Article(id=1276976013246596077, tenantId=1146029695717560320, journalId=1276577828834349082, issueId=1276975955985961244, articleNumber=null, orderNo=null, doi=10.19540/j.cnki.cjcmm.20250905.704, pmid=null, cstr=null, oa=null, hot=null, price=null, onlineType=0, articleFormat=0, articleType=null, articleTypeStr=null, receivedDate=1753459200000, receivedDateStr=2025-07-26, revisedDate=null, revisedDateStr=null, acceptedDate=null, acceptedDateStr=null, onlineDate=1782384406625, onlineDateStr=2026-06-25, pubDate=1767196800000, pubDateStr=2026-01-01, doiRegisterDate=null, doiRegisterDateStr=null, onlineIssueDate=1782384406625, onlineIssueDateStr=2026-06-25, onlineJustAcceptDate=null, onlineJustAcceptDateStr=null, onlineFirstDate=null, onlineFirstDateStr=null, sourceXml=null, magXml=null, createTime=1782384406625, creator=13701087609, updateTime=1782384406625, updator=13701087609, issue=Issue{id=1276975955985961244, tenantId=1146029695717560320, journalId=1276577828834349082, year='2026', volume='51', issue='1', pageStart='1', pageEnd='300', issueExtLink='null', onlineDate='null', pubDate='1767196800000', pubDateStr='2026-01-01', beforeIssueId=null, nextIssueId=null, price=null, status=1, issueComplete=1, articleOrder=1, issueType=-1, specialIssue=null, createTime=1782384392973, creator='13701087609', updateTime=1782384484405, updator='13701087609', preIssue=null, nextIssue=null, articleTotal=null, ext={EN=IssueExt(id=1276976339546673871, tenantId=1146029695717560320, journalId=1276577828834349082, issueId=1276975955985961244, language=EN, specialIssueTitle=, coverIllustrator=null, specialIssueEditor=, specialIssueAbout=), CN=IssueExt(id=1276976339546673872, tenantId=1146029695717560320, journalId=1276577828834349082, issueId=1276975955985961244, language=CN, specialIssueTitle=, coverIllustrator=null, specialIssueEditor=, specialIssueAbout=)}, issueFiles=null, downloadFileDto=null}, startPage=163, endPage=172, ext={EN=ArticleExt(id=1276976013443728367, articleId=1276976013246596077, tenantId=1146029695717560320, journalId=1276577828834349082, language=EN, title=Mechanism of sarsasapogenin targeting HIF1α protein stability in inhibiting glycolytic metabolic reprogramming in colorectal cancer, columnId=null, journalTitle=Chinese Journal of Traditional Chinese Medicine, columnName=null, runingTitle=null, highlight=null, articleAbstract=

This study investigated the effects and molecular mechanisms of sarsasapogenin (SSG) on colorectal cancer (CRC). After HRT-18 and HCT116 cells were treated with varying concentrations of SSG, the effect of SSG on CRC cell proliferation, migration, and glycolysis was assessed by cell counting kit-8 (CCK-8), real-time cellular analysis (RTCA), colony formation assay, high-content imaging analysis, and Seahorse glycolysis stress test. Changes in intracellular lactate release and adenosine triphosphate (ATP) levels under SSG treatment were measured by lactate and ATP detection kits, respectively. The effects of SSG on the transcription level and protein expression of the key glycolytic gene hypoxia-inducible factor 1α (HIF1α) were evaluated via quantitative polymerase chain reaction (qPCR) and Western blot. Direct binding between SSG and HIF1α was identified by drug affinity responsive target stability (DARTS). The UbiBrowser database, microscale thermophoresis (MST), and molecular docking simulations were employed to screen and validate the E3 ubiquitin ligase mediating HIF1α degradation. The results showed that SSG significantly inhibited CRC cell proliferation and colony formation in a dose-dependent manner. The 24-hour half-maximal inhibitory concentrations (IC₅₀) of SSG for HRT-18 and HCT116 cells were 6.275 μmol·L^-1 and 7.029 μmol·L^-1, respectively. After 24 hours of treatment with SSG at concentrations of 2.0, 4.0, and 6.0 μmol·L^-1, the HRT-18 and HCT116 clone formation rate was significantly reduced. High-content imaging results showed that SSG significantly inhibited the migration ability of CRC cells. Seahorse glycolysis stress test, along with lactate and ATP measurements, demonstrated that SSG suppressed basal glycolysis, glycolytic capacity, glycolytic reserve, lactate release, and ATP content in CRC cells. The qPCR and Western blot results showed that SSG had no significant effect on HIF1α mRNA expression, and the HIF1α protein expression was downregulated. DARTS confirmed the direct binding of SSG to HIF1α. UbiBrowser analysis identified five E3 ubiquitin ligases potentially targeting HIF1α. Molecular docking and MST results indicated that the F-box/WD repeat-containing protein 7 (FBXW7) exhibited strong binding affinity to HIF1α in the presence of SSG. In summary, SSG exerts its anti-cancer effects in CRC by targeting HIF1α to promote its FBXW7-mediated proteasomal degradation and consequently inhibiting glycolytic reprogramming.

, authors=null, authorsList=Xiang-rong ZHAN, Wen-kang PENG, Fang YANG, Ying LIU, Xu ZHANG, Ying-li CHEN, Yuan SI, Liang ZHANG, authorCompany=null, correspAuthors=Yuan SI, Liang ZHANG, authorNote=null, correspAuthorsNote=null, copyrightStatement=null, copyrightOwner=null, extLink=null, articleAbsUrl=null, sourceXml=null, magXml=null, pdfUrl=null, pdf=null, pdfFileSize=null, pdfExtLink=null, richHtmlUrl=null, mobilePdfUrl=null, reviewReport=null, pdfFirstPage=null, abstractGraph=null, abstractGraphContent=null, abstractVideo=null, citation=null, cebUrl=null, magXmlContent=null, mapNumber=null, fund=null), CN=ArticleExt(id=1276976013775078386, articleId=1276976013246596077, tenantId=1146029695717560320, journalId=1276577828834349082, language=CN, title=菝葜皂苷元靶向HIF1α蛋白稳定性抑制结直肠癌糖代谢重编程的作用机制, columnId=1276975994707775974, journalTitle=中国中药杂志, columnName=药理, runingTitle=null, highlight=null, articleAbstract=

探讨菝葜皂苷元（SSG）对结直肠癌（CRC）的作用及分子机制。用不同浓度的SSG处理HRT-18细胞和HCT116细胞后，通过CCK-8法、实时无标记细胞分析（RTCA）技术、平板克隆形成实验、高内涵成像分析技术及Seahorse糖酵解压力测试分析SSG对CRC细胞增殖、迁移及糖酵解的影响；乳酸检测试剂盒、三磷酸腺苷（ATP）检测试剂盒检测SSG作用下细胞内乳酸释放及ATP含量的变化；利用qPCR和蛋白免疫印迹法检测SSG对糖酵解关键基因缺氧诱导因子1α（HIF1α）转录水平和蛋白表达的影响；靶点稳定性药物亲和反应实验鉴定SSG与HIF1α的直接结合作用；通过UbiBrowser数据库、微量热泳动实验及分子对接筛选并验证介导HIF1α降解的E3泛素连接酶。结果发现，SSG剂量依赖性显著抑制CRC细胞的增殖、克隆形成，SSG对HRT-18和HCT116细胞的24 h半数抑制浓度是6.275、7.029 μmol·L^-1。2、4、6 μmol·L^-1 SSG处理24 h后，HRT-18和HCT116细胞克隆形成率均明显减少。高内涵成像结果显示，SSG能显著抑制CRC细胞的迁移能力。Seahorse糖酵解压力测定和乳酸、ATP水平检测结果显示，SSG对CRC细胞的基础糖酵解水平、糖酵解能力、糖酵解储备、乳酸释放和ATP含量均起到抑制作用。qPCR和蛋白免疫印迹法检测发现，SSG对HIF1α的mRNA的表达无明显影响，但能下调HIF1α的蛋白表达。靶点稳定性药物亲和反应实验发现SSG与HIF1α存在直接结合。UbiBrowser数据库分析出介导HIF1α的5种E3泛素连接酶。微量热泳动实验及分子对接结果显示，SSG促进E3泛素连接酶F框／WD40域蛋白（FBXW7）与HIF1α的结合。综上表明，SSG通过靶向促进HIF1α蛋白发生FBXW7介导的蛋白酶体降解，抑制CRC细胞糖代谢重编程来发挥抗癌作用。

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詹向荣，硕士研究生，E-mail: Zhanxr1016@163.com

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