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Across multiple cancer cell lines, AD, CD, and m62A suppressed ADAM10 expression and showed strong molecular docking binding energies (\u003C-7 kcal/mol). 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\nEDITED BY  \nJanendra K. Batra,  \nNational Institute of Pathology (ICMR), India  \nREVIEWED BY  \nMervat G. Hassan, Benha University, Egypt Chang Chen,  \nChina Academy of Chinese Medical Sciences, China  \n*CORRESPONDENCE Junjiang Fu  \n [fujunjiang@swmu.edu.cn](fujunjiang@swmu.edu.cn);  \n [fujunjiang@hotmail.com](fujunjiang@hotmail.com)[ ](fujunjiang@hotmail.com)You-hua Xu  \n[yhxu@must.edu. mo](yhxu@must.edu. mo)  \n†These authors have contributed equally to this work  \nRECEIVED 17 May 2024  \nACCEPTED 29 July 2024  \nPUBLISHED 15 August 2024  \nCITATION  \nZhang W, Fu J, Du J, Liu X, Cheng J, Wei C, Xu Y and Fu J (2024) A disintegrin and metalloproteinase domain 10 expression inhibition by the small molecules adenosine, cordycepin and N6, N6-dimethyladenosine and immune regulation in malignant cancers. Front. Immunol. 15:1434027 .  \ndoi: 10.3389/fimmu.2024.1434027  \nCOPYRIGHT  \n© 2024 Zhang, Fu, Du, Liu, Cheng, Wei, Xu and Fu. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY) . The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.  \nA disintegrin and metalloproteinase domain 10 expression inhibition by the small molecules adenosine, cordycepin and N6, N6-dimethyladenosine and immune regulation in malignant cancers  \nWenqian Zhang 1,2,3†, Jiewen Fu 1†, Jiaman Du 1†, Xiaoyan Liu 1, Jingliang Cheng 1, Chunli Wei 1, Youhua Xu 3* and Junjiang Fu 1,3*  \n1 Key Laboratory of Epigenetics and Oncology, The Research Center for Preclinical Medicine, Southwest Medical University, Luzhou, Sichuan, China, 2 Department of Rehabilitation Medicine, The Affiliated Hospital of Southwest Medical University, Luzhou, Sichuan, China, 3State Key Laboratory of Quality Research in Chinese Medicine, Faculty of Chinese Medicine, Macau University of Science and Technology, Taipa, Macao SAR, China  \nA disintegrin and metalloproteinase domain 10 (ADAM10), a member of the ADAM family, is a cellular surface protein with potential adhesion and protease/ convertase functions. The expression regulations in cancers by natural products [adenosine (AD) and its analogs, cordy ce pin (CD), and N6, N6-dimethyladenosine (m62A)], and immune regulation are unclear. As results, AD, CD, and m62A inhibited ADAM10 expression in various cancer cell lines, indicating their roles in anti-cancer agents. Further molecular docking with ADAM10 protein found the binding energies of all docking groups were \u003C-7 kcal/mol for all small-molecules (AD, CD and m62A), suggesting very good binding activities. In addition, analysis of the immunomodulatory roles in cancer showed that ADAM10 was negatively correlated with immunomodulatory genes such as CCL27, CCL14, CCL25, CXCR5, HLA-B, HLA-DOB1, LAG3, TNFRSF18, and TNFRSF4 in bladder urothelial carcinoma, thymoma, breast invasive carcinoma, TGCT, kidney renal papillary cell carcinoma, SKCM and thyroid carcinoma, indicating the immune-promoting roles for ADAM10 . LAG3 mRNA levels were reduced by both AD and CD in vivo. ADAM10 is also negatively associated with  \nAbbreviations: ADAM10, a disintegrin and metalloproteinase domain 10; LAG3, lymphocyte activating 3; SARS-CoV-2, severe acute respiratory syndrome coronavirus 2; COVID-19, Coronavirus Disease 2019; CD, cordycepin; AD, adenosine; m62A, N6, N6-dimethyladenosine; CHX, cycloheximide; RCSB, Research Collaboratory for Structural Bioinformatics; PBD, Protein Data Bank; TCGA, The Cancer Genome Atlas.  \nFrontiers in Immunology 01 [frontiersin.org](frontiersin.org)  \ntumor immunosuppression and interrelated with the immune infiltration of tumors. Overall, the present study d","cbCaijUNzKrVcEmj","https://ap.wps.com/l/cbCaijUNzKrVcEmj","pdf",8253887,14,"English","# Introduction\n# Abstract\n## Results and findings\n## Molecular docking\n## Immunomodulatory correlations","[{\"question\":\"Which small molecules were tested for their effect on ADAM10 expression?\",\"answer\":\"The study tested adenosine (AD), cordycepin (CD), and N6, N6-dimethyladenosine (m62A) for inhibiting ADAM10 expression.\"},{\"question\":\"What did molecular docking indicate about AD, CD, and m62A binding to ADAM10?\",\"answer\":\"Molecular docking showed very good binding activities, with binding energies of all docking groups reported as less than -7 kcal/mol.\"},{\"question\":\"How was ADAM10 linked to immune-related gene patterns in cancers?\",\"answer\":\"Analysis across cancer types found ADAM10 negatively correlated with several immunomodulatory genes, consistent with immune-promoting roles for ADAM10.\"}]","A disintegrin and metalloproteinase domain 10 expression inhibition by the small molecules adenosine, cordycepin and N6, N6-dimethyladenosine and immune regulation in malignant cancers - read online free | PDF",1790003679,35]