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)

Self-assembled monolayers (SAMs) of Gb3 mimics having different lengths of alkyl chains were prepared on gold surfaces, and their interactions with galactose-specific lectin (RCA(120)) and Shiga toxins (Stxs) were investigated by a quartz crystal microbalance (QCM) in aqueous solutions. Their interaction with RCA(120) was enhanced owing to the "cluster effect," regardless of the alkyl chain length of the SAMs. The interaction with Stxs was dependent on the alkyl chain length of Gb3 mimics. Stx-1 and Stx-2 showed a stronger affinity to the Gb3C2 SAM with ethyl disulfide and to the Gb3C10 with decyl disulfide, respectively. Gb3 glycoconjugate polymer with no alkyl spacer inhibited the adsorption of Stx-1 to Gb3C10 SAM but did not inhibit the adsorption of Stx-2 to Gb3C10 SAM. The results suggest that the alkyl chain of the glycolipid takes part in the binding to Stx-2 but not to Stx-1, which is also supported by the computer simulation of Stx-1 with a Gb3 model substance.
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PMID:Self-assembled monolayers of globotriaosylceramide (Gb3) mimics: surface-specific affinity with shiga toxins. 1241 69

Shiga toxins (Stx) 1 and 2 are responsible for intestinal and systemic sequelae of infection by enterohemorrhagic Escherichia coli (EHEC). However, the mechanisms through which enterocytes are damaged remain unclear. While secondary damage from ischemia and inflammation are postulated mechanisms for all intestinal effects, little evidence excludes roles for more primary toxin effects on intestinal epithelial cells. We now document direct pathologic effects of Stx on intestinal epithelial cells. We study a well-characterized rabbit model of EHEC infection, intestinal tissue and stool samples from EHEC-infected patients, and T84 intestinal epithelial cells treated with Stx1. Toxin uptake by intestinal epithelial cells in vitro and in vivo causes galectin-3 depletion from enterocytes by increasing the apical galectin-3 secretion. This Shiga toxin-mediated galectin-3 depletion impairs trafficking of several brush border structural proteins and transporters, including villin, dipeptidyl peptidase IV, and the sodium-proton exchanger 2, a major colonic sodium absorptive protein. The mistargeting of proteins responsible for the absorptive function might be a key event in Stx1-induced diarrhea. These observations provide new evidence that human enterocytes are directly damaged by Stx1. Conceivably, depletion of galectin-3 from enterocytes and subsequent apical protein mistargeting might even provide a means whereby other pathogens might alter intestinal epithelial absorption and produce diarrhea.
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PMID:Shiga toxin 1 interaction with enterocytes causes apical protein mistargeting through the depletion of intracellular galectin-3. 1974 79

Functionalization of quantum dots (QDs) with a single biomolecular tag using traditional approaches in bulk solution has met with limited success. DNA polyhedra consist of an internal void bounded by a well-defined three-dimensional structured surface. The void can house cargo and the surface can be functionalized with stoichiometric and spatial precision. Here, we show that monofunctionalized QDs can be realized by encapsulating QDs inside DNA icosahedra and functionalizing the DNA shell with an endocytic ligand. We deployed the DNA-encapsulated QDs for real-time imaging of three different endocytic ligands-folic acid, galectin-3 (Gal3) and the Shiga toxin B-subunit (STxB). Single-particle tracking of Gal3- or STxB-functionalized QD-loaded DNA icosahedra allows us to monitor compartmental dynamics along endocytic pathways. These DNA-encapsulated QDs, which bear a unique stoichiometry of endocytic ligands, represent a new class of molecular probes for quantitative imaging of endocytic receptor dynamics.
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PMID:Quantum dot-loaded monofunctionalized DNA icosahedra for single-particle tracking of endocytic pathways. 2754 58