Abstract
Protein tyrosine phosphatases (PTPs) are a large family of signaling enzymes playing critical role in signal transduction and regulation of cellular processes. Dysfunction of PTP activity is associated with diabetes, cancer, autoimmune disorders, and neural diseases. PTP inhibitors therefore emerged as promising therapeutic targets. Recent research indicates that besides small organic molecules, metal ions and metal complexes can also strongly inhibit PTPs both in vitro and in vivo, resulting in the increase of phosphorylation of corresponding substrates and the modulation of cellular process. Structure of metal complexes influences the potency and selectivity of PTP inhibition. Detailed studies on this subject are not only expected to yield metal-based drugs targeting individual PTPs, but also to support understanding the function of metals in organisms. This review focuses on recent advancements in this area of research.
Keywords: Protein tyrosine phosphatases, inhibitor, metal ions, vanadium complexes, copper complexes, zinc complexes, gold complexes, metal complexes, selectivity, phosphorylation, HPTP
Anti-Cancer Agents in Medicinal Chemistry
Title: Metal-Based Inhibitors of Protein Tyrosine Phosphatases
Volume: 11 Issue: 1
Author(s): Liping Lu and Miaoli Zhu
Affiliation:
Keywords: Protein tyrosine phosphatases, inhibitor, metal ions, vanadium complexes, copper complexes, zinc complexes, gold complexes, metal complexes, selectivity, phosphorylation, HPTP
Abstract: Protein tyrosine phosphatases (PTPs) are a large family of signaling enzymes playing critical role in signal transduction and regulation of cellular processes. Dysfunction of PTP activity is associated with diabetes, cancer, autoimmune disorders, and neural diseases. PTP inhibitors therefore emerged as promising therapeutic targets. Recent research indicates that besides small organic molecules, metal ions and metal complexes can also strongly inhibit PTPs both in vitro and in vivo, resulting in the increase of phosphorylation of corresponding substrates and the modulation of cellular process. Structure of metal complexes influences the potency and selectivity of PTP inhibition. Detailed studies on this subject are not only expected to yield metal-based drugs targeting individual PTPs, but also to support understanding the function of metals in organisms. This review focuses on recent advancements in this area of research.
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Cite this article as:
Lu Liping and Zhu Miaoli, Metal-Based Inhibitors of Protein Tyrosine Phosphatases, Anti-Cancer Agents in Medicinal Chemistry 2011; 11 (1) . https://dx.doi.org/10.2174/187152011794941271
DOI https://dx.doi.org/10.2174/187152011794941271 |
Print ISSN 1871-5206 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5992 |
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