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extract of Perilla stem inhibits Src homology phosphatase-1 [SHP]-1 and influences insulin signaling
Pakistan Journal of Pharmaceutical Sciences. 2015; 28 (2): 421-424
in En | IMEMR | ID: emr-178135
Responsible library: EMRO
Protein tyrosine phosphatases [PTPs] are enzymes that catalyze protein tyrosine dephosphorylation of which Src homology phosphatase-1 [SHP-1] is one of the best-validated, a widely distributed intracellular tyrosine phosphatase that contains two SH2 domains. Down regulation of SHP-1 tyrosine phosphatases was significantly increased sensitivity to insulin in insulin signaling pathway. Through in vitro enzymatic reaction kinetics experiment, we found that the extract of Perilla stem was a potential inhibitor to [delta]SHP-1, the catalytic domain of SHP-1 protein tyrosine phosphatase, and its IC[50] was 4ug/ml, and was more sensitive towards SHP-1than other PTPs, which indicated that SHP-1 might be a target of the extract of Perilla stem. It can strengthened the level of tyrosine phosphorylation of insulin receptor [IR] and extracellular signal-regulated protein kinase [ERK] in HepG2 cells, and then activated the insulin signaling pathway through inhibiting the protein phosphorylation of SHP-1. These results demonstrated that the extract of Perilla stem could play an important role for diabetes treatment through inhibiting the level of SHP-1 in insulin signaling pathway
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Index: IMEMR Main subject: Insulin Resistance / Plant Extracts / Plant Stems / Protein Tyrosine Phosphatase, Non-Receptor Type 6 / Insulin Language: En Journal: Pak. J. Pharm. Sci. Year: 2015
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Index: IMEMR Main subject: Insulin Resistance / Plant Extracts / Plant Stems / Protein Tyrosine Phosphatase, Non-Receptor Type 6 / Insulin Language: En Journal: Pak. J. Pharm. Sci. Year: 2015