4.6 Article

Immune-Proteome Profiling in Classical Hodgkin Lymphoma Tumor Diagnostic Tissue

期刊

CANCERS
卷 14, 期 1, 页码 -

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MDPI
DOI: 10.3390/cancers14010009

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Hodgkin lymphoma; proteomics; proximity assays; tumor microenvironment; PD-L1; LAG3 CCL17; biomarkers; Immunology

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资金

  1. Swedish Cancer Society (Cancerfonden) [201147PjF]
  2. Swedish Research Council [2020-02258]
  3. Swedish Research Council [2020-02258] Funding Source: Swedish Research Council

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The proximity extension assay (PEA) method was used to identify immune-related proteins that distinguish diagnostic classic Hodgkin Lymphoma (cHL) tissues from control tissues. The study found several proteins that are elevated in both cHL tissues and cHL plasma compared to control samples, and these proteins are also significantly correlated to PD-L1 expression in cHL tissue.
Simple Summary The proximity extension assay (PEA) method enables the detection of proteins in tissue lysates and plasma with high specificity and sensitivity. Knowledge regarding the immune proteome profile in classical Hodgkin Lymphoma (cHL) tumor microenvironment (TME) is critical in an era of emerging immunotherapies and precision medicine. This study identifies several important immune markers that distinguish cHL tissue from reactive lymph nodes and introduces new potential therapeutic targets in an era of personalized medicine. In classical Hodgkin Lymphoma (cHL), immunoediting via protein signaling is key to evading tumor surveillance. We aimed to identify immune-related proteins that distinguish diagnostic cHL tissues (=diagnostic tumor lysates, n = 27) from control tissues (reactive lymph node lysates, n = 30). Further, we correlated our findings with the proteome plasma profile between cHL patients (n = 26) and healthy controls (n = 27). We used the proximity extension assay (PEA) with the OlinkTM multiplex Immuno-Oncology panel, consisting of 92 proteins. Univariate, multivariate-adjusted analysis and Benjamini-Hochberg's false discovery testing (=Padj) were performed to detect significant discrepancies. Proteins distinguishing cHL cases from controls were more numerous in plasma (30 proteins) than tissue (17 proteins), all Padj < 0.05. Eight of the identified proteins in cHL tissue (PD-L1, IL-6, CCL17, CCL3, IL-13, MMP12, TNFRS4, and LAG3) were elevated in both cHL tissues and cHL plasma compared with control samples. Six proteins distinguishing cHL tissues from controls tissues were significantly correlated to PD-L1 expression in cHL tissue (IL-6, MCP-2, CCL3, CCL4, GZMB, and IFN-gamma, all p <= 0.05). In conclusion, this study introduces a distinguishing proteomic profile in cHL tissue and potential immune-related markers of pathophysiological relevance.

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