Analysis of immunoglobulins by two-dimensional gel electrophoresis

Tissot, Jean‐Daniel; Spertini, François

doi:10.1016/0021-9673(94)00844-y

Cited by 33 publications

(26 citation statements)

References 188 publications

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“…This limitation was deliberately taken into account in this pilot study in order to unequivocally uncover the oligoclonality of the enriched mono-specific antibody pools in each patient as an epitope-independent process. Interpreting the spot pattern of the purified antibody pools in 2D gels as being caused by their oligoclonal nature stands in agreement with previous reports where antibody spot pattern have been introduced as a measure for underlying clonality [44][45][46]. Nevertheless, post-translational and artefact protein modifications have to be considered as a source for spot heterogeneities in 2D gels to some extent.…”

Section: Discussionsupporting

confidence: 75%

Clonality characterization of natural epitope-specific antibodies against the tumor-related antigen topoisomerase IIa by peptide chip and proteome analysis: a pilot study with colorectal carcinoma patient samples

et al. 2012

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Patient-specific sequential epitopes were identified by peptide chip analysis using 15mer peptides immobilized on glass slides that covered the topoisomerase IIa protein with a frameshift of five amino acids. Binding specificities of serum antibodies against sequential epitopes were confirmed as being mono-specific by peptide chip re-analysis of epitope-affinity-purified antibody pools. These results demonstrate that serum samples from colon carcinoma patients contain antibodies against sequential epitopes from the topoisomerase IIa antigen. Interactions of patients' antibodies with sequential epitopes displayed by peptides on glass surfaces may thus mirror disease-specific immune situations. Consequently, these data suggest epitope-antibody reactivities on peptide chips as potential diagnostic readouts of individual immune response characteristics, especially because monospecific antibodies can be interrogated. Subsequently, the clonality of the antibodies present in the mono-specific antibody pools was characterized by 2D gel electrophoresis. This analysis suggested that the affinity-purified antibodies were oligoclonal. Similarly to large-scale screening approaches for specific antigen-antibody interactions in order to improve disease diagnostic, we suggest that "protein-wide" screening for specific epitope-paratope interactions may help to develop novel assays for monitoring of personalized therapies, since individual properties of antigen-antibody interactions remain distinguishable.

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Section: Discussionsupporting

confidence: 75%

Clonality characterization of natural epitope-specific antibodies against the tumor-related antigen topoisomerase IIa by peptide chip and proteome analysis: a pilot study with colorectal carcinoma patient samples

et al. 2012

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“…As proposed by Radl et al [70] oligoclonal gammopathies should be considered to form a separate category of immunoglobulinopathies. Our own experience with the study of Ig production in healthy humans, in patients [31,[71][72][73][74][75][76][77], and in animal models [78][79][80][81] confirms that oligoclonal gammopathies and MG usually result from different pathophysiolological processes. MG is most frequently observed in patients or animals with a malignant disease involving a single B-cell clone, whereas oligoclonal gammopathies are often detected in patients without overt B-cell malignancies ( Table 1).…”

Section: Biclonal Triclonal Oligoclonal Gammopathiesmentioning

confidence: 97%

“…The terminology used when multiple clonal Igs are present (biclonal, triclonal, oligoclonal or multiclonal) is imprecise. In 1995, based on a classification by Radl [29,30], we proposed to unify the various terms under the general term of 'immunoglobulinopathy' and we summarized the various clinical situations associated with clonal overproduction of Igs (Table 1) [31].…”

Section: The Immunoglobulinopathiesmentioning

confidence: 99%

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The immunoglobulinopathies: From physiopathology to diagnosis

Tissot

Aubert

et al. 2002

Proteomics

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The diversity of immunoglobulins (Igs) results mainly from recombinations of numerous genes within the heavy (V(Heavy), D, and J(Heavy)) and within the light (V(Light), J(Light)) chain gene loci, and from somatic hypermutations occurring during the immune response of B-cells. Igs production is controlled by complex cellular and humoral mechanisms. Plasma of healthy individuals contains polyclonal Igs. Clonal expansion of cells producing antigen-specific Igs may result from physiological as well as from pathological immune events. Exquisitely sensitive and specific molecular biology techniques have been used to evaluate the clonal diversity of cells producing antigen-specific Ig. However, the application of such techniques is hampered by the necessity to collect the totality of antigen-specific B-cells for subsequent analysis, which is impossible to perform routinely in humans. In addition, these techniques do not provide quantitative information about the concentration of the circulating Igs. It is therefore necessary to use tools allowing study of the quantity of the circulating Igs, and more particularly to detect overproduction of a single homogeneous Ig resulting from the expansion of a B-cell clone secreting Igs. Here, we review the mechanisms of B-cell differentiation and Ig synthesis, discuss the diseases associated with clonal Ig production and review the methods available in the clinical laboratory for Ig analysis.

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“…The interest of 2-DE as well as its limitations in the analysis of monoclonal gammopathy, either in plasma/ serum or urine samples, have been described by different groups [122][123][124][125][126][127][128][129][130][131][132][133][134], and has been useful in difficult cases such as oligoclonal gammapathies, cold agglutinins or cryoglobulins [135].…”

Section: Plasma/serummentioning

confidence: 99%

A better understanding of molecular mechanisms underlying human disease

Bermúdez-Crespo

López

2007

Proteomics Clinical Apps

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This review summarises and discusses the degree to which proteomics is contributing to medical care, providing examples and signspots for future directions. Why do genomic approaches provide a limited view of gene expression? Because of the multifactorial nature of many diseases, proteomics enables us to understand the molecular basis of disease, not only at the organism, whole‐cell or tissue levels, but also in subcellular structures, protein complexes and biological fluids. The application of proteomics in medicine is expected to have a major impact by providing an integrated view of individual disease processes. This review describes several proteomic platforms and examines the role of proteomics as a tool for clinical biomarker discovery, the identification of prognostic and earlier diagnostic markers, their use in monitoring the effects of drug treatments and eventually find more efficient and safer therapeutics for a wide range of pathologies.

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Analysis of immunoglobulins by two-dimensional gel electrophoresis

Cited by 33 publications

References 188 publications

Clonality characterization of natural epitope-specific antibodies against the tumor-related antigen topoisomerase IIa by peptide chip and proteome analysis: a pilot study with colorectal carcinoma patient samples

Clonality characterization of natural epitope-specific antibodies against the tumor-related antigen topoisomerase IIa by peptide chip and proteome analysis: a pilot study with colorectal carcinoma patient samples

The immunoglobulinopathies: From physiopathology to diagnosis

A better understanding of molecular mechanisms underlying human disease

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