Disease relevance of PTPN23

• 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 [1].

High impact information on PTPN23

• Expression analysis and modulation by HIV-Tat of the tyrosine phosphatase HD-PTP [2].
• By RNA fingerprinting, we found that Tat upregulates the tyrosine phosphatase HD-PTP mRNA in a human endothelial cell line [2].
• HD-PTP mRNA was also detected in cell lines derived from tumors that develop in BKV/Tat-transgenic mice [2].
• HD-PTP encodes a 185-kDa protein which is expressed in human endothelial from the umbilical cord and in human Kaposi-spindle cells [2].
• We here show that HD-PTP is highly conserved through evolution from yeast to man, and is ubiquitously distributed in adult and fetal tissues [2].

Biological context of PTPN23

• HD-PTP is expressed in human cell lines derived from different tumors, but the mRNA levels do not appear to correlate with the malignant phenotype of the cells [2].

Anatomical context of PTPN23

• While Vascular Endothelial Growth Factor does not affect protein levels, Fibroblast Growth Factor-2 induces HD-PTP degradation via the proteasome system [1].

Analytical, diagnostic and therapeutic context of PTPN23

• We confirmed the interactions in a mammalian system by Strep-pulldown assays in which pulldown products from the lysates of HEK293T cells expressing either Strep-tagged HD-PTP alone or co-expressing with epitope-tagged proteins were analyzed by Western blotting using specific antibodies [3].

References