SHP-1 in Cell-Cycle Regulation

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


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SHP-1 in Cell-Cycle Regulation



Anti-Cancer Agents in Medicinal Chemistry, 11(1): 89-98.

Author(s): Pilar Lopez-Ruiz, Javier Rodriguez-Ubreva, Ariel Ernesto Cariaga, Maria Alicia Cortes and Begona Colas.

Affiliation: Departamento de Bioquimica y Biologia Molecular, Universidad de Alcala, E-28871, Alcala de Henares-Madrid, Spain.

Abstract

The reversible phosphorylation of tyrosine residues in proteins, which is governed by the balanced action of protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs), is a key element of the signaling pathways that are involved in the control of cell proliferation. Deregulation of either of these key regulators leads to abnormal cell signaling, which is largely associated with human pathologies including cancer. This review focuses on recent studies on the role of the protein tyrosine phosphatase SHP-1 on cell-cycle regulation and its possible roles in tumour onset and progression. SHP-1 is a PTP with two SH2 domains that is expressed in haematopoietic cells and, moderately, in many other cell types, especially malignant epithelial cells. SHP-1 regulates cell proliferation, whether it is by controlling mitogenic pathways activated by receptors with tyrosine kinase activity, or by regulating components of the cell-cycle machinery such as CDK2, p27 and cyclin D1. Since several inhibitors targeting SHP-1 have demonstrated their value in cancer treatment, this phosphatase has been proposed as a therapeutic target for this pathology.

Keywords:

Protein tyrosine phosphatase, p27, CDK2, cyclin D, SH2 domain, cancer, PTPN6, PTKs, pRb, TCR, cGMP.



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Article Details

Volume: 11
Issue Number: 1
First Page: 89
Last Page: 98
Page Count: 10
DOI: 10.2174/187152011794941154
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