Topic
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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TL;DR: Characterization of the forms present by surface-enhanced laser desorption ionization time-of-flight mass spectrometry (SELDI-TOF MS), based on hydrophilic interactions or immunorecognition, provided a sensitive tool for detection of the fine differences among the diverse molecular forms.
Abstract: Galectin-1 (gal-1) is the best studied member of the galectin family of the
human placenta assumed to play important roles in pregnancy. Standard
isolation of gal-1 from human placenta using lactose extraction and affinity
chromatography in the presence of a reducing agent, produced several known
forms of gal-1, which were compared to the recombinant human gal-1 (rhgal-1)
and oxidized recombinant human gal-1 (Ox-gal-1). Isolated placental gal-1
retained lectin binding activity, evidenced by hemagglutination and dot blot
lectin assays. Characterization of the forms present by surface-enhanced
laser desorption ionization time-of-flight mass spectrometry (SELDI-TOF MS),
based on hydrophilic interactions or immunorecognition, provided a sensitive
tool for detection of the fine differences among the diverse molecular
forms. The forms detected included previously established biologically
active oxidized gal-1 and reduced gal-1, as well as some other currently
uncharacterized (less investigate forms. [Projekat Ministarstva nauke
Republike Srbije, br. 173004]
1 citations
Patent•
21 Mar 2001
TL;DR: In this paper, a new rainbow trout (Oncorhynchus mykiss) glycoprotein galectin consisting of a recombinant protein which contains the amino acid sequence shown by the formula was obtained by isolating mRNA from the rainbow trout head kidney or the like, and then screening the cDNA library using its partial sequence as a probe, then integrating the obtained gene into a vector for expression in a host cell.
Abstract: PROBLEM TO BE SOLVED: To obtain a new protein which contains a specific amino acid sequence which can contain mutation(s), has a galectin activity, binds to β-galactose, and can be used as a reagent for elucidating the immunological mechanism of the fish, a reagent for diagnosing fish diseases, etc SOLUTION: This is a new rainbow trout (Oncorhynchus mykiss) glycoprotein galectin consisting of a (recombinant) protein which contains the amino acid sequence shown by the formula, or an amino acid sequence modified by deleting, substituting, or adding one amino acid or more from, in, or to the amino acid sequence, and has a galectin activity, binds to β-galactose A gene coding for the protein is useful as a reagent for elucidating the immuneological mechanism of the fish, a reagent for diagnosing fish diseases, etc The protein is obtained by isolating mRNA from the rainbow trout head kidney or the like, preparing a cDNA library using the obtained mRNA, screening the cDNA library using its partial sequence as a probe, followed by integrating the obtained gene into a vector for expression in a host cell
1 citations
1 citations
TL;DR: The aim of this study was to evaluate the effect of galectin-1 inhibition by shRNA or PTX-008, a topomimetic of antiangiogenic drug Anginex, on in vitro cancer cells invasion and on in vivo tumor growth and metastasis development.
Abstract: Background. Galectin-1 belongs to a phylogenetically conserved family of carbohydrate binding lectins (galectins) that share a conserved carbohydrate recognition domain and are involved in tumor growth and metastasis. The aim of this study was to evaluate the effect of galectin-1 inhibition by shRNA or PTX-008, a topomimetic of antiangiogenic drug Anginex, on in vitro cancer cells invasion and on in vivo tumor growth and metastasis development. Material and Methods. In vitro invasion was evaluated using Matrigel assay. Transfection of SQ20B headn 2011 Apr 2-6; Orlando, FL. Philadelphia (PA): AACR; Cancer Res 2011;71(8 Suppl):Abstract nr 4520. doi:10.1158/1538-7445.AM2011-4520
1 citations
TL;DR: Analysis of the interaction patterns of the carbohydrate at the binding site of wild type and mutated lectins revealed that sialic acid contributed more to the binding when compared with other sugar units in the trisaccharide and enhanced the binding specificity of ACG towards α(2,6)-linked sialyllactose.
1 citations