IMR Press / FBL / Volume 11 / Issue 3 / DOI: 10.2741/1956

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.

The tyrosine phosphatase HD-PTP is regulated by FGF-2 through proteasome degradation
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1 Department of Preclinical Sciences, University of Milan Medical School, Via GB Grassi, 74 Milan, Italy
2 Molecular Oncology Unit, DIBIT and CNR Institute of Bioimaging and Molecular Physiology, H. San Raffaele, Via Olgettina 58 Milan, Italy
Front. Biosci. (Landmark Ed) 2006, 11(3), 2138–2143;
Published: 1 September 2006

Angiogenesis is essential in development and wound healing and contributes to the pathogenesis of many diseases. The signalling pathways activated in angiogenesis are, in part ,known and the overall tyrosine phosphorylation of cellular proteins plays a relevant role. By RNA fingerprinting, we isolated a tyrosine phosphatase, HD-PTP, modulated in human endothelial cells exposed to human immunodeficiency virus type 1 Tat, a viral protein known to be angiogenic. For the first time, we describe HD-PTP at the protein level. HD-PTP, a 185 kDa cytosolic protein which is expressed in endothelial cells of different origin. We show that HD-PTP is upregulated by Tat at the mRNA but not at the protein level. HD-PTP protein is differentially modulated by two angiogenic growth factors. While Vascular Endothelial Growth Factor does not affect protein levels, Fibroblast Growth Factor-2 induces HD-PTP degradation via the proteasome system.

Fibroblast Growth Factor
Vascular Endothelial Growth Factor
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