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PTPRK was identified as a direct target of miR (show MLXIP Proteins)-1260b, and PTPRK expression was inversely correlated with miR (show MLXIP Proteins)-1260b in non-small cell lung cancer cell lines and clinical tissues
Study found a significant association between PTPRK genetic variants and the risk and age at onset of Alzheimer's disease in two independent samples, and provided initial evidence of several genetic variants in PTPRK influencing the risk of cancer and cholesterol levels.
The present study identified RSPO (show RSPO1 Proteins) fusion transcripts, including three novel transcripts, in one-third of colorectal Traditional serrated adenoma (TSA (show PRDX2 Proteins)) and showed that PTPRK-RSPO3 (show RSPO3 Proteins) fusions were the predominant cause of RSPO (show RSPO1 Proteins) overexpression in colorectal TSA (show PRDX2 Proteins).
PTPRK plays dual roles in coordinating angiogenesis. It plays a positive role in cell proliferation, adhesion and tubule formation, but suppresses cell migration, in particular, the FGF-promoted migration.
PTPRK-RSPO3 (show RSPO3 Proteins) fusions and RNF43 (show RNF43 Proteins) mutations were found to be characteristic genetic features of traditional serrated adenomas (TSAs).
By regulating phosphorylation of SRC, RPTPkappa promotes the pathogenic action of rheumatoid arthritis fibroblast-like synoviocytes, mediating cross-activation of growth factor and inflammatory cytokine signalling by TGFbeta in RA FLS.
Notch (show NOTCH1 Proteins) and TGF-beta (show TGFB1 Proteins) act in concert to stimulate induction of PTPRK, which suppresses EGFR (show EGFR Proteins) activation in human keratinocytes.
Findings strongly indicate that the tyrosine phosphorylation of CD133, which is dephosphorylated by PTPRK, regulates AKT (show AKT1 Proteins) signaling and has a critical role in colon cancer progression.
PTPRK underexpression leads to STAT3 (show STAT3 Proteins) activation and contributes to nasal NK/T-cell lymphoma pathogenesis
PTPRK showed lower mRNA expression in duodenal mucose of celiac disease patients.
RPTP-kappa is proteolytically processed to isoforms that have opposing effects on beta-catenin (show CTNNB1 Proteins) activity.
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 catalytic domains, and thus represents a receptor-type PTP. The extracellular region contains a meprin-A5 antigen-PTP mu (MAM) domain, an Ig-like domain and four fibronectin type III-like repeats. This PTP was shown to mediate homophilic intercellular interaction, possibly through the interaction with beta- and gamma-catenin at adherens junctions. Expression of this gene was found to be stimulated by TGF-beta 1, which may be important for the inhibition of keratinocyte proliferation.
dJ480J14.2.1 (protein tyrosine phosphatase, receptor type, K (R-PTP-KAPPA, protein tyrosine phosphatase kappa , protein tyrosine phosphatase kappa
, protein-tyrosine phosphatase kappa
, protein-tyrosine phosphatase, receptor type, kappa
, receptor-type tyrosine-protein phosphatase kappa
, protein tyrosine phosphatase, receptor type, K, extracellular region
, receptor-like protein tyrosine phosphatase kappa extracellular region (RPTPK)