SH2-containing 5′-Inositol Phosphatase, SHIP2, Regulates Cytoskeleton Organization and Ligand-dependent Down-regulation of the Epidermal Growth Factor Receptor
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Therapeutic potential of SH2 domain-containing inositol-5'-phosphatase 1 (SHIP1) and SHIP2 inhibition in cancer.
Many tumors present with increased activation of the phosphatidylinositol 3-kinase (PI3K)-PtdIns(3,4,5)P(3)-protein kinase B (PKB/Akt) signaling pathway. It has long been thought that the lipid phosphatases SH2 domain-containing inositol-5'-phosphatase 1 (SHIP1) and SHIP2 act as tumor suppressors by counteracting with the survival signal induced by this pathway through hydrolysis or PtdIns(3,4,...
متن کاملتغییر بیان ژن SHIP2 (SH2 domain containing inositol 5-phosphatase) با استفاده از سیستم رتروویروس در سلول های کبدی HepG2
Introduction: Dyslypydmy is one of the risk factors of cardiovascular disease in diabetics. Dyslypydmy is diagnosed by increasing in plasma triglyceride density, decreasing HDL Cholesterol, and increasing LDL especially small LDL. Several evidences from human and animal studies indicate that the role of insulin resistance is a major cause of hypertrigly ceridemia in diabetics and people with me...
متن کاملEvidence for SH2 Domain-Containing 5′-Inositol Phosphatase-2 (SHIP2) Contributing to a Lymphatic Dysfunction
The lymphatic vasculature plays a critical role in a number of disease conditions of increasing prevalence, such as autoimmune disorders, obesity, blood vascular diseases, and cancer metastases. Yet, unlike the blood vasculature, the tools available to interrogate the molecular basis of lymphatic dysfunction/disease have been lacking. More recently, investigators have reported that dysregulatio...
متن کاملThe SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin
SHIP-2 is a phosphoinositidylinositol 3,4,5 trisphosphate (PtdIns[3,4,5]P3) 5-phosphatase that contains an NH2-terminal SH2 domain, a central 5-phosphatase domain, and a COOH-terminal proline-rich domain. SHIP-2 negatively regulates insulin signaling. In unstimulated cells, SHIP-2 localized in a perinuclear cytosolic distribution and at the leading edge of the cell. Endogenous and recombinant S...
متن کاملPertuzumab increases epidermal growth factor receptor down-regulation by counteracting epidermal growth factor receptor-ErbB2 heterodimerization.
Epidermal growth factor receptor (EGFR) and ErbB2 readily form heterodimers when both are expressed in the same cell and the EGFR is activated by one of its ligands. Our data show that such heterodimers are constitutively formed also in a ligand-independent manner on overexpression of EGFR and ErbB2 in porcine aortic endothelial cells. Interestingly, cross-linking experiments showed that incuba...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2005
ISSN: 0021-9258
DOI: 10.1074/jbc.m410289200