Serum IgG and IgD and levels in some infectious and noninfectious diseases

I, Rostenberg; Peñaloza, Rosenda

doi:10.1016/0009-8981(78)90310-8

Cited by 25 publications

(17 citation statements)

References 3 publications

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“…Chronic infections were also considered to raise the concentrations of serum IgD (136); indeed, serum IgD was increased in patients with leprosy (144), tuberculosis (20,74), salmonellosis, infectious hepatitis (133), and malaria (29). In a 7-yearold child with a history of recurrent infections, a high level of IgD was noted in serum (125).…”

Section: Serum Igd In Various Diseases and Conditionsmentioning

confidence: 99%

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Immunoglobulin D: Properties, Measurement, and Clinical Relevance

Vladutiu

2000

Clin Diagn Lab Immunol

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Section: Serum Igd In Various Diseases and Conditionsmentioning

confidence: 99%

“…Serum IgD was increased in patients with autoimmune diseases who also had increased IgG, IgA, and IgM (83,87,116,133,141). High values of serum IgD were found in some, but not all, adults with rheumatoid arthritis (136) and in children with juvenile rheumatoid arthritis (51).…”

Section: Immunodeficienciesmentioning

confidence: 99%

Immunoglobulin D: Properties, Measurement, and Clinical Relevance

Vladutiu

2000

Clin Diagn Lab Immunol

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“…In the late 1970’s Rostenberg et al . 2 were the first to link aberrant protein glycosylation patterns to cancer. Later Gehrke and coworkers 3 implicated changes in glycan abundance in epithelial ovarian cancer (EOC) by gas-liquid chromatography (GLC).…”

Section: Introductionmentioning

confidence: 99%

Development of a nanoLC LTQ Orbitrap Mass Spectrometric Method for Profiling Glycans Derived from Plasma from Healthy, Benign Tumor Control, and Epithelial Ovarian Cancer Patients

2008

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We report the development of split-less nano-flow liquid chromatography mass spectrometric analysis of glycans chemically cleaved from glycoproteins in plasma. Porous graphitized carbon operating under reverse-phase conditions and an amide-based stationary phase operating under hydrophilic interaction conditions are quantitatively compared for glycan separation. Both stationary phases demonstrated similar column efficiencies and excellent retention time reproducibility without an internal standard to correct for retention time shift. The 95% confidence intervals of the mean retention times were ±4 seconds across 5 days of analysis for both stationary phases; however, the amide stationary phase was observed to be more robust. The high mass measurement accuracy of less than 2 ppm and fragmentation spectra provided highly confident identifications along with structural information. In addition, data are compared amongst samples derived from 10 healthy controls, 10 controls with a differential diagnosis of benign gynecologic tumors, and 10 diseased epithelial ovarian cancer patients (EOC). Two fucosylated glycans were found to be up-regulated in healthy controls and provided an accurate diagnostic value with an area under the receiver operator characteristic curve of 0.87. However, these same glycans provided a significantly less diagnostic value when used to differentiate EOC from benign tumor control samples with an area under the curve of 0.73.

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“…4 Furthermore, aberrant glycosylation was first linked to cancer in 1978 where aberrant glycosylation patterns of α 1 -antitrypsin were discovered in lung, prostate, and gastrointestinal cancers. 5 Since then, numerous studies have provided evidence for the correlation between aberrant glycosylation and cancer, 6–11 and now, researchers believe that glycans may be possible candidates for sensitive and specific disease biomarkers. 12 Recent studies have supported these earlier findings demonstrating aberrant glycosylation in many different types of cancers, 13 including breast, 14–16 prostate, 17–18 liver, 19 ovarian, 20–24 pancreatic, 25 etc.…”

Section: Introductionmentioning

confidence: 99%

Stable-Isotope Labeled Hydrophobic Hydrazide Reagents for the Relative Quantification of N-Linked Glycans by Electrospray Ionization Mass Spectrometry

et al. 2011

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This study presents the development of stable-isotope labeled hydrophobic, hydrazide reagents for the relative quantification of N-linked glycans. The P2GPN ‘light’ (12C) and ‘heavy’ (13C6) pair are used to differentially label two N-linked glycan samples. The samples are combined 1:1, separated using HILIC, and then mass differentiated and quantified using mass spectrometry. These reagents have several benefits: 1) impart hydrophobic character to the glycans affording an increase in electrospray ionization efficiency and MS detection; 2) indistinguishable chromatographic, MS, and MS/MS performance of the ‘light’ and ‘heavy’ reagents affording relative quantification; and 3) analytical variability is significantly reduced due to the two samples being mixed together after sample preparation. Obtaining these analytical benefits only requires ~4 hours of sample preparation time. It is shown that these reagents are capable of quantifying changes in glycosylation in simple mixtures, and the analytical variability of the reagents in pooled plasma samples is shown to be less than ±30%. Additionally, the incorporation of an internal standard allows one to account for the difference in systematic error between the two samples due to the samples being processed in parallel and not mixed until after derivatization.

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Serum IgG and IgD and levels in some infectious and noninfectious diseases

Cited by 25 publications

References 3 publications

Immunoglobulin D: Properties, Measurement, and Clinical Relevance

Immunoglobulin D: Properties, Measurement, and Clinical Relevance

Development of a nanoLC LTQ Orbitrap Mass Spectrometric Method for Profiling Glycans Derived from Plasma from Healthy, Benign Tumor Control, and Epithelial Ovarian Cancer Patients

Stable-Isotope Labeled Hydrophobic Hydrazide Reagents for the Relative Quantification of N-Linked Glycans by Electrospray Ionization Mass Spectrometry

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