Distinct glycosyltransferase expression governs organ-specific survival in pancreatic cancer metastasis

Pancreatic ductal adenocarcinoma (PDAC) is among the most lethal cancers, with over 83% of patients presenting metastases to vital organs such as the liver, lungs, and peritoneum. Although glycosylation has been established as a critical factor in PDAC development, little is known about the molecular underpinnings of organ-specific metastasis. In this study, we investigated the role of glycosyltransferases (GTs) in mediating PDAC metastatic organotropism. Through an unbiased transcriptomic screen, we identified distinct GT expression patterns in liver- and lung-tropic PDAC cells. Notably, GCNT3 and B3GNT3 were selectively upregulated in liver and lung-tropic cells, respectively. These mutually exclusive expression patterns were validated in human metastatic PDAC specimens, where GCNT3 was enriched in liver metastatic lesions and B3GNT3 in lung metastases. Proteomic profiling revealed that differential expression of these GTs is associated with epithelial-mesenchymal transition and glycoproteome remodeling in metastatic cells. Functional studies using in vitro assays, ex vivo organotypic cultures, and in vivo metastasis models demonstrated that loss of GCNT3 or B3GNT3 impairs the proliferation and survival of PDAC cells in their respective metastatic organ environments. Together, these findings uncover a glycosylation-based mechanism that facilitates organ-specific survival of metastatic PDAC cells and highlight glycosyltransferases as potential therapeutic targets for disrupting metastatic adaptation.

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Publication Details

Journal
Oncogene
Published
2026-07-30
DOI
https://doi.org/10.1038/s41388-026-03896-5
Primary Topic
Glycosylation and Glycoproteins Research
Type
article
Field-Weighted Citation Impact
0.00

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article

Distinct glycosyltransferase expression governs organ-specific survival in pancreatic cancer metastasis

Jesse L. Cox, Moorthy P. Ponnusamy, Sanchita Rauth, Michael Anthony Hollingsworth et al.
Oncogene
Glycosylation and Glycoproteins Research
article

Distinct glycosyltransferase expression governs organ-specific survival in pancreatic cancer metastasis

Jesse L. Cox, Moorthy P. Ponnusamy, Sanchita Rauth, Michael Anthony Hollingsworth, Zahraa Wajih Alsafwani, Venkatesh Varadharaj, Nivedeta Krishna Kumar, Pratima Raut, Jean L. Grem, Geoffrey A. Talmon, Palanisamy Nallasamy, Dominick J. DiMaio, Saravanakumar Marimuthu, Frank Leon, Surinder K. Batra, Paul M. Grandgenett, Neelanjana Gayen, Annant Bir Kaur, Poompozhil Mathivanan, Kirtana Arikath, Wyatt Petersen, Madhu Bommideni, Kavita Mallya
article en

Abstract

Pancreatic ductal adenocarcinoma (PDAC) is among the most lethal cancers, with over 83% of patients presenting metastases to vital organs such as the liver, lungs, and peritoneum. Although glycosylation has been established as a critical factor in PDAC development, little is known about the molecular underpinnings of organ-specific metastasis. In this study, we investigated the role of glycosyltransferases (GTs) in mediating PDAC metastatic organotropism. Through an unbiased transcriptomic screen, we identified distinct GT expression patterns in liver- and lung-tropic PDAC cells. Notably, GCNT3 and B3GNT3 were selectively upregulated in liver and lung-tropic cells, respectively. These mutually exclusive expression patterns were validated in human metastatic PDAC specimens, where GCNT3 was enriched in liver metastatic lesions and B3GNT3 in lung metastases. Proteomic profiling revealed that differential expression of these GTs is associated with epithelial-mesenchymal transition and glycoproteome remodeling in metastatic cells. Functional studies using in vitro assays, ex vivo organotypic cultures, and in vivo metastasis models demonstrated that loss of GCNT3 or B3GNT3 impairs the proliferation and survival of PDAC cells in their respective metastatic organ environments. Together, these findings uncover a glycosylation-based mechanism that facilitates organ-specific survival of metastatic PDAC cells and highlight glycosyltransferases as potential therapeutic targets for disrupting metastatic adaptation.

Oncogene
Nebraska Medical Center (US), University of Nebraska Medical Center (US)
National Institutes of Health, National Cancer Institute
Good health and well-being
Openalex Percentile: Top 15%
Glycosylation and Glycoproteins Research
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