Evidence mapPaperPMID 41968399Full record

ArticleThe Kaohsiung journal of medical sciences2026

KAT2A Promotes the Progression of Renal Cell Carcinoma by Regulating the Succinylation of SERPINE2.

Chang-Cheng Liu, Xue-Dong Li

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In one paragraph

Article in The Kaohsiung journal of medical sciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

2 authors.

Chang-Cheng LiuThe Second Affiliated Hospital of Harbin Medical University, Harbin, Heilongjiang, China.
Xue-Dong LiThe Second Affiliated Hospital of Harbin Medical University, Harbin, Heilongjiang, China.ORCID https://orcid.org/0009-0009-2795-7121

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Epithelial-mesenchymal transition (EMT) and angiogenesis are critical drivers of renal cell carcinoma (RCC) progression, yet their upstream regulatory mechanisms remain incompletely understood. This study aimed to investigate the role of KAT2A in RCC and elucidate the underlying molecular mechanism by which it promotes tumor progression. To investigate KAT2A and SERPINE2 in RCC, we assessed their expression and downstream effects using real-time quantitative PCR and western blot. EMT markers (E-cadherin, N-cadherin, Vimentin) and SERPINE2 succinylation were also measured. Functional assays (CCK-8, colony formation, transwell, tube formation) evaluated cell viability, proliferation, migration, and angiogenesis. Co-localization (immunofluorescence) and interaction (co-immunoprecipitation) of KAT2A and SERPINE2 were confirmed. Finally, Ki-67, KAT2A, and SERPINE2 expression in RCC tumors were examined via immunohistochemistry. We identified that KAT2A expression was significantly elevated in RCC tissues and correlated with poor patient prognosis. Functionally, KAT2A depletion markedly inhibited RCC cell proliferation, migration, EMT, and HUVECs angiogenesis in vitro, as well as suppressed tumor growth in vivo. Mechanistically, KAT2A directly interacted with SERPINE2 and promoted its succinylation at lysine 158 (K158). This post-translational modification enhanced SERPINE2 protein stability, and SERPINE2 overexpression effectively reversed the tumor-suppressive effects induced by KAT2A silencing. Our findings reveal that the KAT2A/SERPINE2 axis is a key regulator of RCC pathogenesis, identifying KAT2A-mediated SERPINE2 succinylation as a novel mechanism and potential therapeutic target for RCC treatment.

Indexed as

KAT2Arenal cell carcinomaSERPINE2Succinylation

Identifiers

PMID41968399
PMCPMC13399823

What Socratic holds

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.