Immunohistochemical Localization of Six Galectin Subtypes in the Mouse Digestive Tract
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TLDR
The subtype-specific localization of galectin suggests its important roles in host-pathogen interaction and epithelial homeostasis such as membrane polarization and trafficking in the gut.Abstract:
Galectin, an animal lectin that recognizes beta-galactoside of glycoconjugates, is abundant in the gut. This IHC study showed the subtype-specific localization of galectin in the mouse digestive tract. Mucosal epithelium showed region/cell-specific localization of each galectin subtype. Gastric mucous cells exhibited intense immunoreactions for galectin-2 and galectin-4/6 with a limited localization of galectin-3 at the surface of the gastric mucosa. Electron microscopically, galectin-3 immunoreactivity coated indigenous bacteria on the gastric surface mucous cells. Epithelial cells in the small intestine showed characteristic localizations of galectin-2 and galectin-4/6 in the cytoplasm of goblet cells and the baso-lateral membrane of enterocytes in association with maturation, respectively. Galectin-3 expressed only at the villus tips was concentrated at the myosin-rich terminal web of fully matured enterocytes. Epithelial cells of the large intestine contained intense immunoreactions for galectin-3 and galectin-4/6 but not for galectin-2. The stratified squamous epithelium of the forestomach was immunoreactive for galectin-3 and galectin-7, but the basal layer lacked galectin-3 immunoreactivity. Outside the epithelium, only galectin-1 was localized in the connective tissue, smooth muscles, and neuronal cell bodies. The subtype-specific localization of galectin suggests its important roles in host-pathogen interaction and epithelial homeostasis such as membrane polarization and trafficking in the gut.read more
Citations
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Glycosylation, galectins and cellular signaling
TL;DR: Both tissue-specific expression of the enzymes and the metabolic supply of sugar-nucleotides to the ER and Golgi regulate glycan distribution while protein sequences specify NXS/T site multiplicity, providing metabolic and genetic contributions to galectin-glycoprotein interactions.
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Galectins in innate immunity: dual functions of host soluble β‐galactoside‐binding lectins as damage‐associated molecular patterns (DAMPs) and as receptors for pathogen‐associated molecular patterns (PAMPs)
TL;DR: The glycocalyx is a glycan layer found on the surfaces of host cells as well as microorganisms and enveloped virus, which contains various structurally different glycans, which provide cell‐ or microorganism‐specific ‘glycoinformation’ and is decoded by host glycan‐binding proteins, lectins.
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Immunological Effects of Human Milk Oligosaccharides.
TL;DR: The role of HMOs in altering immune responses through binding to immune-related receptors and thus modulate neonatal immunity in the infant gut, and possibly also sites throughout the body, is focused on.
Journal ArticleDOI
Galectin-9 induced by dietary synbiotics is involved in suppression of allergic symptoms in mice and humans
S. de Kivit,Eirikur Saeland,Aletta D. Kraneveld,H. J. G. van de Kant,Bastiaan Schouten,B.C.A.M. van Esch,Jan Knol,Aline B. Sprikkelman,L. B. van der Aa,Léon M.J. Knippels,Johan Garssen,Y. (Yvette) van Kooyk,Linette E M Willemsen +12 more
TL;DR: The involvement of galectin‐9 as a mechanism by which scGOS/lcFOS in combination with Bifidobacterium breve M‐16V protects against acute allergic symptoms was investigated.
Journal ArticleDOI
Host-soluble galectin-1 promotes HIV-1 replication through a direct interaction with glycans of viral gp120 and host CD4.
Christian St-Pierre,Hiroshi Manya,Michel Ouellet,Gary F. Clark,Tamao Endo,Michel J. Tremblay,Sachiko Sato +6 more
TL;DR: It is shown that galectin-1 directly binds to HIV-1 in a β-galactoside-dependent fashion through recognition of clusters of N-linked glycans on the viral envelope gp120, and the data suggest that galECTin- 1 binds preferentially to CD4, the host receptor for gp120.
References
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Galectins: a family of animal beta-galactoside-binding lectins.
Samuel H. Barondes,Vincent Castronovo,Douglas N.W. Cooper,Richard D. Cummings,Kurt Drickamer,Ten Felzi,Michael A. Gitt,Jun Hirabayashi,Colin Hughes,Ken-ichi Kasai,Hakon Leffler,Fu-Tong Liu,Reuben Lotan,Arthur M. Mercurio,Michel Monsigny,Shiv Pillai,Françoise Poirer,Avraham Raz,Peter W.J. Rigby,James M. Rini,John L. Wang +20 more
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Introduction to galectins
TL;DR: A brief introduction to the galectins as a protein family with some comments on nomenclature is given.
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Secretion of the galectin family of mammalian carbohydrate-binding proteins
TL;DR: Questions remain largely unanswered but recent studies are beginning to give glimpses into some novel aspects of the secretion of galectins, including their role as modulators of cell adhesion and signalling.
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Galectins and their ligands: amplifiers, silencers or tuners of the inflammatory response?
Gabriel A. Rabinovich,Linda G. Baum,Nicola Tinari,Roberto Paganelli,Clara Natoli,Fu-Tong Liu,Stefano Iacobelli +6 more
TL;DR: The current wealth of new information promises a future scenario in which individual members of the galectin family or their ligands will be used as powerful anti-inflammatory mediators and selective modulators of the immune response.
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The family of metazoan metal-independent β-galactoside-binding lectins: structure, function and molecular evolution
Jun Hirabayashi,Ken-ichi Kasai +1 more
TL;DR: It appears that beta-galactoside-binding lectins and some non-lectin proteins form a superfamily whose members are widely distributed from vertebrates to invertebrates and a consideration of molecular evolution suggests that lectins belonging to this family probably existed in the Precambrian era.