EC Number   |
Application |
Reference |
|---|
   3.1.3.36 | medicine |
a SHIP2-antisense oligonucleotide therapy can improve the decrease in insulin-induced glucose disposal observed after high-fat feeding. This effect can be retraced on a molecular level by an improvement in insulin-induced Akt phosphorylation |
677466 |
| 3.1.3.36 | medicine |
examination of patients with Lowe oculocerebrorenal syndrome, MIM 309000, and their families for mutations in enzyme gene |
653244 |
| 3.1.3.36 | medicine |
inhibition of hypothalamic 5ptase IV expression by this antisense approach results in reduced daily food intake and body weight loss. 5ptase IV is a powerful regulator of signaling through PI3-kinase in hypothalamus and may become an interesting target for therapeutics of obesity and related disorders |
679517 |
| 3.1.3.36 | medicine |
inhibition of SHIP2 for the prevention and/or treatment of type 2 diabetes |
679439 |
| 3.1.3.36 | medicine |
organization of the actin cytoskeleton via D-myo-phosphatidylinositol 4,5-bisphosphate is involved in the regulation of hepatocyte differentiation by the extracellular matrix |
680062 |
| 3.1.3.36 | medicine |
SHIP2 plays an important role in insulin-dependent signaling pathways controlling glucose and lipid, metabolsim in vivo. A fine tuning of SHIP2 expression/activation in target organs is likely to be beneficial to correct metabolic dysfunctions in pathological conditions such as insulin resistance diabetes melitus and obesity |
677869 |
| 3.1.3.36 | molecular biology |
c-Jun NH2-terminal kinase (JNK)-interacting protein 1 (JIP1) interacts with SHIP2 and thereby positively modulates the MLK3/JIP1-mediated JNK1 activation. Furthermore, SHIP2 positively regulates the tyrosine phosphorylation of JIP1. By its interacting properties, SHIP2 can modulate JIP1-mediated JNK pathway signaling |
691713 |
| 3.1.3.36 | molecular biology |
catalytically inactive SHIP2 mutant P686A/D690A/R691A reduces preadipocyte proliferation by attenuating PDGFR signaling |
693329 |
| 3.1.3.36 | molecular biology |
hydrolysis of phosphatidylinositol 4,5-bisphosphate by PI(4,5)P2 5-phosphatase mediates calcium-induced inactivation of TRPV6 channels |
693056 |
| 3.1.3.36 | molecular biology |
intersectin1 (ITSN1) is identified as a binding partner of the SH2 domain containing inositol 5-phosphatase 2 (SHIP2). In response to epidermal growth factor, SHIP2 expression is able to recruit the ITSN1 short form (ITSN1-S) to the cell membrane, while SHIP2 overexpression does not modulate the ITSN-mediated extracellular signal-regulated kinase1/2 and c-Jun NH2-terminal kinase activation |
692357 |
