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PMID:24481115

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Citation

Chen, YP, Yang, CG, Wei, PY, Li, L, Luo, DQ, Zheng, ZH and Lu, XH (2014) Penostatin Derivatives, a Novel Kind of Protein Phosphatase 1B Inhibitors Isolated from Solid Cultures of the Entomogenous Fungus Isaria tenuipes. Molecules 19:1663-71

Abstract

Protein tyrosine phosphatase 1B (PTP1B) is implicated as a negative regulator of insulin receptor (IR) signaling and a potential drug target for the treatment of type II diabetes and other associated metabolic syndromes. Therefore, small molecular inhibitors of PTP1B can be considered as an attractive approach for the design of new therapeutic agents of type II diabetes diseases. In a continuing search for new protein phosphatase inhibitors from fungi, we have isolated a new compound, named penostatin J (1), together with three known ones, penostatin C (2), penostatin A (3), and penostatin B (4), from cultures of the entomogenous fungus Isaria tenuipes. The structure of penostatin J (1) was elucidated by extensive spectroscopic analysis. We also demonstrate for the first time that penostatin derivatives exhibit the best PTP1B inhibitory action. These findings suggest that penostatin derivatives are a potential novel kind of PTP1B inhibitors.

Links

PubMed Online version:10.3390/molecules19021663

Keywords


Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

PIG:Q71M99

GO:0005769: early endosome

ECO:0000314:

C

Figure 1: This figure shows the similar structure between the protein Tyrosine Phosphate 1B and penostatin J and how they both are insulin receptors and are key in cell communication

complete
CACAO 9422

See also

References

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