RNA interference targeting SHP‐1 attenuates myocardial infarction in rats

Shinoda, Masahiro; Tsuchida, Keiko; Hata, Tomoko; Makino, Naoki

doi:10.1096/fj.05-4020fje

Cited by 36 publications

(30 citation statements)

References 32 publications

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“…We also demonstrate that SHP-1, but not its closest structurally related family member, SHP-2, is the specific phosphatase for GIV. This is in keeping with the fact that whereas SHP-1 antagonizes Akt signaling (18,(41)(42)(43)(44) and inhibits chemotaxis (27,(45)(46)(47)(48), SHP-2 is frequently associated with enhancement of the PI3K-Akt pathway (49 -53) during growth factor-initiated cell migration (54). Of note, all of the experimental evidence supporting SHP-1 ability to antagonize the Akt pathway was obtained using mesenchymal and hematopoietic cells and the biological role of the epithelium-specific isoform of SHP-1 and how it might inhibit chemotaxis/cell migration remained elusive (55).…”

Section: Discussionsupporting

confidence: 80%

Src Homology Domain 2-containing Protein-tyrosine Phosphatase-1 (SHP-1) Binds and Dephosphorylates Gα-interacting, Vesicle-associated Protein (GIV)/Girdin and Attenuates the GIV-Phosphatidylinositol 3-Kinase (PI3K)-Akt Signaling Pathway

Mittal

Pavlova²,

Garcia‐Marcos

et al. 2011

Journal of Biological Chemistry

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GIV (G␣-interacting vesicle-associated protein, also known as Girdin) is a bona fide enhancer of PI3K-Akt signals during a diverse set of biological processes, e.g. wound healing, macrophage chemotaxis, tumor angiogenesis, and cancer invasion/metastasis. We recently demonstrated that tyrosine phosphorylation of GIV by receptor and non-receptor-tyrosine kinases is a key step that is required for GIV to directly bind and enhance PI3K activity. Here we report the discovery that Src homology 2-containing phosphatase-1 (SHP-1) is the

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Section: Discussionsupporting

confidence: 80%

Src Homology Domain 2-containing Protein-tyrosine Phosphatase-1 (SHP-1) Binds and Dephosphorylates Gα-interacting, Vesicle-associated Protein (GIV)/Girdin and Attenuates the GIV-Phosphatidylinositol 3-Kinase (PI3K)-Akt Signaling Pathway

Mittal

Pavlova²,

Garcia‐Marcos

et al. 2011

Journal of Biological Chemistry

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“…The PCR products were analyzed by agarose gel electrophoresis (1.3%) followed by staining with ethidium bromide and scanning with Gel-Doc (Bio-Rad). For semiquantitative PCR, GAPDH was used as an internal control to evaluate total RNA input, as previously described by our group (38).…”

Section: Methodsmentioning

confidence: 99%

Improving insulin sensitivity via activation of PPAR-γ increases telomerase activity in the heart of OLETF rats

Makino¹,

Maeda²,

Oyama³

et al. 2009

American Journal of Physiology-Heart and Circulatory Physiology

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ing insulin sensitivity via activation of PPAR-␥ increases telomerase activity in the heart of OLETF rats. Am J Physiol Heart Circ Physiol 297: H2188 -H2195, 2009. First published October 23, 2009 doi:10.1152/ajpheart.00421.2009.-This study was conducted to examine telomere biology in terms of improving insulin sensitivity in a type 2 diabetic animal model: Otsuka Long-Evans Tokushima fatty (OLETF) rats. To improve insulin sensitivity, pioglitazone (PG; 10 mg ⅐ kg Ϫ1 ⅐ day Ϫ1 ) was administrated to OLETF rats from 20 to 40 wk of age, and the effects of treatment were compared with those in untreated OLETF or control Long-Evans Tokushima Otsuka fatty rats. At the end of the study, the homeostasis model assessment of insulin resistance significantly increased in OLETF rats but decreased in OLETF rats treated with PG. No shortening of telomere length was observed in the heart tissue of OLETF rats, whereas telomerase activity was decreased in OLETF heart tissue. The mRNA expression of both telomerase reverse transcriptase and telomere repeat binding factor 2 was downregulated in the hearts of OLETF rats. The protein expression of phospho-Akt, insulin-like growth factor, and endothelial nitric oxide synthase was reduced in OLETF rats. On the other hand, myocardial matrix metalloproteinase-9 expression was elevated in OLETF rats. The changes observed in OLETF rats were inhibited by PG treatment. However, protein and mRNA expression of Sirt1, a lifespan modulator, were attenuated in OLETF rat hearts, although they were enhanced in OLETF rats with PG treatement. Myocardial fibrosis was less extensive and diastolic dysfunction more greatly ameliorated in PG-treated OLETF rats than in OLETF rats. These findings suggest that improving insulin sensitivity via the activation of peroxisom proliferator-activated receptor-␥ may exert regulatory effects on cardiac telomere biology and may have desirable morphological and functional effects on the diabetic heart.

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“…47 Therefore, we examined the possible interaction of SHP-1 and ATIP and found that AT 2 receptor stimulation increases the formation of ATIP and SHP-1complex and their translocation into the nucleus and enhances cell differentiation in rat neurons. 38 In contrast, Sugano et al recently demonstrated that treatment with small interfering RNA (siRNA) against SHP-1 in acute myocardial ischemia markedly reduced the infarct size 48 and accelerated angiogenesis through increased phosphorylation of KDR/flk-1, 49 suggesting that knocking down of SHP-1 has beneficial effects on ischemic disease. However, the involvement of Ang II in these experiments is not clear.…”

Section: Shp-1mentioning

confidence: 98%

Emerging Concepts of Regulation of Angiotensin II Receptors

Mogi

Iwai

Horiuchi

2007

ATVB

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Abstract-Angiotensin (Ang II) is the principal vasoactive substance of the renin-angiotensin system (RAS), having a variety of physiological actions including vasoconstriction, aldosterone release, and cell growth. 1 Ang II binds 2 major receptors: the Ang II type-1 (AT 1 ) receptor and type-2 (AT 2 ) receptor. The majority of well-known Ang II actions are mediated via AT 1 receptor stimulation, and angiotensin converting enzyme inhibitors (ACEI) and AT 1 receptor blockers (ARBs) have been widely used as antihypertensive drugs, with the expectation of cardiovascular protective effects. AT 2 receptor stimulation by unbound Ang II could also be expected during treatment with ARBs. Recent accumulating evidence has suggested that the AT 2 receptor not only opposes the AT 1 receptor but also has unique effects beyond an interaction with AT 1 receptor signaling. On the other hand, recent experimental studies have also demonstrated the existence of proteins interacting with Ang II receptors by screening with a yeast-based 2-hybrid protein-protein interaction assay technique and revealed their functions (Table). [2][3][4][5][6][7][8][9] Therefore, recent advances in studies of Ang II receptors could prove the existence of a variety of new players and targets in addition to the traditional "Ang II world" and provide a new insight into cardiovascular biology. Here, we have summarized these emerging concepts concerning Ang II receptor interacting proteins and discuss new potent therapeutic targets in cardiovascular disease.

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RNA interference targeting SHP‐1 attenuates myocardial infarction in rats

Cited by 36 publications

References 32 publications

Src Homology Domain 2-containing Protein-tyrosine Phosphatase-1 (SHP-1) Binds and Dephosphorylates Gα-interacting, Vesicle-associated Protein (GIV)/Girdin and Attenuates the GIV-Phosphatidylinositol 3-Kinase (PI3K)-Akt Signaling Pathway

Src Homology Domain 2-containing Protein-tyrosine Phosphatase-1 (SHP-1) Binds and Dephosphorylates Gα-interacting, Vesicle-associated Protein (GIV)/Girdin and Attenuates the GIV-Phosphatidylinositol 3-Kinase (PI3K)-Akt Signaling Pathway

Improving insulin sensitivity via activation of PPAR-γ increases telomerase activity in the heart of OLETF rats

Emerging Concepts of Regulation of Angiotensin II Receptors

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