Metal-Based Inhibitors of Protein Tyrosine Phosphatases

ISSN: 1875-5992 (Online)
ISSN: 1871-5206 (Print)


Volume 16, 12 Issues, 2016


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Anti-Cancer Agents in Medicinal Chemistry

Formerly: Current Medicinal Chemistry - Anti-Cancer Agents

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  • 27th of 59 in Chemistry, Medicinal

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Editor-in-Chief:
Michelle Prudhomme
Universite Blaise Pascal - C.N.R.S
Aubiere Cedex
France


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Metal-Based Inhibitors of Protein Tyrosine Phosphatases



Anti-Cancer Agents in Medicinal Chemistry, 11(1): 164-171.

Author(s): Liping Lu and Miaoli Zhu.

Affiliation: Institute of Molecular Science, Shanxi University, 92 Wucheng Road, Taiyuan, Shanxi 030006, People's Republic of China.

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.



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Article Details

Volume: 11
Issue Number: 1
First Page: 164
Last Page: 171
Page Count: 8
DOI: 10.2174/187152011794941271
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