Effects of Sialic Acid Substitutions on Recognition by Sambucus nigra Agglutinin and Maackia amurensis Hemagglutinin

Linden, Els C.M. Brinkman-Van der; Sonnenburg, Justin L.; Varki, Ajit

doi:10.1006/abio.2001.5539

Cited by 59 publications

(51 citation statements)

References 51 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…3A). MAL I, which binds Neu5Ac␣2,3Gal but (11,30,38), was Յ60%. Therefore, all three lectins could interfere directly with EV70 binding by competing for virus attachment sites containing ␣2,3-linked sialic acid.…”

Section: Ev70mentioning

confidence: 95%

“…We also examined the binding of MAL I lectin, which preferentially binds to ␣2,3-linked sialic acid; however, we saw no decrease in MAL I binding to U-937 cells following sialidase treatment (data not shown). This may be explained by the fact that MAL I binds both sialylated and unsialylated glycans under certain experimental conditions, including flow cytometry (11). Lectin binding to ␣2,3-linked sialic acid inhibits EV70 attachment.…”

Section: Ev70mentioning

confidence: 99%

See 1 more Smart Citation

Enterovirus 70 Binds to Different Glycoconjugates Containing α2,3-Linked Sialic Acid on Different Cell Lines

Nokhbeh

Hazra

Alexander

et al. 2005

J Virol

View full text Add to dashboard Cite

Sialic acids are a ubiquitous family of negatively charged sugar molecules found on the surfaces of mammalian cells, usually at the termini of glycans attached to glycoproteins, glycosphingolipids, and the proteoglycan keratan sulfate (2, 10, 72). Sialic acid is an essential component of cell surface receptors for a variety of microorganisms and microbial toxins (2,34,47). Members of at least eight different virus families-Ortho-

show abstract

Section: Ev70mentioning

confidence: 95%

Section: Ev70mentioning

confidence: 99%

Enterovirus 70 Binds to Different Glycoconjugates Containing α2,3-Linked Sialic Acid on Different Cell Lines

Nokhbeh

Hazra

Alexander

et al. 2005

J Virol

View full text Add to dashboard Cite

show abstract

“…Preparations called 'MAA' are typically unspecified mixtures of two Maackia lectins, that is, one originally identified as a 'leukoagglutinin' (MAL) and a second one, a 'hemagglutinin' (MAH). [47][48][49] As these two lectins have differing specificity, the significance of any published results using 'MAA' preparations must be interpreted cautiously. A further complication arises because the MAL lectin is sometimes sold as 'MAL-I' and MAH as 'MAL-II'.…”

Section: Detection Of a Nonhuman Sialic Acid Neu5gc In Human Tissuesmentioning

confidence: 99%

“…A further complication arises because the MAL lectin is sometimes sold as 'MAL-I' and MAH as 'MAL-II'. 49 Finally, MAL can also recognize a glycan wherein the Sia is replaced with a sulfate ester at the 3-position of galactose. 50 Clearly, use of these lectins must be better controlled if interpretations are to be accurate.…”

Section: Detection Of a Nonhuman Sialic Acid Neu5gc In Human Tissuesmentioning

confidence: 99%

Diversity in cell surface sialic acid presentations: implications for biology and disease

Varki

2007

Laboratory Investigation

Self Cite

466

398

View full text Add to dashboard Cite

Sialic acids (Sias) are typically found as terminal monosaccharides attached to cell surface glycoconjugates. They play many important roles in many physiological and pathological processes, including microbe binding that leads to infections, regulation of the immune response, the progression and spread of human malignancies and in certain aspects of human evolution. This review will provide some examples of these diverse roles of Sias and briefly address immunohistochemical approaches to their detection.

show abstract

“…Thus, LacNAc or more likely poly(LacNAc) in the (2,2,6) tri-and/or (2,4,2,6) tetra-antennary N-glycans is necessary for the increase of ROMK1 at the cell surface by soluble Klotho. Plant lectins are useful tools for studying the structure of glycans because they bind to specific sugar residues (Corfield et al, 1983;Brinkman-Van der Linden et al, 2002). Among them, SNA specifically bind ␣2,6-sialylated, but not ␣2,3-sialylated, glycoconjugates (Corfield et al, 1983;BrinkmanVan der Linden et al, 2002).…”

Section: Regulation Of Romk1 By Klotho 41mentioning

confidence: 99%

Regulation of Renal Outer Medullary Potassium Channel and Renal K⁺Excretion by Klotho

Kuy¹,

Hu²,

Kurosu³

et al. 2009

Mol Pharmacol

186

158

View full text Add to dashboard Cite

Klotho is an aging-suppression protein predominantly expressed in kidney, parathyroid glands, and choroids plexus of the brain. The extracellular domain of Klotho, a type-1 membrane protein, is secreted into urine and blood and may function as an endocrine or paracrine hormone. The functional role of Klotho in the kidney remains largely unknown. Recent studies reported that treatment by the extracellular domain of Klotho (KLe) increases cell-surface abundance of transient receptor potential vanilloid type isoform 5, an epithelial Ca 2ϩ channel critical for Ca 2ϩ reabsorption in the kidney. Whether Klotho regulates surface expression of other channels in the kidney is not known. Here, we report that KLe treatment increases the cell-membrane abundance of the renal K ϩ channel renal outer medullary potassium channel 1 (ROMK1) by removing terminal sialic acids from N-glycan of the channel. Removal of sialic acids exposes underlying disaccharide galactose-Nacetylglucosamine, a ligand for a ubiquitous galactoside-binding lectin galectin-1. Binding to galectin-1 at the extracellular surface prevents clathrin-mediated endocytosis of ROMK1 and leads to accumulation of functional channel on the plasma membrane. Intravenous administration of KLe increases the level of Klotho in urine and increases urinary excretion of K ϩ . These results suggest that Klotho may have a broader function in the regulation of ion transport in the kidney.Mice homozygous for hypomorphic insertional mutation in the Klotho gene exhibit multiple phenotypes closely resembling human aging, including shortened life span, muscle and skin atrophy, pulmonary emphysema, osteopenia, hyperphosphatemia, and vascular and soft tissue calcification (Kuro-o et al., 1997). The encoded protein, Klotho, is a type-1 single-pass membrane protein with a large extracellular domain, a membrane-spanning segment, and a short (ϳ20 amino acids) intracellular carboxyl terminus (Kuro-o et al., 1997). Overexpression of Klotho extends life span in mice, supporting that Klotho is an aging-suppression molecule (Kurosu et al., 2005).The biological function of Klotho and how Klotho deficiency causes aging remain elusive. Klotho is predominantly expressed in distal renal tubules of the kidney, parathyroid glands, and choroids plexus of the brain (Kuro-o et al., 1997;Kurosu et al., 2005;Imura et al., 2007). The large extracellular domain of Klotho is cleaved by a membrane-anchored protease ADAM10 and secreted into blood, urine, and cerebrospinal fluid Kurosu et al., 2005;Chen et al., 2007). The presence of the extracellular domain of Klotho in blood, urine, and cerebrospinal fluid suggests that it may function as an endocrine or paracrine hormone. Recent studies have revealed distinct biological functions for membrane Klotho and the extracellular domain of Klotho Article, publication date, and citation information can be found at http://molpharm.aspetjournals.org. doi:10.1124/mol.109.055780.ABBREVIATIONS: FGF, fibroblast growth factor; KLe, extracellular domain of Klotho; KL1...

show abstract

Effects of Sialic Acid Substitutions on Recognition by Sambucus nigra Agglutinin and Maackia amurensis Hemagglutinin

Cited by 59 publications

References 51 publications

Enterovirus 70 Binds to Different Glycoconjugates Containing α2,3-Linked Sialic Acid on Different Cell Lines

Enterovirus 70 Binds to Different Glycoconjugates Containing α2,3-Linked Sialic Acid on Different Cell Lines

Diversity in cell surface sialic acid presentations: implications for biology and disease

Regulation of Renal Outer Medullary Potassium Channel and Renal K⁺Excretion by Klotho

Contact Info

Product

Resources

About

Effects of Sialic Acid Substitutions on Recognition by Sambucus nigra Agglutinin and Maackia amurensis Hemagglutinin

Cited by 59 publications

References 51 publications

Enterovirus 70 Binds to Different Glycoconjugates Containing α2,3-Linked Sialic Acid on Different Cell Lines

Enterovirus 70 Binds to Different Glycoconjugates Containing α2,3-Linked Sialic Acid on Different Cell Lines

Diversity in cell surface sialic acid presentations: implications for biology and disease

Regulation of Renal Outer Medullary Potassium Channel and Renal K+Excretion by Klotho

Contact Info

Product

Resources

About

Regulation of Renal Outer Medullary Potassium Channel and Renal K⁺Excretion by Klotho