Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P17931 (galectin-3)
 2,860 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The expression of galectin-3, a beta-galactoside-binding lectin, was studied in atherosclerotic lesions from specimens obtained from carotid endarterectomies, lower limb amputations, and thoracic aortas from autopsies of young adult trauma victims. Immunohistochemical staining with the monoclonal antibody M3/38 demonstrated the presence of galectin-3 in advanced atherosclerotic lesions from each of 13 cases of carotid endarterectomy and 16 lower limb amputations and in the thoracic aorta of 4 of 20 cases of trauma victim adults. Immunostaining did not detect galectin-3 in umbilical cord and normal thoracic aorta arteries and limb veins. Dual immunostaining with monoclonal antibodies M3/38 for galectin-3 and clone 1A4 for smooth muscle alpha-actin or HAM56 for human macrophage antigen showed that galectin-3 was localized predominantly in foam cells and macrophages and rarely (<5%) in the smooth muscle cells of atherosclerotic lesions. The incidence of galectin-3-positive cells was higher in the carotid artery atherosclerotic lesions, which are richer in foam cells, than in the lower limb atherosclerotic lesions, which are more fibrotic. Reverse transcription polymerase chain reaction showed a significantly higher ratio of galectin-3/beta-actin transcripts in 20 atherosclerotic arteries compared with that of 5 umbilical cord arteries. Western blot analysis confirmed a higher level of galectin-3 in atherosclerotic carotid and lower limb arteries compared with that of umbilical cord arteries. The increased expression of galectin-3 in atherosclerotic lesions suggests the involvement of this multifunctional protein in atherogenesis.
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PMID:Galectin-3 expression in human atherosclerotic lesions. 958 89

Oligosaccharide-plasmid DNA conjugates were synthesized simply and effectively via the diazocoupling method. Plasmids (pUC19, pTRI-beta-actin, and pEGFP-C1) were treated with an N-beta-lactoside-substituted diazonium salt to yield diazocoupling products with degree of substitutions of 2.5-3.1 mol% of overall nucleobases. The lactose-pUC19 conjugate was found to resist restriction enzymes more strongly than the nonconjugated plasmid DNA and to acquire a strong binding affinity to galactose-specific lectin RCA(120). The diazocoupling modification of pTRI-beta-actin plasmid DNA little influenced in vitro transcription with T7 RNA polymerase. When lactose-pEGFP-C1 conjugate was transfected to baby hamster kidney (BHK) cells by means of cationic lipids, transduced gene was expressed in BHK cells similarly with the nonconjugated pEGFP-C1. The modification of plasmid DNA with carbohydrate enhanced the resistance to restriction enzymes and developed a strong binding affinity to galactose-specific lectin.
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PMID:Conjugation of plasmid DNAs with lactose via diazocoupling enhances resistance to restriction enzymes and acquires binding affinity to galactose-specific lectin. 1040 69

We measured the relative expression levels of galectin-3 mRNA to beta-actin mRNA in normal thyroid tissues, thyroid tumor tissues and thyroid-derived fibroblasts. Galectin-3 mRNA was expressed ubiquitously in both benign and malignant thyroid tumors. Although a significant increase in its expression was observed in papillary carcinomas, no significant difference was observed between follicular carcinomas and adenomas. In contrast to the previous optimistic reports using immunohistochemical analysis of the galectin-3 protein expression, these results demonstrate that galectin-3 mRNA may not be a suitable target for molecular-based diagnosis of thyroid carcinomas.
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PMID:Ubiquitous expression of galectin-3 mRNA in benign and malignant thyroid tumors. 1296 25

Syncytiotrophoblast formation is affected by a number of pathological conditions and suppressed syncytiotrophoblast formation due to hypoxia may play a role in the pathogenesis of preeclampsia. However, the molecular basis of hypoxia-inhibited trophoblast syncytialization is poorly understood. To determine the effect of hypoxia on trophoblast syncytialization, a proteomic analysis was performed in the human cytotrophoblast cell line BeWo using two-dimensional electrophoresis and MALDI-TOF-TOF-MS. Hypoxia induced marked inhibition of BeWo cell fusion and differentiation. The proteomic profiling was established under hypoxia in BeWo cell syncytialization. The results showed that twenty proteins were significantly up-or down-regulated under hypoxia, compared with cells under normoxia. In response to hypoxia, three antioxidants, peroxiredoxin 1, peroxiredoxin 2 and 1-Cys peroxiredoxin, were down-regulated, two proteins involved in glycolysis pathway (malate dehydrogenase and enolase) were up-regulated. The expression of two members of the annexin family (annexin A2 and annexin A5) increased. We also found a decreased expression of 14-3-3 tau protein in hypoxia treated cells. Proteins implied in protein degradation and folding were also identified. The expression of two cytoskeleton components (keratin 1 and beta-actin) was found to be down-regulated. In addition, galectin-3 was up-regulated. These proteins have been implicated in regulating cellular oxidative stress, glycolysis, signal transduction, protein folding and degradation, cell mobility and cytoskeletal structure formation. Western blot analysis revealed that the levels of peroxiredoxin 1 and 14-3-3 tau decreased, whereas the levels of annexin A5 and annexin A2 increased in BeWo cells under hypoxia. These findings provided new insights into the molecular mechanisms in mediating cellular response to hypoxia in trophoblast syncytialization.
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PMID:Proteomic analysis of hypoxia-induced responses in the syncytialization of human placental cell line BeWo. 1709 81

Epithelial cells are characterised by distinct apical and basolateral membrane domains that are separated by tight junctions. Establishment and maintenance of this polarity depend on specific gene expression and protein targeting to their correct location. Our former studies, performed with renal epithelial MDCK cells, revealed a new function for galectin-3, a member of a conserved family of lectins. There, galectin-3 is required for intracellular sorting and correct targeting of non-raft-associated glycoproteins to the apical plasma membrane. In the present study, we found transport defects of the intestinal brush border hydrolases lactase-phlorizin hydrolase (LPH) and dipeptidylpeptidase IV (DPPIV) in galectin-3-null mutant mice. We could show that, in enterocytes of wild-type mice, both glycoproteins directly interact with galectin-3 and transit through non-raft-dependent apical transport platforms. Therefore, this genetic analysis provides definitive evidence for the involvement of galectin-3 in protein intracellular trafficking in vivo. Further investigations revealed that gal3-null enterocytes also exhibit striking cytoarchitecture defects, with the presence of numerous and regular protrusions located along basolateral membranes. Moreover, beta-actin and villin, two characteristic markers of brush borders, become abnormally distributed along these atypical basolateral membranes in gal3(-/-) mice. Taken together, our results demonstrate that, in addition to a pivotal role in apical trafficking, galectin-3 also participates in epithelial morphogenesis in mouse enterocytes.
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PMID:Loss of galectin-3 impairs membrane polarisation of mouse enterocytes in vivo. 1821 59