Ptprm-KO Mouse

Ptprm, also known as Protein tyrosine phosphatase receptor type M, is a transmembrane receptor type tyrosine phosphatase. It plays crucial roles in multiple biological processes.

In the nervous system, it is critical for synapse formation regulated by zinc ions, which is essential for normal mammalian brain development and information transmission [1]. It is also involved in cell adhesion via its extracellular domains and cell signaling via its cytoplasmic phosphatase domains [9].

In cancer research, PTPRM shows diverse functions. In small intestinal neuroendocrine tumors (SI-NETs), it is a candidate tumor suppressor gene as its overexpression reduces cell growth and proliferation and induces apoptosis [2]. In glioblastoma, FN1-induced PTPRM methylation promotes tumor development by activating STAT3 signalling [3]. In non-small cell lung cancer, circRNA PTPRM promotes cancer progression by modulating the miR-139-5p/SETD5 axis [4]. In pancreatic cancer, decreased PTPRM in plasma is associated with poor prognosis [5]. In cervical cancer, high expression of PTPRM predicts poor prognosis and promotes tumor growth and lymph node metastasis [6]. In colorectal cancer, loss of PTPRM is associated with the adenoma-carcinoma sequence and its inactivation promotes oncogenic cell growth [8]. In spermatogonia, BMI1 promotes their proliferation through epigenetic repression of Ptprm [7].

In conclusion, Ptprm is involved in synapse formation in the nervous system and has complex roles in various cancers, either as a potential tumor suppressor or a promoter of cancer progression. The study of Ptprm using gene-knockout or related models helps to understand its functions in normal and disease-related biological processes, providing insights for potential therapeutic strategies in cancer and understanding brain function [1-8].

References:

1. Mo, Xiaoqiang, Liu, Mengxue, Gong, Jihong, Yang, Xiaofei, Li, Jun. 2022. PTPRM Is Critical for Synapse Formation Regulated by Zinc Ion. In Frontiers in molecular neuroscience, 15, 822458. doi:10.3389/fnmol.2022.822458. https://pubmed.ncbi.nlm.nih.gov/35386272/

2. Barazeghi, Elham, Hellman, Per, Westin, Gunnar, Stålberg, Peter. . PTPRM, a candidate tumor suppressor gene in small intestinal neuroendocrine tumors. In Endocrine connections, 8, 1126-1135. doi:10.1530/EC-19-0279. https://pubmed.ncbi.nlm.nih.gov/31349215/

3. Song, Jian, Zhao, Di, Sun, Guozhu, Lv, Zhongqiang, Jiao, Baohua. . PTPRM methylation induced by FN1 promotes the development of glioblastoma by activating STAT3 signalling. In Pharmaceutical biology, 59, 904-911. doi:10.1080/13880209.2021.1944220. https://pubmed.ncbi.nlm.nih.gov/34225581/

4. Jiang, Zeyong, Zhao, Jian, Zou, Hanlin, Cai, Kaican. . CircRNA PTPRM Promotes Non-Small Cell Lung Cancer Progression by Modulating the miR-139-5p/SETD5 Axis. In Technology in cancer research & treatment, 21, 15330338221090090. doi:10.1177/15330338221090090. https://pubmed.ncbi.nlm.nih.gov/35491723/

5. Sahni, Sumit, Krisp, Christoph, Molloy, Mark P, Samra, Jaswinder, Mittal, Anubhav. 2020. PSMD11, PTPRM and PTPRB as novel biomarkers of pancreatic cancer progression. In Biochimica et biophysica acta. General subjects, 1864, 129682. doi:10.1016/j.bbagen.2020.129682. https://pubmed.ncbi.nlm.nih.gov/32663515/

6. Liu, Pan, Zhang, Chunyu, Liao, Yuandong, Wang, Wei, Yao, Shuzhong. 2020. High expression of PTPRM predicts poor prognosis and promotes tumor growth and lymph node metastasis in cervical cancer. In Cell death & disease, 11, 687. doi:10.1038/s41419-020-02826-x. https://pubmed.ncbi.nlm.nih.gov/32826853/

7. Zhang, Ke, Xu, Jinfu, Ding, Yue, Xue, Boxin, Zheng, Bo. 2021. BMI1 promotes spermatogonia proliferation through epigenetic repression of Ptprm. In Biochemical and biophysical research communications, 583, 169-177. doi:10.1016/j.bbrc.2021.10.074. https://pubmed.ncbi.nlm.nih.gov/34739857/

8. Sudhir, Putty-Reddy, Lin, Shiu-Ting, Chia-Wen, Chien, Jou, Yuh-Shan, Chen, Jeou-Yuan. 2015. Loss of PTPRM associates with the pathogenic development of colorectal adenoma-carcinoma sequence. In Scientific reports, 5, 9633. doi:10.1038/srep09633. https://pubmed.ncbi.nlm.nih.gov/25910225/

9. Hay, Iain M, Shamin, Maria, Caroe, Eve R, Sharpe, Hayley J, Deane, Janet E. 2022. Determinants of receptor tyrosine phosphatase homophilic adhesion: Structural comparison of PTPRK and PTPRM extracellular domains. In The Journal of biological chemistry, 299, 102750. doi:10.1016/j.jbc.2022.102750. https://pubmed.ncbi.nlm.nih.gov/36436563/