Ptprf, Protein Tyrosine Phosphatase Receptor Type F, is an important phosphatase involved in regulating cell growth, differentiation, and oncogenic transformation [2]. It localizes to adherens junctions and may be involved in the regulation of epithelial cell-cell contacts, peptide growth factor signaling, and the canonical Wnt pathway [6].

In cancer research, in lung adenocarcinoma, Fascin Actin-Bundling Protein 1 (FSCN1) promotes the secretion of cytokines in tumor cells, which in turn increase PTPRF expression in macrophages, leading to M2 polarization of macrophages and tumor progression. Knocking down PTPRF in macrophages reduces lung adenocarcinoma proliferative and metastatic capacity [1]. In gastric adenocarcinoma, lower PTPRF levels are associated with advanced tumor TNM stages and poorer overall survival. Overexpressing PTPRF inhibits tumor migration and invasion by deactivating the ERK1/2 signaling pathway [2]. In breast cancer, PPARγ inhibits tumor cell proliferation by upregulating PTPRF expression [3]. In gliomas, lncRNA TCONS_00004099-derived microRNA promotes glioma malignant behaviors through targeting PTPRF [4]. In non-small-cell lung cancer, PTPRF expression is prognostic for shorter overall survival but predictive of improved survival with erlotinib [5]. In gall bladder carcinoma, downregulation of PTPRF is noted during the expression of miR-145 [7].

In conclusion, Ptprf plays a crucial role in various biological processes and disease conditions, especially in cancer development and progression. Studies on Ptprf using gene-related models have provided valuable insights into its functions in different diseases, which may help in developing new therapeutic strategies.

References:

1. Huang, Yiwei, Shan, Guangyao, Yi, Yanjun, Jiang, Wei, Zhan, Cheng. 2022. FSCN1 induced PTPRF-dependent tumor microenvironment inflammatory reprogramming promotes lung adenocarcinoma progression via regulating macrophagic glycolysis. In Cellular oncology (Dordrecht, Netherlands), 45, 1383-1399. doi:10.1007/s13402-022-00726-0. https://pubmed.ncbi.nlm.nih.gov/36223033/

2. Tian, Xiang'an, Yang, Chengju, Yang, Liguang, Sun, Qinli, Liu, Naiqing. 2018. PTPRF as a novel tumor suppressor through deactivation of ERK1/2 signaling in gastric adenocarcinoma. In OncoTargets and therapy, 11, 7795-7803. doi:10.2147/OTT.S178152. https://pubmed.ncbi.nlm.nih.gov/30464527/

3. Xu, Y-Y, Liu, H, Su, L, Bed-David, Y, Li, Y-J. . PPARγ inhibits breast cancer progression by upregulating PTPRF expression. In European review for medical and pharmacological sciences, 23, 9965-9977. doi:10.26355/eurrev_201911_19563. https://pubmed.ncbi.nlm.nih.gov/31799666/

4. Wang, Yuhao, Shan, Aijun, Zhou, Zhiwei, Du, Bo, Lei, Bingxi. . LncRNA TCONS_00004099-derived microRNA regulates oncogenesis through PTPRF in gliomas. In Annals of translational medicine, 9, 1023. doi:10.21037/atm-21-2442. https://pubmed.ncbi.nlm.nih.gov/34277823/

5. Soulières, Denis, Hirsch, Fred R, Shepherd, Frances A, Shames, David S, Klughammer, Barbara. . PTPRF Expression as a Potential Prognostic/Predictive Marker for Treatment with Erlotinib in Non-Small-Cell Lung Cancer. In Journal of thoracic oncology : official publication of the International Association for the Study of Lung Cancer, 10, 1364-1369. doi:10.1097/JTO.0000000000000624. https://pubmed.ncbi.nlm.nih.gov/26291013/

6. Borck, Guntram, de Vries, Liat, Wu, Hsin-Jung, Kubisch, Christian, Basel-Vanagaite, Lina. 2014. Homozygous truncating PTPRF mutation causes athelia. In Human genetics, 133, 1041-7. doi:10.1007/s00439-014-1445-1. https://pubmed.ncbi.nlm.nih.gov/24781087/

7. Zhao, Weiwei, Gong, Yanxuan, Chen, Yugang. 2022. MRNA Profiling Involved in Triggering of STAT1 with Regulatory Involvement of IRF7, PTPRF, and miR-145p in Patients Suffering from Gall Bladder Carcinoma. In Journal of healthcare engineering, 2022, 1770643. doi:10.1155/2022/1770643. https://pubmed.ncbi.nlm.nih.gov/35035811/