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41 papers found.
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Improved and semi-automated reductive β-elimination workflow for higher throughput protein O-glycosylation analysis

: Maximilianos Kotsias, Radoslaw P. Kozak, Richard A. Gardner. Data curation: Maximilianos Kotsias. Formal analysis: Maximilianos Kotsias. Funding acquisition: Manfred Wuhrer, Daniel I. R. Spencer ... . Spencer. 12 / 14 Resources: Radoslaw P. Kozak, Daniel I. R. Spencer. Software: Maximilianos Kotsias, Richard A. Gardner. Supervision: Radoslaw P. Kozak, Richard A. Gardner, Manfred Wuhrer, Daniel I. R

Serum sialylation changes in cancer

Cancer is a major cause of death in both developing and developed countries. Early detection and efficient therapy can greatly enhance survival. Aberrant glycosylation has been recognized to be one of the hallmarks of cancer as glycans participate in many cancer-associated events. Cancer-associated glycosylation changes often involve sialic acids which play important roles in...

HappyTools: A software for high-throughput HPLC data processing and quantitation

: Albert Bondt, Manfred Wuhrer, Daniel Ian Richard Spencer. 12 / 14 Validation: Bas Cornelis Jansen, Lise Hafkenscheid, Albert Bondt, Richard Andrew Gardner, Jenifer Lynn Hendel. Writing ± original draft ... : Bas Cornelis Jansen, Lise Hafkenscheid, Albert Bondt, Richard Andrew Gardner, Jenifer Lynn Hendel, Manfred Wuhrer, Daniel Ian Richard Spencer. Writing ± review & editing: Bas Cornelis Jansen, Albert

The glycomic effect of N-acetylglucosaminyltransferase III overexpression in metastatic melanoma cells. GnT-III modifies highly branched N-glycans

N-acetylglucosaminyltransferase III (GnT-III) is known to catalyze N-glycan “bisection” and thereby modulate the formation of highly branched complex structures within the Golgi apparatus. While active, it inhibits the action of other GlcNAc transferases such as GnT-IV and GnT-V. Moreover, GnT-III is considered as an inhibitor of the metastatic potential of cancer cells both in...

Reversed-phase separation methods for glycan analysis

Reversed-phase chromatography is a method that is often used for glycan separation. For this, glycans are often derivatized with a hydrophobic tag to achieve retention on hydrophobic stationary phases. The separation and elution order of glycans in reversed-phase chromatography is highly dependent on the hydrophobicity of the tag and the contribution of the glycan itself to the...

Fab glycosylation of immunoglobulin G does not associate with improvement of rheumatoid arthritis during pregnancy

Background Changes in immunoglobulin G (IgG) constant domain (Fc) glycosylation are associated with changes in rheumatoid arthritis (RA) disease activity in response to pregnancy. Here, we sought to determine whether the same holds true for variable domain (Fab) glycosylation. Methods IgGs were captured from RA and control sera obtained before (RA only), during and after...

Subclass-specific IgG glycosylation is associated with markers of inflammation and metabolic health

• PubMed • Google Scholar Search for Marian Beekman in:Nature Research journals • PubMed • Google Scholar Search for Manfred Wuhrer in:Nature Research journals • PubMed • Google Scholar Contributions The ... that they have no competing interests. Corresponding author Correspondence to Manfred Wuhrer. Electronic supplementary material Supplemental DataSupplemental Table S1Supplemental Table S3 Rights

Patients with IgG1-anti-red blood cell autoantibodies show aberrant Fc-glycosylation

Autoimmune hemolytic anemia (AIHA) is a potentially severe disease in which red blood cells (RBC) are destroyed by IgG anti-RBC autoantibodies which can lead to hemolysis. We recently found IgG Fc-glycosylation towards platelet and RBC alloantigens to be skewed towards decreased fucosylation, increased galactosylation and sialylation. The lowered core-fucosylation increases the...

Clinical Glycomics Employing Graphitized Carbon Liquid Chromatography–Mass Spectrometry

structures and glycan features. Consequently, this strategy is a very powerful Published in the topical collection Recent Developments in Clinical Omics with guest editors Martin Giera and Manfred Wuhrer

Multi-level glyco-engineering techniques to generate IgG with defined Fc-glycans

Theo Rispens 4 Manfred Wuhrer 1 Gestur Vidarsson 0 0 Sanquin Research, Department Experimental Immunohematology , Amsterdam , The Netherlands, and Landsteiner Laboratory , Academic Medical Centre

Human plasma protein N-glycosylation

Glycosylation is the most abundant and complex protein modification, and can have a profound structural and functional effect on the conjugate. The oligosaccharide fraction is recognized to be involved in multiple biological processes, and to affect proteins physical properties, and has consequentially been labeled a critical quality attribute of biopharmaceuticals. Additionally...

Variation of Human Salivary O-Glycome

The study of saliva O-glycosylation is receiving increasing attention due to the potential of glycans for disease biomarkers, but also due to easy access and non-invasive collection of saliva as biological fluid. Saliva is rich in glycoproteins which are secreted from the bloodstream or produced by salivary glands. Mucins, which are highly O-glycosylated proteins, are...

Glycomics using mass spectrometry

Manfred Wuhrer 0 ) Department of Parasitology, Biomolecular Mass Spectrometry Unit, Leiden University Medical Center , Albinusdreef 2, 2333ZA Leiden, The Netherlands Mass spectrometry plays an

Comparison of Fc N-Glycosylation of Pharmaceutical Products of Intravenous Immunoglobulin G

Intravenous immunoglobulin (IVIg) products from different pharmaceutical companies vary in composition, in part because of the selected blood donors and production process. N-glycosylation of the Fc-portion of IgG varies between blood donors and may influence both the side-effects and therapeutic effectiveness of IVIg. At present, the variation in Fc N-glycosylation between IVIg...

Pro-inflammatory pattern of IgG1 Fc glycosylation in multiple sclerosis cerebrospinal fluid

Background Immunoglobulin G (IgG) effector functions are regulated by the composition of glycans attached to a conserved N-glycosylation site in the Fc part. Intrathecal production of IgG, especially IgG1, is a hallmark of multiple sclerosis (MS), but nothing is known about IgG Fc glycosylation in MS and in cerebrospinal fluid (CSF) in general. Methods We applied mass...

The Art of Destruction: Optimizing Collision Energies in Quadrupole-Time of Flight (Q-TOF) Instruments for Glycopeptide-Based Glycoproteomics

In-depth site-specific investigations of protein glycosylation are the basis for understanding the biological function of glycoproteins. Mass spectrometry-based N- and O-glycopeptide analyses enable determination of the glycosylation site, site occupancy, as well as glycan varieties present on a particular site. However, the depth of information is highly dependent on the applied...

Pro-inflammatory pattern of IgG1 Fc glycosylation in multiple sclerosis cerebrospinal fluid

Immunoglobulin G (IgG) effector functions are regulated by the composition of glycans attached to a conserved N-glycosylation site in the Fc part. Intrathecal production of IgG, especially IgG1, is a hallmark of multiple sclerosis (MS), but nothing is known about IgG Fc glycosylation in MS and in cerebrospinal fluid (CSF) in general. We applied mass spectrometry of tryptic Fc...

Acute phase inflammation is characterized by rapid changes in plasma/peritoneal fluid N-glycosylation in mice

Murine zymosan-induced peritonitis is a widely used model for studying the molecular and cellular events responsible for the initiation, persistence and/or resolution of inflammation. Among these events, it is becoming increasingly evident that changes in glycosylation of proteins, especially in the plasma and at the site of inflammation, play an important role in the...