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Am J Physiol Heart Circ Physiol 281: H396-H403, 2001;
0363-6135/01 $5.00
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Vol. 281, Issue 1, H396-H403, July 2001

PTP-epsilon , a tyrosine phosphatase expressed in endothelium, negatively regulates endothelial cell proliferation

Larry J. Thompson1, Jihong Jiang1,2, Nageswara Madamanchi2, Marschall S. Runge2, and Cam Patterson2

1 Sealy Center for Molecular Cardiology, University of Texas Medical Branch, Galveston, Texas 77555; and 2 Department of Internal Medicine and Program in Molecular Cardiology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-7075

The vascular endothelium is a dynamic interface between the blood vessel and circulating factors and, as such, plays a critical role in vascular events like inflammation, angiogenesis, and hemostasis. Whereas specific protein tyrosine kinases have been identified in these processes, less is known about their protein tyrosine phosphatase (PTP) counterparts. We utilized a RT-PCR/differential hybridization assay to identify PTP-epsilon as a highly abundant endothelial cell PTP. PTP-epsilon mRNA expression is growth factor responsive, suggesting a role for this enzyme in endothelial cell proliferation. Overexpression of PTP-epsilon decreases proliferation by 60% in human umbilical vein endothelial cells (HUVEC) but not in smooth muscle cells or fibroblasts. In contrast, overexpression of PTP-epsilon (D284A), a catalytically inactive mutant, has no significant effect on HUVEC proliferation. These data provide the first functional characterization of PTP-epsilon in endothelial cells and identify a novel pathway that negatively regulates endothelial cell growth. Such a pathway may have important implications in vascular development and angiogenesis.

angiogenesis; signaling


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