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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
TL;DR: The use of galectin histochemistry for the analysis of diethylstilbestrol-induced renal tumors in male Syrian hamster kidney is reported, illustrating the feasibility to complement immunohistochemical data by application of the tissue lectins as probes, and to detect regulation of galECTin reactivity with differential characteristics within tumor progression in vivo and unique features of the tumor cell line in vitro and in vivo.
Abstract: Endogenous lectins act as effectors of cellular activities such as growth regulation, migration, and adhesion. Following their immunohistochemical localization in our previous study (Saussez et al. in Histochem Cell Biol 123:29-41, 2005) we purified several galectins and used them as tools for monitoring accessible binding sites. Herein, we report the use of galectin histochemistry for the analysis of diethylstilbestrol (DES)-induced renal tumors in male Syrian hamster kidney (SHKT). Sections of normal kidney and DES-treated kidney were analyzed with biotinylated galectins-1, -3 (full-length and truncated), and -7. Accessible binding sites were detected, localization was predominantly extracellular and confined to medium-sized and large tumors. Monitoring the SHKT-derived HKT-1097 line, processed in vitro or as xenograft material, cytoplasmic and nuclear staining for galectins-1, -3, and -3tr could be observed. Adaptation of SHKT cells to long-term growth in culture is thus associated with emergence of this signal. Our data set illustrates the feasibility to complement immunohistochemical data by application of the tissue lectins as probes, and to detect regulation of galectin reactivity with differential characteristics within tumor progression in vivo and unique features of the tumor cell line in vitro and in vivo.

14 citations

Journal ArticleDOI
TL;DR: 1H, 13C, and 15N chemical shift assignments for human galectin-7 dimer as determined by using heteronuclear, triple resonance NMR spectroscopy.
Abstract: Galectins are multifunctional proteins with carbohydrate/protein-binding properties and distinct expression profiles. Homodimeric galectin-7 (p53-induced gene 1) is a potent pro-apoptotic effector with clinical relevance. Here, we report 1H, 13C, and 15N chemical shift assignments for human galectin-7 dimer as determined by using heteronuclear, triple resonance NMR spectroscopy.

14 citations

Journal ArticleDOI
TL;DR: The significance of glycosylation and the role of galectin class of β-galactoside-binding proteins modulate angiogenesis by novel carbohydrate-based recognition systems involving interactions between glycans of angiogenic cell surface receptors and galectins are discussed.
Abstract: Ocular neovascularization can affect almost all the tissues of the eye: the cornea, the iris, the retina, and the choroid. Pathological neovascularization is the underlying cause of vision loss in common ocular conditions such as diabetic retinopathy, retinopathy of prematurity and age-related macular neovascularization. Glycosylation is the most common covalent posttranslational modification of proteins in mammalian cells. A growing body of evidence demonstrates that glycosylation influences the process of angiogenesis and impacts activation, proliferation, and migration of endothelial cells as well as the interaction of angiogenic endothelial cells with other cell types necessary to form blood vessels. Recent studies have provided evidence that members of the galectin class of β-galactoside-binding proteins modulate angiogenesis by novel carbohydrate-based recognition systems involving interactions between glycans of angiogenic cell surface receptors and galectins. This review discusses the significance of glycosylation and the role of galectins in the pathogenesis of ocular neovascularization.

14 citations

Journal ArticleDOI
TL;DR: Recent progress is described in understanding the role of galectin-3 in cancer biology, with emphasis on bladder tumor progression and metastasis.

14 citations

Journal ArticleDOI
18 Apr 2019
TL;DR: This work reports that the synthesis of novel C1-galactopyranosyl heteroaryl derivatives as galectin inhibitors, in which galECTin selectivity is governed by the composition of the heterocycle and affinity, is driven by the structure of the aryl substituent to give compounds selective for either galectIn-1 or galect in-3.
Abstract: Galectins are carbohydrate-recognizing proteins involved in many different pathological processes, including cancer and immune-related disorders. Inhibitors of galectins have evolved from natural oligosaccharides toward more drug-like truncated galactoside scaffolds that only retain key specific interactions of the galactose scaffolds with the galectin carbohydrate recognition domains. In this context, C1-galactosides are attractive and stable scaffolds, and this work reports that the synthesis of novel C1-galactopyranosyl heteroaryl derivatives as galectin inhibitors, in which galectin selectivity is governed by the composition of the heterocycle and affinity, is driven by the structure of the aryl substituent to give compounds selective for either galectin-1 or galectin-3. The affinities are close to or better than those of lactose and other natural galectin-binding disaccharides, selectivities induced by the C1-heteroaryl groups are superior to lactose, and compound hydrolytic stabilities and drug-like...

14 citations


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