Clinicopathological and Prognostic Significance of PRMT5 in Cancers: A System Review and Meta-Analysis

Abstract

Purpose Since protein arginine methyltransferase 5 (PRMT5) is abnormally expressed in various tumors, in this study we aim to assess the association between PRMT5 and clinicopathological and prognostic features. Methods Electronic databases including PubMed, Web of Science, Scopus, ScienceDirect, and the Cochrane Library were searched until July 25, 2021. The critical appraisal of the eligible studies was performed using the Newcastle–Ottawa Quality Assessment Scale. Pooled hazard ratios (HR) and pooled odds ratios (OR) were calculated to assess the effect. Engauge Digitizer version 12.1, STATA version 15.1, and R version 4.0.5 were used to obtain and analysis the data. Results A total of 32 original studies covering 15,583 patients were included. In our data, it indicated that high level of PRMT5 was significantly correlated with advanced tumor stage (OR = 2.12, 95% CI: 1.22-3.70, P =.008; I2 = 80.7%) and positively correlated with poor overall survival (HR = 1.59, 95% CI: 1.46-1.73, P < .001; I2 = 50%) and progression-free survival (HR = 1.53, 95% CI: 1.24-1.88, P < .001; I2 = 0%). In addition, sub-group analysis showed that high level of PRMT5 was associated with poor overall survival for such 5 kinds of cancers as hepatocellular carcinoma, pancreatic cancer, breast cancer, gastric cancer, and lung cancer. Conclusion For the first time we found PRMT5 was pan-cancerous as a prognostic biomarker and high level of PRMT5 was associated with poor prognosis for certain cancers.

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“… 4 Protein arginine methyltransferase 5 (PRMT5) is a kind of protein arginine methylase, as a key enzyme involved in gene transcription regulation and signal transduction DNA repair damage and cell proliferation and other biological processes. 5 At the same time, PRMT5 clearly catalyzes the symmetric methylation of multiple histone and non‐histone substrates in vivo and plays an important role in regulating multiple cell processes. 6 , 7 In the nucleus, PRMT5 can interact with SWI/SNF, catalyze the symmetrical dimethylation of the substrates of histone H2A arginine 3 (H2AR3me2s), histone H3 arginine 8 (H3R8me2s) and histone H4 arginine 3 (H4R3me2s), and inhibit the transcription of downstream cycle regulators and tumor suppressor genes.…”