico B. Thus, JAK2 downstream signaling proteins phosphorylation of STAT3 at Y705 and S727 as well as STAT3 target protein Mcl-1 expression was decreased with treatment of Lico B. Our results suggest that Lico B inhibits ESCC cell growth, arrests cell cycle and induces apoptosis, revealing the underlying mechanism involved in JAK2/STAT3 signaling pathways after Lico B treatment."
sparser
"Also, JAK2 phosphorylates STAT3 at Tyr705, inducing its dimerization and translocation to the nucleus where it regulates the expression of different proteins involved in cancer progression, such as cyclin D1, COX2, VEGF, and SOCS3, a negative regulator of leptin signaling [ xref , xref ]."
reach
"Hypothalamic phosphorylated Janus kinase 2 (p-JAK2), phosphorylated signal transducer and activator of transcription 3 (p-STAT3), and phosphatidylinositol-3-kinase (PI3K) signaling, and hepatic sterol regulatory element binding protein-1 (SREBP-1) were qualified by Western blotting."
rlimsp
"Furthermore, the phosphorylation at Tyr705 of STAT3, which is known to be a phosphorylation site for Janus kinase 2 (JAK2), was completely inhibited by purvalanol A early (3 h) after drug treatment, although the phosphorylation of STAT3 at Ser727, which is a phosphorylation site for Ras/Raf/MEK and extracellular signal-regulated protein kinase 1/2, was still detectable until late (12 h) after treatment."
sparser
"Furthermore, treatment of JAK2 clinical medicine AZD1480 to ESCC cells showed similar tendency with Lico B. Thus, JAK2 downstream signaling proteins phosphorylation of STAT3 at Y705 and S727 as well as STAT3 target protein Mcl-1 expression was decreased with treatment of Lico B. Our results suggest that Lico B inhibits ESCC cell growth, arrests cell cycle and induces apoptosis, revealing the underlying mechanism involved in JAK2/STAT3 signaling pathways after Lico B treatment."
"Maximal activation of STAT3 requires phosphorylation at both Tyr705 and Ser727 sites (14). Although JAK2 kinase is shown to be responsible for phosphorylating STAT3 at Tyr705, we have shown that IL-1 receptor associated kinase 1 (IRAK-1) is capable of selectively phosphorylating STAT3 at Ser727 (15)."
"Induction of STAT3 Tyr705 and Ser727 phosphorylations by Galpha(s)QL was suppressed by inhibition of protein kinase A, Janus kinase 2/3, Rac1, c-Jun N-terminal kinase (JNK), or phosphatidylinositol 3-kinase, and a similar profile was observed in response to beta2-adrenergic receptor stimulation"
"Induction of STAT3 Tyr705 and Ser727 phosphorylations by Galpha(s)QL was suppressed by inhibition of protein kinase A, Janus kinase 2/3, Rac1, c-Jun N-terminal kinase (JNK), or phosphatidylinositol 3-kinase, and a similar profile was observed in response to beta2-adrenergic receptor stimulation"
JAK2 phosphorylated on an unknown residue, an unknown residue, and an unknown residue phosphorylates STAT3. 1 / 1
1
|