Abstract

BackgroundBelonging to the protein arginine methyltransferase (PRMT) family, the enzyme encoded by coactivator associated arginine methyltransferase 1 (CARM1) catalyzes the methylation of protein arginine residues, especially acts on histones and other chromatin related proteins, which is essential in regulating gene expression. Beyond its well-established involvement in the regulation of transcription, recent studies have revealed a novel role of CARM1 in tumorigenesis and development, but there is still a lack of systematic understanding of CARM1 in human cancers. An integrated analysis of CARM1 in pan-cancer may contribute to further explore its prognostic value and potential immunological function in tumor therapy.ResultsBased on systematic analysis of data in multiple databases, we firstly verified that CARM1 is highly expressed in most tumors compared with corresponding normal tissues, and is bound up with poor prognosis in some tumors. Subsequently, relevance between CARM1 expression level and tumor immune microenvironment is analyzed from the perspectives of tumor mutation burden, microsatellite instability, mismatch repair genes, methyltransferases genes, immune checkpoint genes and immune cells infiltration, indicating a potential relationship between CARM1 expression and tumor microenvironment. A gene enrichment analysis followed shortly, which implied that the role of CARM1 in tumor pathogenesis may be related to transcriptional imbalance and viral carcinogenesis.ConclusionsOur first comprehensive bioinformatics analysis provides a broad molecular perspective on the role of CARM1 in various tumors, highlights its value in clinical prognosis and potential association with tumor immune microenvironment, which may furnish an immune based antitumor strategy to provide a reference for more accurate and personalized immunotherapy in the future.

Highlights

  • Belonging to the protein arginine methyltransferase (PRMT) family, the enzyme encoded by coactivator associated arginine methyltransferase 1 (CARM1) catalyzes the methylation of protein arginine residues, especially acts on histones and other chromatin related proteins, which is essential in regulating gene expression

  • Expression profile of CARM1 across normal tissues and cancer samples In this work, we aimed to investigate the role of human CARM1 in tumorigenesis and development

  • CARM1 protein is usually composed of a N-terminal pH like domain, a C-terminal transactivase domain, and a central catalytic domain, and its structure is conserved among most species (Fig. S1a, see Additional file 1, e.g., H. sapiens, M. mulatta, R. norvegicus, etc.)

Read more

Summary

Introduction

Belonging to the protein arginine methyltransferase (PRMT) family, the enzyme encoded by coactivator associated arginine methyltransferase 1 (CARM1) catalyzes the methylation of protein arginine residues, especially acts on histones and other chromatin related proteins, which is essential in regulating gene expression. Existing studies on exploring the mechanisms of CARM1 methylation affecting tumor progression have shown that CARM1 is a coactivator of several cancer-related transcription factors and can be involved in promoting tumor cell proliferation and metastasis by methylating cancerrelated transcription factors, including NF-κB, p53, steroid receptors and so on, and its high expression is associated with poor prognosis of tumors [15]. Methylation of the key glycolytic enzyme pyruvate kinase M2 isoform (PKM2) by CARM1 shifts the metabolic balance from oxidative phosphorylation to aerobic glycolysis, producing a large amount of ATP, so as to promote tumor cell proliferation and migration [4]. Current evidence about effects of CARM1 on various cancers has been shown in Fig. 1c and Table 4 [5, 6, 13, 16,17,18,19,20,21,22,23,24,25]

Objectives
Methods
Results
Discussion
Conclusion
Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.