ptprk - Synonyms for ptprk | Synonyms Of ptprk

Examples of "ptprk"
Patients with reduced PTPRK transcript expression have shorter breast cancer survival times and are more likely to have breast cancer metastases or to die from breast cancer. In an experimental model of breast cancer, PTPRK was reduced in breast cancer cell lines with PTPRK ribozymes. In these cells, adhesion to matrigel, transwell migration, and cell growth were all increased following the reduction of PTPRK expression, again supporting a function for PTPRK as a tumor suppressor.
Receptor-type tyrosine-protein phosphatase kappa is an enzyme that in humans is encoded by the "PTPRK" gene. PTPRK is also known as PTPkappa and PTPκ.
NPNT; NRP1; NRP2; PRSS7; PTPRK; PTPRM; PTPRO; PTPRT;
PTPRH; PTPRJ; PTPRK; PTPRM; PTPRO; PTPRS; PTPRT; PTPRU;
PTPRK mRNA was shown to be significantly reduced by RT-PCR in human lung cancer-derived cell lines.
Alternative splicing of exons 16, 17a, and 20a has been described for PTPRK. Two novel forms of PTPRK were identified from mouse full-length cDNA sequences and were predicted to result in two PTPkappa splice variants: a secreted form of PTPkappa and a membrane tethered form.
PTPRK has also been shown to be downregulated in response to androgen stimulation in human LNCaP prostate cancer cells. The mechanism whereby PTPRK is downregulated is via the expression of a microRNA, miR-133b, which is upregulated in response to androgen stimulation.
Types include PTPRA, PTPRB, PTPRC, PTPRD, PTPRE, PTPRF, PTPRG, PTPRH, PTPRJ, PTPRK, PTPRM, PTPRN, PTPRN2, PTPRO, PTPRQ, PTPRR, PTPRS, PTPRT, PTPRU, and PTPRZ.
Assem and colleagues identified loss of heterozygosity (LOH) events in malignant glioma specimens, and identified PTPRK as a significant gene candidate in one LOH region. A significant correlation between the presence of PTPRK mutations and short patient survival time was observed. PTPRK was amplified from tumor cDNA to confirm the LOH observed. In these specimens, 6 different mutations were observed, two of which (one in each phosphatase domain) disrupted the enzymatic activity of PTPRK. Expression of wild-type PTPkappa in U87-MG and U251-MG cells resulted in a reduction in cell proliferation, migration and invasion. Expression of the variants of PTPkappa with mutations in the phosphatase domains, however, increased cell proliferation, migration and invasion, supporting a role for the involvement of the mutated variants of PTPkappa in tumorigenicity.
The human PTPRK gene is located on the long arm of chromosome 6, a putative tumor suppressor region of the genome.
Using a transposon-based genetic screen, researchers found that disruption of the PTPRK gene in gastrointestinal tract epithelium resulted in an intestinal lesion, classified as either an intraepithelial neoplasia, an adenocarcinoma or an adenoma.
PTPkappa is expressed in human keratinocytes. TGFβ1 is a growth inhibitor in human keratinocytes. Stimulation of the cultured human keratinocyte cell line, HaCaT, with TGFβ1 increases the levels of PTPkappa (PTPRK) mRNA as assayed by northern blot analysis. TGFβ1 also increased PTPkappa mRNA and protein in normal and tumor mammary cell lines. HER2 overexpression reduced PTPkappa mRNA and protein expression.
Using a β-galactosidase (β-gal) reporter gene inserted into the phosphatase domain of the murine PTPkappa (PTPRK) gene, Shen and colleagues determined the detailed expression pattern of endogenous PTPRK. β-gal activity was observed in many areas of the adult forebrain, including layers II and IV, and to a lesser extent in layer VI of the cortex. β-gal activity was also observed in apical dendrites of cortical pyramidal cells, the granule layer of the olfactory and accessory olfactory bulbs, the anterior hypothalamus, paraventricular nucleus, and in granule and pyramidal layers of the dentate gyrus and CA 1-3 regions of the hippocampus. In the midbrain, β-gal was observed in the subthalamic nucleus, the superior and inferior colliculi and in the red nucleus. β-gal activity was also observed in the neural retina, in the inner nuclear layer and in small ganglion cells of the ganglion cell layer.
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP possesses an extracellular region, a single transmembrane region, and two tandem intracellular catalytic tyrosine phosphatase domains, and thus represents a receptor-type PTP (RPTP). The extracellular region contains a meprin-A5 antigen-PTPmu (MAM) domain, one Ig-like domain and four fibronectin type III-like repeats, and thus is a member of the type R2B RPTP family. It was cloned by many groups and given different names, including PCP-2, PTP pi, PTP lambda, hPTP-J, PTPRO, and PTP psi. Other type R2B RPTPs include PTPRM, PTPRK, and PTPRT. Analysis of the genomic structure of PCP-2 suggests that it is the most distantly related of the type R2B RPTPS.
This PTP possesses an extracellular region, a single transmembrane region, and two tandem intracellular catalytic domains, and thus represents a receptor-type PTP (RPTP). The extracellular region contains a meprin-A5 antigen-PTPmu (MAM) domain, one Ig-like domain and four fibronectin type III-like repeats. PTPrho is a member of the type R2B subfamily of RPTPs, which also includes the RPTPs PTPmu (PTPRM), PTPkappa (PTPRK), and PCP-2 (PTPRU). Comparison of R2B cDNA sequences identified that PTPmu is most closely related to PTPrho. PTPrho is alternatively spliced. Alternative splicing of exons 14, 16, and 22a have been described for PTPrho (PTPRT). Two alternatively spliced transcript variants of this gene, which encode distinct proteins, have been reported. The first isoform encodes the larger version of the protein. The second variant lacks a region of the extracellular domain between the fourth FNIII domain and the transmembrane domain and in the juxtamembrane domain.