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)

Galactose-specific lectin from Viscum album (VAA) was found to induce aggregation of human platelets in a dose- and sugar-dependent manner. Small nonaggregating concentrations of VAA primed the response of platelets to known aggregants (ADP, arachidonic acid, thrombin, ristocetin, and A23187). VAA-induced platelet aggregation was completely reversible by addition of the sugar inhibitor lactose and the platelets from disrupted aggregates maintained the response to other aggregants. The lectin-induced aggregation of washed platelets was more resistant to metabolic inhibitors than thrombin- or arachidonic acid-dependent cell interaction. In contrast to the related galactose-specific lectin from Ricinus communis and the soy bean agglutinin, the lectin did not aggregate liposomes prepared from total platelet lipids, indicating different affinities of aggregation-mediating lectins to platelet glycolipids.
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PMID:Galactose-specific lectin from Viscum album as a mediator of aggregation and priming of human platelets. 776 7

In vitro growth assays with a purified D-galactose-specific lectin Kb-CWL I extracted from Kluyveromyces bulgaricus showed marked antifungal effects on 9 of 12 test strains belonging to the genera Kluyveromyces, Saccharomyces, Pichia, Candida, Rhodotorula and Schizosaccharomyces. The inhibition of growth was proportional to the lectin concentration (0.04 and 0.08 mg ml-1) in the culture medium. Under the test conditions, K. bulgaricus, K. lactis and S. bayanus were consistently agglutinated without growth inhibition. D-Galactose, the inhibitory sugar of the cell aggregation activity, did not abolish the antifungal effects of the lectin Kb-CWL I on other yeast strains tested. In C. albicans and C. tropicalis, the lectin influenced the dimorphism of these strains and stimulated germ tube formation.
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PMID:Alternate interactions of the D-galactose-specific yeast lectin Kb-CWL I with sensitive yeast strains. 846 95

Current methods of research into thyroid nodular disease (TND) based on the polymerase chain reaction (PCR) and reverse-transcription (RT) permit the detection of some markers, even in poorly cellular biological material. The findings from fine-needle aspiration biopsy (FNAB), the most commonly used procedure in TND, do not always correlate with the postoperative histopathological diagnosis, sometimes giving a false negative result. The aim of this present study was to improve the classical cytological evaluation of the material obtained with ultrasound-guided biopsy with a RT-PCR based technique in order to detect carcinoma even in a minimally invasive form. Aspirate from the 30 patients included in the study was smeared for conventional cytology (H+E and MGG staining) and the leftover material in the needle was frozen for subsequent PCR analysis. Fine-needle aspiration specimens were evaluated for the presence of galectin-3 (GAL-3), the most promising molecular marker of malignancy. As a positive control for cells of follicular origin, thyroglobulin (Tg) gene expression was performed. RT-PCR was performed on extracted RNA and with specific primers for the screened genes, based on a one-step reaction with a Biometra PCR machine. Tg expression was observed in 23 aspirates, among which 10 were positive for the expression of GAL-3 [3 cases of PTC, 1 an oxyphilic variant of FTC, 1 an oxyphilic variant of follicular adenoma (FA), 1 a foetal variant of FA, 2 of Hashimoto thyroiditis (HT) and 2 of HT with coexisting FA]. Our results are the first evidence that GAL-3 expression, previously documented in thyroid carcinoma of follicular origin, is also present in Hashimoto thyroiditis. This study reveals some limitations in nodule or multiple nodules of benign character. If the diagnosis of HT is excluded, then the usefulness of the method in the diagnosis of malignancy may still be very high.
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PMID:Galectin-3 is not an universal marker of malignancy in thyroid nodular disease in children and adolescents. 1257 40

The X-ray structure of mistletoe lectin I (MLI), a type-II ribosome-inactivating protein (RIP), cocrystallized with galactose is described. The model was refined at 3.0 A resolution to an R-factor of 19.9% using 21 899 reflections, with Rfree 24.0%. MLI forms a homodimer (A-B)2 in the crystal, as it does in solution at high concentration. The dimer is formed through contacts between the N-terminal domains of two B-chains involving weak polar and non-polar interactions. Consequently, the overall arrangement of sugar-binding sites in MLI differs from those in monomeric type-II RIPs: two N-terminal sugar-binding sites are 15 A apart on one side of the dimer, and two C-terminal sugar-binding sites are 87 A apart on the other side. Galactose binding is achieved by common hydrogen bonds for the two binding sites via hydroxy groups 3-OH and 4-OH and hydrophobic contact by an aromatic ring. In addition, at the N-terminal site 2-OH forms hydrogen bonds with Asp27 and Lys41, and at the C-terminal site 3-OH and 6-OH undergo water-mediated interactions and C5 has a hydrophobic contact. MLI is a galactose-specific lectin and shows little affinity for N-acetylgalactosamine. The reason for this is discussed. Structural differences among the RIPs investigated in this study (their quaternary structures, location of sugar-binding sites, and fine sugar specificities of their B-chains, which could have diverged through evolution from a two-domain protein) may affect the binding sites, and consequently the cellular transport processes and biological responses of these toxins.
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PMID:Crystal structure at 3 A of mistletoe lectin I, a dimeric type-II ribosome-inactivating protein, complexed with galactose. 1282 44

Pathological conditions, such as Parkinson's disease and attention deficit hyperactivity disorder, have been linked to alterations of specific dopamine (DA) pathways. However, since exogenous DA does not cross the blood-brain barrier, DA levels can be modulated e.g. by DA precursors or DA reuptake blockers. Hereby histochemical, analytical and behavioral evidence shows that a galactosylated form of DA (GAL-DA) carries DA into the brain, thus modulating activity and nonselective attention in rats. To this aim adult male rats of the Naples high-excitability (NHE) and random bred controls (NRB) lines were given a single i.p. injection of GAL-DA (10 or 100 mg/kg). Three hours later the behavior was videotaped and analyzed for horizontal activity, orienting frequency and scanning duration. The dose of 100 mglkg of GAL-DA reduced by 25% the horizontal activity in NHE rats, mainly in the first part of the testing period. No effect was observed on orienting frequency or on scanning duration. However, GAL-DA 100 mg/kg was associated with longer rearing episodes in the second part of the testing period in NHE rats. In parallel experiments histochemistry with a galactose-specific lectin showed 10% increase in galactose residues into the striatum between 0.5 and 3.0 h. To quantify the level of GAL-DA, its metabolite DA-succinate and DA in the prefrontal cortex, neostriatum, and cerebellum, rats were killed 2.0 h after the injection of prodrug. Mass high performance liquid chromatography (HPLC) was used for analysis of GAL-DA and DA succinate whereas electrochemical HPLC for DA. Both HPLC techniques demonstrate that GAL-DA carries and releases DA into the brain. Specifically 100 mg/kg of GAL-DA increased DA level in the striatum in the NHE rats only. Moreover, DA in the mesencephalon (MES) was correlated positively with striatal and prefrontal cortex DA in NHE rats. In contrast DA in the MES was negatively correlated with striatal DA in NRB. GAL-DA disrupted these correlations in both rat lines. Thus, this new DA prodrug may modify DA neurotransmission and might have a potential clinical application.
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PMID:Galactosylated dopamine enters into the brain, blocks the mesocorticolimbic system and modulates activity and scanning time in Naples high excitability rats. 1816 52

Galactose C3-triazole derivatives were synthesized by Cu(I)-catalyzed cycloaddition between acetylenes and galactose C3-azido derivatives. Evaluation against galectin-3, 7, 8N (N-terminal) and 9N (N-terminal) revealed 1,4-disubstituted triazoles to be high-affinity inhibitors of galectin-3 with selectivity over galectin-7, 8N, and 9N. Conformational analysis of 1,4-di- and 1,4,5-tri-substituted galactose C3-triazoles suggested that a triazole C5-substituent interfered sterically with the galectin proteins, which explained their poor affinities compared to the corresponding 1,4-disubstituted triazoles. Introduction of two 1,4-disubstituted triazole moieties onto thiodigalactoside resulted in affinities down to 29 nM for galectin-3.
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PMID:1H-1,2,3-triazol-1-yl thiodigalactoside derivatives as high affinity galectin-3 inhibitors. 2053 69

In this study, we found that expression and secretion of galectin-3 (GAL-3) were upregulated by amyloid-beta42 (Abeta42) exposure in human umbilical cord blood-derived mesenchymal stem cell (hUCB-MSC) without cell death. Abeta42-exposed rat primary cortical neuronal cells co-treated with recombinant GAL-3 were protected from neuronal death in a dose-dependent manner. hUCB-MSCs were cocultured with Abeta42-exposed rat primary neuronal cells or the neuroblastoma cell line, SH-SY5Y in a Transwell chamber. Coculture of hUCB-MSCs reduced cell death of Abeta42-exposed neurons and SH-SY5Y cells. This neuroprotective effect of hUCB-MSCs was reduced significantly by GAL-3 siRNA. These data suggested that hUCB-MSC-derived GAL-3 is a survival factor against Abeta42 neurotoxicity.
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PMID:Galectin-3 secreted by human umbilical cord blood-derived mesenchymal stem cells reduces amyloid-beta42 neurotoxicity in vitro. 2065 11

Recently, liquid-based cytology (LBC) has been widely applied to various samples in diagnostic cytology and its usefulness has been reported. In this study, we investigated thyroid cytology that applied LBC and immunocytochemistry to achieve more objective diagnosis and greater diagnostic accuracy. This study included 125 cases (57 papillary carcinomas (PCs), 22 follicular tumors, 43 adenomatous goiters and 3 with Basedow's disease). After preparing the LBC slide, immunocytochemical staining was performed on each slide with six antibodies (HBME-1, cytokeratin 19 (CK19), high molecular weight cytokeratin (34JE12), galectin-3, CD15 and CA 19-9). All antibodies presented immunopositivity frequently in PCs, but only a few or some of them were positive in other cases. These antibodies were considered positive markers for PCs, and the most reliable marker was 34betaE12; its sensitivity, specificity and diagnostic accuracy were 82.5%, 100% and 92.0%, respectively. Relations of immunocytochemical profiles against these markers were assessed using panel 34betaE12, GAL-3 and CK19. More than or equal to two of these markers showed co-positive in 53 of 57 PCs, and negative for all markers was observed in only one case. In the other (non PC) cases, the former was 0 of 58 and the latter was 40 cases. In this panel, the sensitivity, specificity and diagnostic accuracy were 93.0%, 100% and 96.8%, respectively. All of these values were higher than or equal to single values of 34betaE12. We concluded that the panel in this study is useful for more objective and accurate diagnosis of thyroid cytology.
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PMID:Immunocytochemical analysis for differential diagnosis of thyroid lesions using liquid-based cytology. 2161 33

D-(+)-Galactose-conjugated single-walled carbon nanotubes (SWCNTs) were synthesized for use as biosensors to detect the cancer marker galectin-3. To investigate the binding of galectin-3 to the d-(+)-galactose-conjugated SWCNTs, an electrochemical biosensor was fabricated by using molybdenum electrodes. The binding affinities of the conjugated SWCNTs to galectin-3 were quantified using electrochemical sensitivity measurements based on the differences in resistance together with typical I-V characterization. The electrochemical sensitivity measurements of the d-(+)-galactose-conjugated SWCNTs differed significantly between the samples with and without galectin-3. This indicates that d-(+)-galactose-conjugated SWCNTs are potentially useful electrochemical biosensors for the detection of cancer marker galectin-3.
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PMID:D-(+)-galactose-conjugated single-walled carbon nanotubes as new chemical probes for electrochemical biosensors for the cancer marker galectin-3. 2168 60

The role of pro-angiogenic marker galectin-3 (GAL-3) was examined in differential diagnosis of follicular neoplasms of thyroid into histological subsets of follicular adenoma (FA), follicular carcinoma (FC) and follicular variant of papillary thyroid carcinoma (FVPTC). The study included 22 cases from January 2006 to June 2011 comprising of FA (n = 12), FC (n = 3) and FVPTC (n = 7). Immunohistochemical evaluation of GAL-3 was performed on representative histologic sections from the resected thyroid specimens. The proportion of stained cells and intensity of staining in tumor blood vessels were evaluated. GAL-3 expression showed that angiogenesis was prominent in malignancy (FC and FVPTC) and negative in non-neoplastic thyroid parenchyma and benign condition (FA). GAL-3 expression was found to differentiate benign from malignant follicular neoplasms. Focal and diffuse positivity for GAL-3 was found to be associated with FC and FVPTC respectively, thus GAL-3 can be used as a immunohistochemical marker in the differential diagnosis of follicular neoplasms of thyroid based on the type of expression. Limitation of this study was relatively less number of cases studied; however, this data need to be corroborated in larger cohort.
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PMID:Role of pro-angiogenic marker galectin-3 in follicular neoplasms of thyroid. 2325 27


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