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.

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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

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article

Loss of ST8SIA6 is associated with enhanced MUC16-Integrin β4 signaling and aggressive phenotypes in colorectal cancer

Chung‐Hsien Lin, Chuan‐Fa Chang, Hsin‐Pao Chen, Ngoc Uyen Nhi Nguyen et al.
Biochemistry and Biophysics Reports
Glycosylation and Glycoproteins Research
article

Loss of ST8SIA6 is associated with enhanced MUC16-Integrin β4 signaling and aggressive phenotypes in colorectal cancer

Chung‐Hsien Lin, Chuan‐Fa Chang, Hsin‐Pao Chen, Ngoc Uyen Nhi Nguyen, Ching-Cheng Hsu, Wei-Ling Lin, Pei-Chun Shih, Yung-Kuo Lee
article en

Abstract

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.

Biochemistry and Biophysics ReportsVol. 47
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)
National Science and Technology Council
Good health and well-being
Openalex Percentile: Top 17%
Glycosylation and Glycoproteins Research
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