Authors
Lin, X., Nicolazzi, G. A., Liu, X., Nwokolo, C., Zick, Y., Saenz, J., Brown, J. W.
Abstract
Galectins are a family of proteins that bind galactose containing glycans. One member, galectin-8 preferentially binds galactose that contains a terminal sulfate. Aberrant expression and secretion of sulfated glycosylation epitopes such as 3'-Sulfo-LeA/C is a feature of high-risk human foregut metaplasias. In addition, recent work has demonstrated that 3'-Sulfo-LeC is a marker of mature murine zymogenic chief cells of the stomach, and that 3'-Sulfo-LeC epitope is secreted via cathartocytosis during cell transition to a metaplastic state. Based on those findings, we used Lgals8-/- mice to determine whether galectin-8 might play a role in chief cell homeostasis. We observed delayed gastric differentiation in the Lgals8-/- mice, but discovered that this phenotype was due to an unappreciated deletion of Mmrn1 and Snca in the Lgals8-/- line. We show that multimerin-1 tempers WNT stimulation of the gastric corpus at early age as evidenced by Beta-Catenin staining and proliferation throughout the gland. Because multimerin-1 is synthesized and secreted from endothelial cells and not from the epithelial compartment, these data uncover a role for mesodermal cells in epithelial developmental and maturation of the mouse stomach. As prior studies have suggested overlapping functions of galectin-8 and multimerin-1, future studies using pure knockouts are necessary to refine these phenotypes.
Preprint server:
bioRxiv
The authors list and abstract were imported from bioRxiv on 06 Nov 2025.
Advertisement
Stats
- Recommendations n/a n/a positive of 0 vote(s)
- Views 39
- Comments 0