OAS3 is a Co-Immune Biomarker Associated With Tumour Microenvironment, Disease Staging, Prognosis, and Treatment Response in Multiple Cancer Types

Li, Xinyu; Hou, Lei; Zhang, Luyu; Zhang, Liming; Wang, Biao; Wang, Zhenfeng; Wen, Mingzhe; Yang, Xitao

doi:10.3389/fcell.2022.815480

Cited by 6 publications

(4 citation statements)

References 44 publications

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“…Cancer-associated pathways influenced by SIS ECM in CT26 spheroids were driven by an upregulation in 2’-5’ oligoadenylate synthetases 2 and 3 ( Oas2 , Oas3 ) (Supplementary Fig. 6d) also associate with immune regulation, which are enzymes activated by IFN signaling cascades and has been shown to establish an immunosuppressive microenvironment 46 . IFN-related genes (Prkd1 and Irf7) were also enriched in the presence of SIS ECM.…”

Section: Resultsmentioning

confidence: 99%

Engineering Tumor Stroma Morphogenesis Using Dynamic Cell-Matrix Spheroid Assembly

Buckenmeyer,

Brooks,

Taylor

et al. 2024

Preprint

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The tumor microenvironment consists of resident tumor cells organized within a compositionally diverse, three-dimensional (3D) extracellular matrix (ECM) network that cannot be replicated in vitro using bottom-up synthesis. We report a new self-assembly system to engineer ECM-rich 3D MatriSpheres wherein tumor cells actively organize and concentrate microgram quantities of decellularized ECM dispersions which modulate cell phenotype. 3D colorectal cancer (CRC) MatriSpheres were created using decellularized small intestine submucosa (SIS) as an orthotopic ECM source that had greater proteomic homology to CRC tumor ECM than traditional ECM formulations such as Matrigel. SIS ECM was rapidly concentrated from its environment and assembled into ECM-rich 3D stroma-like regions by mouse and human CRC cell lines within 4-5 days via a mechanism that was rheologically distinct from bulk hydrogel formation. Both ECM organization and transcriptional regulation by 3D ECM cues affected programs of malignancy, lipid metabolism, and immunoregulation that corresponded with an in vivo MC38 tumor cell subpopulation identified via single cell RNA sequencing. This 3D modeling approach stimulates tumor specific tissue morphogenesis that incorporates the complexities of both cancer cell and ECM compartments in a scalable, spontaneous assembly process that may further facilitate precision medicine.

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Section: Resultsmentioning

confidence: 99%

Engineering Tumor Stroma Morphogenesis Using Dynamic Cell-Matrix Spheroid Assembly

Buckenmeyer,

Brooks,

Taylor

et al. 2024

Preprint

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“…3B ). Specifically, the interaction diagram illustrated that a number of serotonylated proteins were closely linked to the regulation of tumor necrosis factor (TNF), cancer metabolism, and cancer development/treatment, which included the mammalian target of rapamycin (mTOR), 23 epidermal growth factor receptor (EGFR), 24 2’-5’-oligoadenylate synthetase (OAS3), 25 rho-associated coiled-coil-containing protein kinase 1 (ROCK1), 26 p21-activated kinase 4 (PAK4), 27 etc . The serotonylation on these proteins may exhibit significant regulatory functions for their activities.…”

Section: Resultsmentioning

confidence: 99%

pH-Controlled chemoselective rapid azo-coupling reaction (CRACR) enables global profiling of serotonylation proteome in cancer cells

Zhang,

Wu,

Gao

et al. 2024

Preprint

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Serotonylation has been identified as a novel protein post-translational modification (PTM) for decades, where an isopeptide bond is formed between the glutamine residue and serotonin through transamination. Transglutaminase 2 (also known as TGM2 or TGase2) was proven to act as the main writer enzyme for this PTM and a number of key regulatory proteins (including small GTPases, fibronectin, fibrinogen, serotonin transporter, and histone H3) have been characterized as the substrates of serotonylation. However, due to the lack of pan-specific antibody for serotonylated glutamine, the precise enrichment and proteomic profiling of serotonylation still remain challenging. In our previous research, we developed an aryldiazonium probe to label protein serotonylation in a bioorthogonal manner. This chemical biology tool can be utilized alternatively for the antibody-free enrichment of serotonylated proteins, which depends on a pH-controlled chemoselective rapid azo-coupling reaction (CRACR). Here, we report the application of a photoactive aryldiazonium-biotin probe for the global profiling of serotonylation proteome in cancer cells. Thus, over 500 serotonylated proteins were identified from HCT 116 cells. Importantly, a number of modification sites of these serotonylated proteins were determine, attributed to the successful application of our chemical proteomic approach. Overall, these findings provided new insights into the significant association between cellular protein serotonylation and cancer development, further suggesting that to target TGM2-mediated monoaminylation may serve as a promising strategy for cancer therapeutics.

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“…And the RBM10 expression is closely related to TMB, MSI, the number of new antigens, and MMR genes in a variety of cancers. Immune checkpoint inhibitors are considered to be the most effective anti-tumor immunotherapy [44]. Here, the RBM10 expression is significantly associated with most ICP genes, especially in HNSC, KICH, LIHC, COAD, TGCT, THCA, THYM, and UCEC.…”

Section: Discussionmentioning

confidence: 99%

RBM10 Is a Biomarker Associated with Pan-Cancer Prognosis and Immune Infiltration: System Analysis Combined with In Vitro and Vivo Experiments

Cao

Pang

Shi

2022

Oxidative Medicine and Cellular Longevity

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RNA binding motif protein 10 (RBM10) is a splicing factor that has been reported to be involved in the occurrence and progression of multiple malignancies. However, the RBM10 involvement in pan-cancer immunotherapy is not clear. In here, we provide the first comprehensive assessment of the prognostic value and immunological function of RBM10 in human pan-cancer utilizing multiple public databases. Data reveal the aberrant RBM10 expression in most tumors, and its expression is positively or negatively linked with the clinical prognosis of various cancers, depending on the different types and subtypes of cancers. In most tumors, RBM10 mutations are frequently occurred, which is closely related to tumor progression. Moreover, our results also show that RBM10 is considerably linked with most of the immune checkpoint genes, tumor immune cell infiltration, tumor mutation burden, and microsatellite instability. Additionally, RBM10 is significantly positively correlated with the sensitivity of trametinib, 17-AAG, PD-0325901, RDEA119, cetuximab, and afatinib, indicating potential antagonism between RBM10 inhibitors and these antitumor drugs, and more likely to develop drug resistance. We also verify that downregulation of RBM10 enhances the malignant phenotype of lung adenocarcinoma cells using in vitro cell experiments, and in vivo animal experiments show that the overexpression of RBM10 reduces the growth of tumors. Furthermore, upregulating RBM10 greatly reduces the PD-L1 protein levels, while silencing RBM10 considerably enhances PD-L1 protein levels. Moreover, the overexpression of RBM10 decreases the protein stability of PD-L1. To sum up, our pan-cancer analysis indicates that RBM10 is a promising biomarker for prognosis and immunotherapy, which provides a new insight for cancer immunotherapy.

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OAS3 is a Co-Immune Biomarker Associated With Tumour Microenvironment, Disease Staging, Prognosis, and Treatment Response in Multiple Cancer Types

Cited by 6 publications

References 44 publications

Engineering Tumor Stroma Morphogenesis Using Dynamic Cell-Matrix Spheroid Assembly

Engineering Tumor Stroma Morphogenesis Using Dynamic Cell-Matrix Spheroid Assembly

pH-Controlled chemoselective rapid azo-coupling reaction (CRACR) enables global profiling of serotonylation proteome in cancer cells

RBM10 Is a Biomarker Associated with Pan-Cancer Prognosis and Immune Infiltration: System Analysis Combined with In Vitro and Vivo Experiments

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