Article

Differential Cellular Expression of Galectin Family mRNAs in the Epithelial Cells of the Mouse Digestive Tract

Laboratory of Cytology and Histology, Hokkaido University Graduate School of Medicine, Kita 15-Nishi 7, Kita-ku, Sapporo 060-8638, Japan.
Journal of Histochemistry and Cytochemistry (Impact Factor: 1.96). 12/2005; 53(11):1323-34. DOI: 10.1369/jhc.5A6685.2005
Source: PubMed

ABSTRACT

Galectin is an animal lectin that recognizes beta-galactosides of glycoconjugates and is abundant in the gut. This study revealed the cellular expression of galectin subtypes throughout the mouse digestive tract by in situ hybridization. Signals for five subtypes (galectin-2, -3, -4/6, and -7) were detected exclusively in the epithelia. In the glandular stomach, galectin-2 and -4/6 were predominantly expressed from gastric pits to neck of gastric glands, where mucous cells were the main cellular sources. The small intestine exhibited intense, maturation-associated expressions of galectin-2, -3, and -4/6 mRNAs. Galectin-2 was intensely expressed from crypts to the base of villi, whereas transcripts of galectin-3 gathered at villous tips. Signals for galectin-4/6 were most intense at the lower half of villi. Galectin-2 was also expressed in goblet cells of the small intestine but not in those of the large intestine. In the large intestine, galectin-4/6 predominated, and the upper half of crypts simultaneously contained transcripts of galectin-3. Stratified epithelium from the lip to forestomach and anus intensely expressed galectin-7 with weak expressions of galectin-3. Because galectins in the digestive tract may be multi-functional, information on their cell/stage-specific expression contributes to a better understanding of the functions and pathological involvements of galectins.

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Available from: Junko Nio-Kobayashi
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    • " the duodenum and ileum regarding the patterns of expression of galectin - 4 and - 6 . Both proteins were expressed strongly in the epithelium and both proteins were undetectable in the lamina propria , at least under our fixation conditions . A decreasing gradient of expression of the Lgals4 mRNA has been reported along the crypt to villus axis ( Nio et al . 2005 ) . In contrast , we observed that the protein expression appeared slightly weaker in the crypts than in the villi . These results suggest that , although the gene is strongly expressed in the intestinal crypts , the protein accumulates progressively as the cells differentiate and migrate from the crypt to the villus . The galectin - 6 "
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    ABSTRACT: The galectin-4 protein is mostly expressed in the digestive tract and is associated with lipid raft stabilization, protein apical trafficking, wound healing, and inflammation. While most mammalian species, including humans, have a single Lgals4 gene, some mice have two paralogues: Lgals4 and Lgals6. So far, their significant similarities have hindered the analysis of their respective expression and function. We took advantage of two antibodies that discriminate between the galectin-4 and galectin-6 proteins to document their patterns of expression in the normal and the dextran sodium sulfate (DSS)-damaged digestive tract in the mouse. In the normal digestive tract, their pattern of expression from tongue to colon is quite similar, which suggests functional redundancy. However, the presence of galectin-4, but not galectin-6, in the lamina propria of the DSS-damaged colon, its association with luminal colonic bacteria, and differences in subcellular localization of these proteins suggest that they also have distinct roles in the normal and the damaged mouse digestive tract. Our results provide a rare example of ancestral and derived functions evolving after tandem gene duplication.
    Full-text · Article · Jan 2013 · Journal of Histochemistry and Cytochemistry
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    • "All probes were labeled with 33 P-dATP using terminal deoxynucleotidyl transferase (Invitrogen). The procedure for in situ hybridization has been described previously (Nio et al. 2005 "
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    ABSTRACT: Galectin-1 and galectin-3, β-galactoside-binding lectins, are specifically expressed in the regressing corpus luteum (CL) of mice, however, their function remains unclear. In this study, we examined the effects of prolactin (PRL) and prostaglandin F(2α) (PGF(2α)), two main regulatory molecules of mouse CL function, on galectin expression. In situ hybridization analysis clearly demonstrated an initial increase of galectin-1 in the CL newly formed (CLN) after postpartum ovulation 48 h after compulsory weaning. This was accompanied by a decline in 3β-hydroxysteroid dehydrogenase (3β-HSD) and luteinizing hormone receptor (LH-R) expression, suggesting a withdrawal of PRL stimulation. At 72 h after the weaning, the expression of both galectins in CLN was remarkably increased, being associated with an intense expression of progesterone degradation enzyme (20α-HSD). Compulsory weaning did not significantly alter both galectin expression in the remaining CL of pregnancy (CLP), while PGF(2α) strongly up-regulated both galectin expression only in the remaining CLP which lacked LH-R in postpartum mice. Administration of Bromocriptine, an antagonist for PRL secretion, to non-pregnant cyclic mice induced an accumulation of galectin-1 -but not galectin-3- in all CL of various generations, and additional PRL treatment reduced its accumulation, suggesting a direct suppressive effect of PRL on galectin-1 expression. Although the function and regulatory mechanism of galectin in the CL is not fully understood, PGF(2α) is an excellent candidate which regulates galectin expression but its effect may be abolished by LH-R-mediated signal. PRL withdrawal seems to be necessary for an initiation of luteolysis and the following PGF(2α)-induced galectin expression.
    Full-text · Article · Sep 2012 · Reproduction
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    • "In a study aimed at analyzing the expression of galectins along the mouse digestive tract, expression of galectin-3 was detected by in situ hybridization exclusively in epithelial cells. Transcripts were abundant within the large intestine, including the cecum, colon, and rectum, whereas the stomach and small intestine showed weak signals that increased slightly toward the ileum (Nio et al., 2005). However, in a more recent "
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    ABSTRACT: Galectin-3 belongs to a family of highly conserved animal lectins characterized by their ability to recognize multiple N-acetyllactosamine sequences, which can be displayed on both N- and O-glycans on cell surface glycoconjugates. Although first identified in macrophages, galectin-3 (also called "Mac-2, εBP, CBP35 or L-29") has been found to be widely distributed in several tissues and developmental stages where, depending on its extracellular or intracellular localization, it can display a broad diversity of biological functions including immunomodulation, host-pathogen interactions, embryogenesis, angiogenesis, cell migration, wound healing and apoptosis. In spite of the existence of several reviews describing the multifunctional properties of galectin-3, an integrated view of the regulated expression of this glycan-binding protein in different normal tissues is lacking. Here we attempt to summarize and integrate available information on galectin-3 distribution in normal haematopoietic and non-haematopoietic tissues, mainly in adulthood, with only a brief reference to its expression during embryonic stages. In addition, given the multiplicity of biological roles attributed to this protein, a brief description of galectin-3 functions is also included. Understanding how galectin-3 is regulated in normal tissues will contribute to a rational design of approaches aimed at modulating galectin-3 expression and subcellular localization for experimental and therapeutic purposes.
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