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Galectin

About: Galectin is a research topic. Over the lifetime, 2076 publications have been published within this topic receiving 103409 citations. The topic is also known as: IPR001079 & Galectin.


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Journal ArticleDOI
06 Dec 2014-Blood
TL;DR: The findings suggest that GCS-100 can induce apoptosis in AML cells as a single agent or in combination with the BH3 mimetic ABT-737 and the agent is effective even in the presence of MSC suggesting it could be efficacious in the leukemia niche.

1 citations

Journal ArticleDOI
TL;DR: During affinity chromatographic purification of bovine heart 14 kDa galactose-binding lectin (galectin 1) on lactose-Sepharose, several high molecular weight non-lectin glycoproteins were co-purified with the lectin, indicating that a complex containing galectin molecules bound sugar specifically to endogenous glycoprotein sites with sugar binding sites still available had been retained on lactoses.
Abstract: During affinity chromatographic purification of bovine heart 14 kDa galactose-binding lectin (galectin 1) on lactose-Sepharose, several high molecular weight non-lectin glycoproteins were co-purified with the lectin. Glycoprotein binding to the affinity matrix was neither hydrophobic nor ionic, but galactose-dependent since lactose abolished binding. Purification of galectin from the co-purified glycoproteins by affinity electrophoresis in presence of the specific sugar lactose increased agglutination activity about 65-fold, indicating that a complex containing galectin molecules bound sugar specifically to endogenous glycoproteins with sugar binding sites still available had been retained on lactose-Sepharose.

1 citations

Book ChapterDOI
01 Jan 2022
TL;DR: In this article , the fluorescent protein GFP was fused with the exosomal sorting motif of galectin-3 to direct GFP into exosomes, which can be assessed by proteinase K accessibility analysis.
Abstract: Cells use unconventional secretion to deliver the β-galactoside binding lectin galectin-3 from the cell interior into the extracellular milieu. This process starts with galectin-3 recruitment into intraluminal vesicles (ILVs), which are later released at the plasma membrane as exosomes. Electron microscopy is utilized to determine the location of GFP-tagged galectin-3 in pelleted exosomes. We also describe how these vesicles are harvested from cell culture media to determine their composition. The fluorescent protein GFP was fused with the exosomal sorting motif of galectin-3 to direct GFP into exosomes. Recruitment of this fusion construct into the lumen of exosomes can be assessed by proteinase K accessibility analysis.

1 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023182
2022176
2021107
2020120
201995
2018119