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Protein Tyrosine Phosphatase 1B Inhibition: Opportunities and Challenges

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Abstract:

Protein tyrosine phosphatase 1B (PTP1B) has been implicated as one of the key negative regulators of insulin and leptin signal transduction pathways. PTP1B deficient mice are more sensitive to insulin, and have improved glycemic control and resistance to diet-induced obesity than the wild-type control mice. Inhibiting PTP1B action using antisense oligonucleotides and small molecule inhibitors represents novel therapeutic approach for the treatment of insulin resistance, type II diabetes, and obesity. The rapid development of this field is evidenced by the increasing number of patents and publications in recent years. This review will highlight the recent advances in various approaches for attenuating PTP1B action, particularly small molecule PTP1B inhibitors, and the challenges associated with developing PTP1B inhibitors with drug like properties.

Keywords: antisense oligonucleotide; cellular permeability; insulin resistance; obesity; phosphotyrosyl mimetics; protein tyrosine phosphatase; second phosphotyrosyl binding site; structure-based drug design; type II diabetes

Document Type: Review Article

DOI: http://dx.doi.org/10.2174/0929867033457296

Affiliations: Metabolic Disease Research, R4MC, AP10, Abbott Laboratories, Abbott Park, IL 60064- 6098, USA.

Publication date: August 1, 2003

More about this publication?
  • Current Medicinal Chemistry covers all the latest and outstanding developments in medicinal chemistry and rational drug design. Each issue contains a series of timely in-depth reviews written by leaders in the field covering a range of the current topics in medicinal chemistry. Current Medicinal Chemistry is an essential journal for every medicinal chemist who wishes to be kept informed and up-to-date with the latest and most important developments.
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