[4] Enzymatic deglycosylation of asparagine-linked glycans: Purification, properties, and specificity of oligosaccharide-cleaving enzymes from Flavobacterium meningosepticum

Tarentino, Anthony L.; Plummer, Thomas H.

doi:10.1016/0076-6879(94)30006-2

Cited by 270 publications

(184 citation statements)

References 10 publications

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“…The specificity of EndoS for the N-linked glycans of a specific glycoprotein (IgG) makes it stand out from the other known enzymes in family 18 of glycosyl hydrolases. Most of these enzymes, including EndoF 1-3 from Elizabethkingia meningoseptica (formerly Flavobacterium meningosepticum), are specific for certain glycan structures that can be attached to any protein or peptide and are enhanced by or require denaturation of the protein backbone (30). This is in complete contrast to EndoS, which exclusively hydrolyzes native IgG or IgG Fc, suggesting that the substrate specificity depends on proteinprotein interactions between the enzyme and IgG Fc (2, 4).…”

Section: Discussionmentioning

confidence: 60%

IgG glycan hydrolysis by a bacterial enzyme as a therapy against autoimmune conditions

Collin

Shannon

Björck

2008

Proc. Natl. Acad. Sci. U.S.A.

108

117

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Section: Discussionmentioning

confidence: 60%

IgG glycan hydrolysis by a bacterial enzyme as a therapy against autoimmune conditions

Collin

Shannon

Björck

2008

Proc. Natl. Acad. Sci. U.S.A.

108

117

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“…Several enzymes are available for releasing Nglycans. The most popular is PNGase F 11 . PNGase F cleaves off the intact glycan as glycosylamine, which is readily converted to regular glycan.…”

Section: Release Of Glycansmentioning

confidence: 99%

Analysis of protein glycosylation by mass spectrometry

2007

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We present a detailed protocol for the structural analysis of protein-linked glycans. In this approach, appropriate for glycomics studies, N-linked glycans are released using peptide N-glycosidase F and O-linked glycans are released by reductive alkaline b-elimination. Using strategies based on mass spectrometry (matrix-assisted laser desorption/ionization-time of flight mass spectrometry and nano-electrospray ionization mass spectrometry/mass spectrometry (nano-ESI-MS-MS)), chemical derivatization, sequential exoglycosidase digestions and linkage analysis, the structures of the N-and/or O-glycans are defined. This approach can be used to study the glycosylation of isolated complex glycoproteins or of numerous glycoproteins encountered in a complex biological medium (cells, tissues and physiological fluids).

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“…One distinguishing feature for these two types of N-glycans is their sensitivity to digestion with Endo H. In general, N-glycans on proteins prior to their delivery to the medial Golgi complex are substrates for Endo H, whereas Nglycans on proteins after this point in the secretory pathway are not substrates due to processing by N-acetylglucosaminyltransferase I and mannosidase II. PNGase F, by contrast, cleaves N-glycans from glycoproteins regardless of their localization along the secretory pathway (25). When co-expressed with Ost␤, the Ost␣ N-linked carbohydrate was processed to an Endo H-resistant form (Fig.…”

Section: Expression and Localization Of Mouse Ost␣ And Ost␤ Inmentioning

confidence: 99%

The Heteromeric Organic Solute Transporter α-β, Ostα-Ostβ, Is an Ileal Basolateral Bile Acid Transporter

Dawson

Hubbert

Haywood

et al. 2005

Journal of Biological Chemistry

348

364

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Bile acids are transported across the ileal enterocyte brush border membrane by the well characterized apical sodium-dependent bile acid transporter (Asbt) Slc10a2; however, the carrier(s) responsible for transporting bile acids across the ileocyte basolateral membrane into the portal circulation have not been fully identified. Transcriptional profiling of wild type and Slc10a2 null mice was employed to identify a new candidate basolateral bile acid carrier, the heteromeric organic solute transporter (Ost)␣-Ost␤. By Northern blot analysis, Ost␣ and Ost␤ mRNA was detected only in mouse kidney and intestine, mirroring the horizontal gradient of expression of Asbt in the gastrointestinal tract. Analysis of Ost␣ and Ost␤ protein expression by immunohistochemistry localized both subunits to the basolateral surface of the mouse ileal enterocyte. The transport properties of Ost␣-Ost␤ were analyzed in stably transfected Madin-Darby canine kidney cells. Coexpression of mouse Ost␣-Ost␤, but not the individual subunits, stimulated Na ؉ -independent bile acid uptake and the apical-to-basolateral transport of taurocholate. In contrast, basolateral-to-apical transport was not affected by Ost␣-Ost␤ expression. Co-expression of Ost␣ and Ost␤ was required to convert the Ost␣ subunit to a mature glycosylated endoglycosidase H-resistant form, suggesting that co-expression facilitates the trafficking of Ost␣ through the Golgi apparatus. Immunolocalization studies showed that co-expression was necessary for plasma membrane expression of both Ost␣ and Ost␤. These results demonstrate that the mouse Ost␣-Ost␤ heteromeric transporter is a basolateral bile acid carrier and may be responsible for bile acid efflux in ileum and other ASBT-expressing tissues.

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[4] Enzymatic deglycosylation of asparagine-linked glycans: Purification, properties, and specificity of oligosaccharide-cleaving enzymes from Flavobacterium meningosepticum

Cited by 270 publications

References 10 publications

IgG glycan hydrolysis by a bacterial enzyme as a therapy against autoimmune conditions

IgG glycan hydrolysis by a bacterial enzyme as a therapy against autoimmune conditions

Analysis of protein glycosylation by mass spectrometry

The Heteromeric Organic Solute Transporter α-β, Ostα-Ostβ, Is an Ileal Basolateral Bile Acid Transporter

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