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Toxicological disruption of signaling homeostasis: Tyrosine phosphatses as targets
Citation:
SAMET, J. M. AND T. Tal. Toxicological disruption of signaling homeostasis: Tyrosine phosphatses as targets. Annual Review of Pharmacology and Toxicology. Annual Reviews Inc., Palo Alto, CA, 50(1):215-235, (2010).
Impact/Purpose:
The protein tyrosine phosphatases (PTP) comprise a diverse group of enzymes whose activity opposes that of the tyrosine kinases
Description:
The protein tyrosine phosphatases (PTP) comprised a diverse group of enzymes whose activity opposes that of the tyrosine kinases. As such, the PTP have critical roles in maintaining signaling quiescence in resting cells and in restoring homeostasis by effecting signal termination. Interest in these enzymes has increased in recent years following the discovery that the activity of PTP is modulated through redox mechanisms during signaling. The molecular features that enable redox regulation of PTP during physiological signaling also render them highly susceptible to oxidative and electrophilic inactivation by a broad spectrum of structurally disparate xenobiotics compounds. The loss of PTP activity results in a profound disregulation of protein phosphotyrosine metabolism, leading to widespread and persistent activation of signaling cascades in the cell. The research described herein has been reviewed by the National Health and Environmental Effects Research Laboratory and has been approved for publication. Approval does not signify that the contents necessarily reflect the views and policies of the U.S. EPA, nor does mention of trade names constitute endorsement of recommendation for use.
