Loss of ST8SIA6 is associated with enhanced MUC16-Integrin β4 signaling and aggressive phenotypes in colorectal cancer
Colorectal cancer (CRC) remains a leading cause of cancer-related mortality, underscoring the need to better understand tumor-intrinsic mechanisms underlying aggressive disease progression. Aberrant glycosylation is increasingly recognized as a key regulator of cancer cell behavior; however, the functional contribution of α2,8-sialylation to CRC remains poorly defined. Here, we investigated the role of the α2,8-sialyltransferase (ST8SIA6) in CRC progression and its impact on mucin-mediated signaling. Analysis of human CRC tissue arrays showed that ST8SIA6 expression was reduced in higher-stage tumors. ST8SIA6 silencing enhanced migration and invasion and was associated with EMT-like molecular changes. Using Siglec-7-based lectin enrichment and proteomic analysis, we identified MUC16 as a prominent Siglec-7-reactive glycoprotein associated with ST8SIA6. Loss of ST8SIA6 reduced Siglec-7 reactivity of MUC16 and increased its cell-surface localization. Increased membrane-associated MUC16 was accompanied by enhanced association with integrin β4 and increased Src and FAK phosphorylation. Blockade of integrin β4 attenuated Src/FAK activation and suppressed CRC cell migration, supporting a functional role for this axis. In vivo, ST8SIA6-deficient CRC cells exhibited increased lung tumor colonization following tail-vein injection in xenograft models, accompanied by elevated membrane MUC16 and increased MUC16-integrin β4 colocalization. Consistent with these findings, human CRC specimens from advanced stages exhibited increased MUC16 expression and integrin β4 colocalization compared with early-stage tumors. Together, these findings support a model in which loss of ST8SIA6 enhances MUC16-integrin β4 signaling and contributes to aggressive CRC phenotypes through increased MUC16 membrane localization and integrin β4-dependent signaling. These findings identify a previously unrecognized glycosylation-associated signaling axis that warrants further investigation as a biomarker and potential therapeutic target in colorectal cancer.
Authors
- Chung‐Hsien Lin (ORCID: https://orcid.org/0000-0003-0291-6373)
- Chuan‐Fa Chang (ORCID: https://orcid.org/0000-0003-2404-1248)
- Hsin‐Pao Chen
- Ngoc Uyen Nhi Nguyen (ORCID: https://orcid.org/0000-0003-0694-3176)
- Ching-Cheng Hsu
- Wei-Ling Lin (ORCID: https://orcid.org/0000-0002-2139-3099)
- Pei-Chun Shih
- Yung-Kuo Lee
Institutions
- University of South Florida (US)
- Kaohsiung Armed Forces General Hospital (TW)
- National Cheng Kung University Hospital (TW)
- National Cheng Kung University (TW)
- I-Shou University (TW)
Publication Details
- Journal
- Biochemistry and Biophysics Reports
- Published
- 2026-08-25
- DOI
- https://doi.org/10.1016/j.bbrep.2026.102757
- Primary Topic
- Glycosylation and Glycoproteins Research
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Science and Technology Council