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glycan multiple myeloma

Alessandro Natoni, Matthew S Macauley, Michael E O'Dwyer
Aberrant glycosylation is a hallmark of cancer cells with increased evidence pointing to a role in tumor progression. In particular, aberrant sialylation of glycoproteins and glycolipids has been linked to increased immune cell evasion, drug evasion, drug resistance, tumor invasiveness, and vascular dissemination, leading to metastases. Hypersialylation of cancer cells is largely the result of overexpression of sialyltransferases (STs). Differentially, humans express twenty different STs in a tissue-specific manner, each of which catalyzes the attachment of sialic acids via different glycosidic linkages (α2-3, α2-6, or α2-8) to the underlying glycan chain...
2016: Frontiers in Oncology
Jie Chen, Meng Fang, Yun-Peng Zhao, Chang-Hong Yi, Jun Ji, Cheng Cheng, Meng-Meng Wang, Xing Gu, Quan-Sheng Sun, Xiao-Ling Chen, Chun-Fang Gao
The aim of this study was to evaluate the diagnostic and differential diagnostic power of serum N-glycans for light chain multiple myeloma (LCMM). A total of 167 cases of subjects, including 42 LCMM, 42 IgG myeloma, 41 IgA myeloma, and 42 healthy controls were recruited in this study. DNA sequencer-assisted fluorophore-assisted capillary electrophoresis (DSA-FACE) was applied to determine the quantitive abundance of serum N-glycans. The core fucosylated, bisecting and sialylated modifications were analyzed in serum of LCMM patients (n=20) and healthy controls (n=20) randomly selected from the same cohort by lectin blot...
2015: PloS One
Sujatha Gomathinayagam, Drake Laface, Nga Rewa Houston-Cummings, Ruban Mangadu, Renee Moore, Ishaan Shandil, Nathan Sharkey, Huijuan Li, Terrance A Stadheim, Dongxing Zha
Monoclonal antibody (mAb) therapy has been successfully used for the treatment of B-cell lymphomas and is currently extended for the treatment of multiple myeloma (MM). New developments in MM therapeutics have achieved significant survival gains in patients but the disease still remains incurable. Elotuzumab (HuLuc63), an anti-CS1 monoclonal IgG1 antibody, is believed to induce anti-tumor activity and MM cytotoxicity through antibody dependent cellular cytotoxicity (ADCC) and inhibition of MM cell adhesion to bone marrow stromal cells (BMSCs)...
August 20, 2015: Journal of Biotechnology
Thomas M Moehler, Anja Seckinger, Dirk Hose, Mindaugas Andrulis, Jèrôme Moreaux, Thomas Hielscher, Martina Willhauck-Fleckenstein, Anette Merling, Uta Bertsch, Anna Jauch, Hartmut Goldschmidt, Bernard Klein, Reinhard Schwartz-Albiez
The glycome, i.e. the cellular repertoire of glycan structures, contributes to important functions such as adhesion and intercellular communication. Enzymes regulating cellular glycosylation processes are related to the pathogenesis of cancer including multiple myeloma. Here we analyze the transcriptional differences in the glycome of normal (n = 10) and two cohorts of 332 and 345 malignant plasma-cell samples, association with known multiple myeloma subentities as defined by presence of chromosomal aberrations, potential therapeutic targets, and its prognostic impact...
2013: PloS One
Rosina Plomp, Paul J Hensbergen, Yoann Rombouts, Gerhild Zauner, Irina Dragan, Carolien A M Koeleman, André M Deelder, Manfred Wuhrer
Immunoglobulin E (IgE) is a heterodimeric glycoprotein involved in antiparasitic and allergic immune reactions. IgE glycosylation is known to exhibit significant interindividual variation, and several reports have indicated its relevance in determining IgE activity. Here, we present site-specific glycosylation analysis of IgE from three different sources: IgE from the serum of a hyperimmune donor, from the pooled serum of multiple nondiseased donors, and from the pooled serum of 2 patients with IgE myeloma...
February 7, 2014: Journal of Proteome Research
Han-Wen Huang, Chein-Hung Chen, Chun-Hung Lin, Chi-Huey Wong, Kuo-I Lin
Glycosylation, an important posttranslational modification process, can modulate the structure and function of proteins, but its effect on the properties of plasma cells is largely unknown. In this study, we identified a panel of glycoproteins by click reaction with alkynyl sugar analogs in plasma cells coupled with mass spectrometry analysis. The B-cell maturation antigen (BCMA), an essential membrane protein for maintaining the survival of plasma cells, was identified as a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42...
July 2, 2013: Proceedings of the National Academy of Sciences of the United States of America
Gordan Lauc, Jennifer E Huffman, Maja Pučić, Lina Zgaga, Barbara Adamczyk, Ana Mužinić, Mislav Novokmet, Ozren Polašek, Olga Gornik, Jasminka Krištić, Toma Keser, Veronique Vitart, Blanca Scheijen, Hae-Won Uh, Mariam Molokhia, Alan Leslie Patrick, Paul McKeigue, Ivana Kolčić, Ivan Krešimir Lukić, Olivia Swann, Frank N van Leeuwen, L Renee Ruhaak, Jeanine J Houwing-Duistermaat, P Eline Slagboom, Marian Beekman, Anton J M de Craen, André M Deelder, Qiang Zeng, Wei Wang, Nicholas D Hastie, Ulf Gyllensten, James F Wilson, Manfred Wuhrer, Alan F Wright, Pauline M Rudd, Caroline Hayward, Yurii Aulchenko, Harry Campbell, Igor Rudan
Glycosylation of immunoglobulin G (IgG) influences IgG effector function by modulating binding to Fc receptors. To identify genetic loci associated with IgG glycosylation, we quantitated N-linked IgG glycans using two approaches. After isolating IgG from human plasma, we performed 77 quantitative measurements of N-glycosylation using ultra-performance liquid chromatography (UPLC) in 2,247 individuals from four European discovery populations. In parallel, we measured IgG N-glycans using MALDI-TOF mass spectrometry (MS) in a replication cohort of 1,848 Europeans...
2013: PLoS Genetics
Kazuo Takahashi, Archer D Smith, Knud Poulsen, Mogens Kilian, Bruce A Julian, Jiri Mestecky, Jan Novak, Matthew B Renfrow
IgA is the most abundantly produced antibody and plays an important role in the mucosal immune system. Human IgA is represented by two isotypes, IgA1 and IgA2. The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain. Thr(225), Thr(228), Ser(230), Ser(232) and Thr(236) have been identified as the predominant sites of O-glycan attachment. The range and distribution of O-glycan chains at each site within the context of adjacent sites in this clustered region create a complex heterogeneity of surface epitopes that is incompletely defined...
February 3, 2012: Journal of Proteome Research
Yoshinao Wada, Anne Dell, Stuart M Haslam, Bérangère Tissot, Kévin Canis, Parastoo Azadi, Malin Bäckström, Catherine E Costello, Gunnar C Hansson, Yoshiyuki Hiki, Mayumi Ishihara, Hiromi Ito, Kazuaki Kakehi, Niclas Karlsson, Catherine E Hayes, Koichi Kato, Nana Kawasaki, Kay-Hooi Khoo, Kunihiko Kobayashi, Daniel Kolarich, Akihiro Kondo, Carlito Lebrilla, Miyako Nakano, Hisashi Narimatsu, Jan Novak, Milos V Novotny, Erina Ohno, Nicolle H Packer, Elizabeth Palaima, Matthew B Renfrow, Michiko Tajiri, Kristina A Thomsson, Hirokazu Yagi, Shin-Yi Yu, Naoyuki Taniguchi
The Human Proteome Organisation Human Disease Glycomics/Proteome Initiative recently coordinated a multi-institutional study that evaluated methodologies that are widely used for defining the N-glycan content in glycoproteins. The study convincingly endorsed mass spectrometry as the technique of choice for glycomic profiling in the discovery phase of diagnostic research. The present study reports the extension of the Human Disease Glycomics/Proteome Initiative's activities to an assessment of the methodologies currently used for O-glycan analysis...
April 2010: Molecular & Cellular Proteomics: MCP
Tatsuo Oita, Hirokazu Yagi, Akiko Yamashiro, Kenji Sakizono, Kenichi Nagai, Shinpei Kasakura, Koichi Kato, Noriko Takahashi
Although abnormalities of glycosylation profile in serum IgG have been demonstrated in a variety of inflammatory autoimmune diseases such as rheumatoid arthritis, there are only a few reports describing long term monitoring of N-glycosylation profiles in such patients. Here we report the serial finding of N-glycosylation profiles of IgG-kappa M-protein in a patient with multiple myeloma monitored for two years. In this patient, serum formed a gel precipitation upon exposure to air. The HPLC mapping method demonstrated that IgG M-protein in the patient exhibited a significant decrease in the ratio of fucosyl to afucosyl N-glycans compared with that in a healthy control...
July 2007: Rinsho Byori. the Japanese Journal of Clinical Pathology
Yusuke Mimura, Peter R Ashton, Noriko Takahashi, David J Harvey, Roy Jefferis
A conserved structural feature of human IgG molecules is the presence of an oligosaccharide moiety within the Fc region at Asn297. In addition, 15-20% of normal polyclonal IgG molecules bear N-linked oligosaccharides in the variable (V) regions of the light (L) and/or heavy (H) chains. Electrospray ionization mass spectrometry (ESI-MS) has been applied to the glycan analysis of two IgG1 myeloma proteins (Wid and Cri) after mild reduction and acidification. Heterogeneous ion peaks were observed for both the H and L chains of Wid in contrast to Cri whose L chain peak was homogeneous...
September 30, 2007: Journal of Immunological Methods
Matthew B Renfrow, C Logan Mackay, Michael J Chalmers, Bruce A Julian, Jiri Mestecky, Mogens Kilian, Knud Poulsen, Mark R Emmett, Alan G Marshall, Jan Novak
IgA nephropathy (IgAN) is the most common form of primary glomerulonephritis. In IgAN, IgA1 molecules with incompletely galactosylated O-linked glycans in the hinge region (HR) are present in mesangial immunodeposits and in circulating immune complexes. It is not known whether the galactose deficiency in IgA1 proteins occurs randomly or preferentially at specific sites. We have previously demonstrated the first direct localization of multiple O-glycosylation sites on a single IgA1 myeloma protein by use of activated ion-electron capture dissociation (AI-ECD) Fourier transform ion cyclotron resonance (FT-ICR) tandem mass spectrometry...
November 2007: Analytical and Bioanalytical Chemistry
Ryo Hashimoto, Tosifusa Toda, Hisashi Tsutsumi, Masatsugu Ohta, Mayumi Mori
Spontaneous crystallization of monoclonal immunoglobulins (crystalglobulin) is a rare complication of multiple myeloma. We describe a 64-year-old Japanese man with skin ulcers and renal failure associated with immunoglobulin G kappa multiple myeloma. Crystallized immunoglobulin was detected in his serum at room temperature. Analysis of the patient's crystalglobulin by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and mass spectrometry suggested that the crystallization was due to abnormal glycosylation of the immunoglobulin light chain...
April 2007: International Journal of Hematology
Matthew B Renfrow, Helen J Cooper, Milan Tomana, Rose Kulhavy, Yoshiyuki Hiki, Kazunori Toma, Mark R Emmett, Jiri Mestecky, Alan G Marshall, Jan Novak
In a number of human diseases of chronic inflammatory or autoimmune character, immunoglobulin molecules display aberrant glycosylation patterns of N- or O-linked glycans. In IgA nephropathy, IgA1 molecules with incompletely galactosylated O-linked glycans in the hinge region (HR) are present in mesangial immunodeposits and in circulating immune complexes. It is not known whether the Gal deficiency in IgA1 proteins occurs randomly or preferentially at specific sites. To develop experimental approaches to address this question, the synthetic IgA1 hinge region and hinge region from a naturally Gal-deficient IgA1 myeloma protein have been analyzed by 9...
May 13, 2005: Journal of Biological Chemistry
Shiro Nozawa, Daisuke Aoki, Katsumi Tsukazaki, Nobuyuki Susumu, Motoko Sakayori, Nao Suzuki, Atsushi Suzuki, Rie Wakita, Makio Mukai, Yuko Egami, Kyoko Kojima-Aikawa, Isao Ishida, Frederic Belot, Ole Hindsgaul, Minoru Fukuda, Michiko N Fukuda
PURPOSE: The purpose of this research was to generate a human monoclonal antibody specific to gynecological cancers and to evaluate such an antibody as therapy for gynecological cancers. EXPERIMENTAL DESIGN: Transchromosomal KM mice were immunized with the human uterine endometrial cancer cell line SNG-S. Hybridomas were constructed between spleen cells from KM mice and mouse myeloma cells. Reactivity of the antibody was evaluated by immunohistochemistry of pathological specimens of gynecological cancers...
October 15, 2004: Clinical Cancer Research: An Official Journal of the American Association for Cancer Research
Hiroko Iwasaki, Yan Zhang, Kahori Tachibana, Masanori Gotoh, Norihiro Kikuchi, Yeon-Dae Kwon, Akira Togayachi, Takashi Kudo, Tomomi Kubota, Hisashi Narimatsu
The hinge region of human immunoglobulin A1 (*IgA1) possesses multiple O-glycans, of which synthesis is initiated by the addition of GalNAc to serine or threonine through the activity of UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferases (pp-GalNAc-Ts). We found that six pp-GalNAc-Ts, pp-GalNAc-T1, -T2, -T3, -T4, -T6, and -T9, were expressed in B cells, IgA-bearing B cells, and NCI-H929 IgA myeloma cells. pp-GalNAc-T activities of these six enzymes for a synthetic IgA hinge peptide, which has nine possible O-glycosylation sites, were examined using a reversed phase-high performance liquid chromatography, a matrix-assisted laser desorption ionization time of flight mass spectrometry, and peptide sequencing analysis...
February 21, 2003: Journal of Biological Chemistry
C Fagioli, R Sitia
Quality control in the endoplasmic reticulum must discriminate nascent proteins in their folding process from terminally unfolded molecules, selectively degrading the latter. Unassembled Ig-mu and J chains, two glycoproteins with five N-linked glycans and one N-linked glycan, respectively, are degraded by cytosolic proteasomes after a lag from synthesis, during which glycan trimming occurs. Inhibitors of mannosidase I (kifunensine), but not of mannosidase II (swainsonine), prevent the degradation of mu chains...
April 20, 2001: Journal of Biological Chemistry
D Smilovich, N Malagolini, C Fagioli, C de Lalla, R Sitia, F Serafini-Cessi
IgM are glycoproteins secreted by plasma cells as (mu2L2)5+J or (mu2L2)6 polymers. In most species, mu- and J-chains bear five and one N -glycans, respectively. Here we compare the terminal glycosylation patterns of 4-hydroxy-3-nitrophenylacetyl (NP)-specific IgM secreted by transfectants of the J558L mouse myeloma deficient in the alpha2,6 sialyltransferase [alpha2,6ST(N)] or by a hybridoma expressing this enzyme (B1.8 cells). The absence of alpha2,6-sialylation results in an increased addition of alpha1, 3-galactosyl residues to mu- and J-chain N-glycans...
August 1998: Glycobiology
A Pereira, R Mazzara, L Escoda, I Alcorta, B Nomdedeu, D Roelcke
The case of a patient (Col) with multiple myeloma presenting as chronic cold agglutinin (CA) syndrome is reported. The CA (Col) was a monoclonal IgA/k paraprotein which recognizes an antigen fully expressed in adult and newborn erythrocytes, sialidase sensitive and partially resistant to proteases. Hemagglutination-inhibition studies showed that immunodominant N-acetylneuraminic acid bound alpha 2-->3 to O-glycans of glycophorins represents the CA(Col) epitope. These serological and biochemical findings fit with the anti-Sa specificity, of which only two previous examples are known...
June 1993: Annals of Hematology
E B Nikolova, M Tomana, M W Russell
Polyclonal human secretory IgA1 and IgA2 antibodies to a bacterial protein antigen Streptococcus mutans AgI/II, and polyclonal human serum IgA1 and IgA2 antibodies to staphylococcal alpha-toxin, were found to interfere with antigen-mediated C3b fixation. In fluid phase, immune complexes of antigen and IgA failed to fix C3b, whereas antigen-IgG complexes did fix C3b. Partial removal of glycan chains with Streptococcus mitis SK96 glycosidases diminished the capacity of IgA antibodies to interfere with antigen-mediated C3b fixation by the alternative complement pathway...
March 1994: Scandinavian Journal of Immunology
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