Visualization of Galectin-3 Oligomerization on the Surface of Neutrophils and Endothelial Cells Using Fluorescence Resonance Energy Transfer
TLDR
Data suggest that galectin-3 lattices are robust and could, thus, be involved, as previously proposed, in the restriction of receptor clustering, and lattice formation.About:
This article is published in Journal of Biological Chemistry.The article was published on 2007-01-12 and is currently open access. It has received 215 citations till now. The article focuses on the topics: Cell activation & Galectin.read more
Citations
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Protein-glycan interactions in the control of innate and adaptive immune responses
TL;DR: An increasing number of studies reveal the relevance of glycosylation to pathogen recognition, to the modulation of the innate immune system and to the control of immune cell homeostasis and inflammation.
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Mammalian glycosylation in immunity
TL;DR: This Review focuses on the emerging immunological roles of the mammalian glycome, which is one of the four fundamental macromolecular components of all cells, and is highly regulated in the immune system.
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The regulation of inflammation by galectin‐3
Neil C. Henderson,Tariq Sethi +1 more
TL;DR: The manipulation of galectin‐3 expression as a potentially novel therapeutic strategy in the treatment of a broad range of inflammatory diseases is discussed.
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Galectin-1, -2, and -3 Exhibit Differential Recognition of Sialylated Glycans and Blood Group Antigens
Sean R. Stowell,Connie M. Arthur,Padmaja Mehta,Kristen A. Slanina,Ola Blixt,Hakon Leffler,David F. Smith,Richard D. Cummings +7 more
TL;DR: It is demonstrated that each of these galectins mechanistically differ in their binding to glycans on the microarrays and that these differences are reflected in the determinants required for cell binding and signaling.
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Galectins at a glance.
TL;DR: Recent literature on the many cellular activities that have been ascribed to galectins are summarized, including carbohydrate-independent interactions with cytosolic or nuclear targets and carbohydrate-dependent interactions with extracellular glycoconjugates.
References
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Galectins. Structure and function of a large family of animal lectins.
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Galectins: a family of animal beta-galactoside-binding lectins.
Samuel H. Barondes,Vincent Castronovo,Douglas N.W. Cooper,Richard D. Cummings,Kurt Drickamer,Ten Felzi,Michael A. Gitt,Jun Hirabayashi,Colin Hughes,Ken-ichi Kasai,Hakon Leffler,Fu-Tong Liu,Reuben Lotan,Arthur M. Mercurio,Michel Monsigny,Shiv Pillai,Françoise Poirer,Avraham Raz,Peter W.J. Rigby,James M. Rini,John L. Wang +20 more
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The renaissance of fluorescence resonance energy transfer
TL;DR: Improvements in fluorescence resonance energy transfer have led to qualitative and quantitative improvements in the technique, including increased spatial resolution, distance range, and sensitivity.
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Oligosaccharide specificity of galectins: a search by frontal affinity chromatography.
Jun Hirabayashi,Tomomi Hashidate,Yoichiro Arata,Nozomu Nishi,Takanori Nakamura,Mitsuomi Hirashima,Tadasu Urashima,Toshihiko Oka,Masamitsu Futai,Werner E.G. Müller,Fumio Yagi,Ken-ichi Kasai +11 more
TL;DR: In this paper, a frontal affinity chromatography (FAC) was used to quantitatively analyze the interactions at 20 °C between 13 galectins including 16 CRDs originating from mammals, chick, nematode, sponge, and mushroom, with 41 pyridylaminated (PA) oligosaccharides.
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Negative regulation of T-cell activation and autoimmunity by Mgat5 N -glycosylation
TL;DR: It is demonstrated that a deficiency in β1,6 N-acetylglucosaminyltransferase V (Mgat5), an enzyme in the N-glycosylation pathway, lowers T-cell activation thresholds by directly enhancing TCR clustering.