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INS — STAT1
Text-mined interactions from Literome
Rojas et al., IUBMB Life 2000
(Insulin Resistance) :
Insulin induces phosphorylation and activation of JAK2 tyrosine, as well as its association with
STAT1 and SHP2 in insulin-sensitive tissues of intact rats, thus demonstrating a new pathway in transduction of insulin signals ... The acute treatment with epinephrine showed no difference in
insulin induced JAK2 tyrosine phosphorylation or
JAK2/STAT1 and JAK2/SHP2 association in comparison with the control ... In fasting and dexamethasone treated rats, therefore, insulin induced JAK2 tyrosine phosphorylation decreases, and the JAK2 protein expression is differentially regulated such that the
insulin induced JAK2 association with SHP2 and
STAT1 shows opposite interactions with the kinase
Rocha et al., Curr Eye Res 2000
(Diabetes Mellitus, Experimental) :
The
activation of
insulin receptors following insulin treatment, and the involvement of insulin receptor substrates-1 and -2, Shc, JAK-2 and
STAT-1 , were analyzed by immunoprecipitation, followed by SDS-PAGE and immunoblotting of rat lacrimal and salivary glands after exposure to insulin ... Functional studies demonstrated that
insulin induced a dose dependent phosphorylation of the insulin receptor, IGF-1R, insulin receptor substrates-1 and -2, Shc, and
STAT-1 ... In rats with streptozotocin induced diabetes mellitus there was a significant reduction in
insulin induced insulin receptor and
STAT-1 phosphorylation in the lacrimal gland but not in the salivary gland ; there was no influence on Shc phosphorylation in either tissue
Rocha et al., Acta Ophthalmol Scand 2003
:
The level of phosphorylation determined by densitometry in the older group of rats showed that ageing significantly reduced
insulin induced IR phosphorylation in LG and SG and
STAT-1 phosphorylation in SG, compared to in the control group, but did not alter Shc phosphorylation
Chuang et al., Biochem Biophys Res Commun 1997
(Carcinoma, Hepatocellular) :
These data indicate that insulin receptor signaling can activate the transcriptional regulatory function of STAT protein, and that
insulin actions on
Stat1alpha are
mediated through signaling pathways independent of JAK family of kinases