» Articles » PMID: 37052731

Sialylation of Cell Surface Glycoconjugates Modulates Cytosolic Galectin-mediated Responses Upon Organelle Damage : Minireview

Overview
Journal Glycoconj J
Publisher Springer
Date 2023 Apr 13
PMID 37052731
Authors
Affiliations
Soon will be listed here.
Abstract

Sialylation is an important terminal modification of glycoconjugates that mediate diverse functions in physiology and disease. In this review we focus on how altered cell surface sialylation status is sensed by cytosolic galectins when the integrity of intracellular vesicles or organelles is compromised to expose luminal glycans to the cytosolic milieu, and how this impacts galectin-mediated cellular responses. In addition, we discuss the roles of mammalian sialidases on the cell surface, in the organelle lumen and cytosol, and raise the possibility that intracellular glycan processing may be critical in controlling various galectin-mediated responses when cells encounter stress.

References
1.
Liu F, Rabinovich G . Galectins as modulators of tumour progression. Nat Rev Cancer. 2005; 5(1):29-41. DOI: 10.1038/nrc1527. View

2.
Hirabayashi J, Hashidate T, Arata Y, Nishi N, Nakamura T, Hirashima M . Oligosaccharide specificity of galectins: a search by frontal affinity chromatography. Biochim Biophys Acta. 2002; 1572(2-3):232-54. DOI: 10.1016/s0304-4165(02)00311-2. View

3.
Hughes R . Secretion of the galectin family of mammalian carbohydrate-binding proteins. Biochim Biophys Acta. 1999; 1473(1):172-85. DOI: 10.1016/s0304-4165(99)00177-4. View

4.
Nabi I, Shankar J, Dennis J . The galectin lattice at a glance. J Cell Sci. 2015; 128(13):2213-9. DOI: 10.1242/jcs.151159. View

5.
Hong M, Weng I, Li F, Lin W, Liu F . Intracellular galectins sense cytosolically exposed glycans as danger and mediate cellular responses. J Biomed Sci. 2021; 28(1):16. PMC: 7931364. DOI: 10.1186/s12929-021-00713-x. View