Development of Enzyme Immunoassays Specific for Keratan Sulphate- and Core-Protein-Epitopes of the Large Aggregating Proteoglycan from Human Articular Cartilage

Fischer, Dagmar‐Christiane; Kolbe-Busch, Susanne; Stöcker, Georg; Hoffmann, Andreas; Haubeck, H.-D.

doi:10.1515/cclm.1994.32.4.285

Cited by 7 publications

(16 citation statements)

References 12 publications

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“…Determination of keratan sulfate concentration in serum was performed using the monoclonal antibody 5-D-4 (Medac) in an antigen-inhibition assay as described previously (Fischer et al, 1994(Fischer et al, , 1996Ku È chle et al, 1999;Cursiefen et al, 2000b).…”

Section: Methodsmentioning

confidence: 99%

Immunohistochemical Classification of Primary and Recurrent Macular Corneal Dystrophy in Germany: Subclassification of Immunophenotype I A Using a Novel Keratan Sulfate Antibody

Cursiefen¹,

Hofmann-Rummelt²,

Schlötzer‐Schrehardt³

et al. 2001

Experimental Eye Research

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Section: Methodsmentioning

confidence: 99%

Immunohistochemical Classification of Primary and Recurrent Macular Corneal Dystrophy in Germany: Subclassification of Immunophenotype I A Using a Novel Keratan Sulfate Antibody

Cursiefen¹,

Hofmann-Rummelt²,

Schlötzer‐Schrehardt³

et al. 2001

Experimental Eye Research

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“…The study of glycoprotein antigens after deglycosylation has also indicated the importance of some carbohydrate determinants in autoimmune diseases [11,[103][104][105][106], and has revealed that carbohydrate determinants can be important in antigens used for diagnostic tests for circulating antibodies in autoimmune [107] and infectious diseases [22]. T-cell recognition of collagen in rheumatoid arthritis is dependent on carbohydrate epitopes, and removal of the hydroxylysine-linked sugars with TFMS indicated that the carbohydrate was necessary for reactivity of the T-cell clones [11,106].…”

Section: Determination Of the Reactivity Of Antibodies With Protein Omentioning

confidence: 99%

“…Removal of keratan sulphate chains with TFMS increased reactivity of T-cells with aggrecan in mice [103] and in rheumatoid arthritis patients [104,105]. An antibody against the core protein of aggrecan was shown to be a useful marker for inflammatory disease, as synovial fluid from patients with degenerative joint diseases had increased proteoglycan fragments that could be detected with this antibody [107]. Tests of serum for antibodies against T. gondii used for diagnosis of toxoplasmosis can be performed using surface antigen I expressed by P. pastoris.…”

Section: Determination Of the Reactivity Of Antibodies With Protein Omentioning

confidence: 99%

Deglycosylation of glycoproteins with trifluoromethanesulphonic acid: elucidation of molecular structure and function

EDGE

2003

Biochemical Journal

114

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The alteration of proteins by post-translational modifications, including phosphorylation, sulphation, processing by proteolysis, lipid attachment and glycosylation, gives rise to a broad range of molecules that can have an identical underlying protein core. An understanding of glycosylation of proteins is important in clarifying the nature of the numerous variants observed and in determining the biological roles of these modifications. Deglycosylation with TFMS (trifluoromethanesulphonic acid) [Edge, Faltynek, Hof, Reichert, and Weber, (1981) Anal. Biochem. 118, 131-137] has been used extensively to remove carbohydrate from glycoproteins, while leaving the protein backbone intact. Glycosylated proteins from animals, plants, fungi and bacteria have been deglycosylated with TFMS, and the most extensively studied types of carbohydrate chains in mammals, the N-linked, O-linked and glycosaminoglycan chains, are all removed by this procedure. The method is based on the finding that linkages between sugars are sensitive to cleavage by TFMS, whereas the peptide bond is stable and is not broken, even with prolonged deglycosylation. The relative susceptibility of individual sugars in glycosidic linkage varies with the substituents at C-2 and the occurrence of amido and acetyl groups, but even the most stable sugars are removed under conditions that are sufficiently mild to prevent scission of peptide bonds. The post-translational modifications of proteins have been shown to be required for diverse biological functions, and selective procedures to remove these modifications play an important role in the elucidation of protein structure and function.

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“…Degradation products of aggrecan can be detected in body fluids, including synovial fluid, where they reflect aggrecan turnover [38,39]. Previous studies show that the proteoglycan aggrecan is a target for autoreactive T cells in RA and ankylosing spondylitis [40-42].…”

Section: Discussionmentioning

confidence: 99%

Novel self-epitopes derived from aggrecan, fibrillin, and matrix metalloproteinase-3 drive distinct autoreactive T-cell responses in juvenile idiopathic arthritis and in health

et al. 2006

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Juvenile idiopathic arthritis (JIA) is a heterogeneous autoimmune disease characterized by chronic joint inflammation. Knowing which antigens drive the autoreactive T-cell response in JIA is crucial for the understanding of disease pathogenesis and additionally may provide targets for antigen-specific immune therapy. In this study, we tested 9 self-peptides derived from joint-related autoantigens for T-cell recognition (T-cell proliferative responses and cytokine production) in 36 JIA patients and 15 healthy controls. Positive T-cell proliferative responses (stimulation index ≥2) to one or more peptides were detected in peripheral blood mononuclear cells (PBMC) of 69% of JIA patients irrespective of major histocompatibility complex (MHC) genotype. The peptides derived from aggrecan, fibrillin, and matrix metalloproteinase (MMP)-3 yielded the highest frequency of T-cell proliferative responses in JIA patients. In both the oligoarticular and polyarticular subtypes of JIA, the aggrecan peptide induced T-cell proliferative responses that were inversely related with disease duration. The fibrillin peptide, to our knowledge, is the first identified autoantigen that is primarily recognized in polyarticular JIA patients. Finally, the epitope derived from MMP-3 elicited immune responses in both subtypes of JIA and in healthy controls. Cytokine production in short-term peptide-specific T-cell lines revealed production of interferon-γ (aggrecan/MMP-3) and interleukin (IL)-17 (aggrecan) and inhibition of IL-10 production (aggrecan). Here, we have identified a triplet of self-epitopes, each with distinct patterns of T-cell recognition in JIA patients. Additional experiments need to be performed to explore their qualities and role in disease pathogenesis in further detail.

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Development of Enzyme Immunoassays Specific for Keratan Sulphate- and Core-Protein-Epitopes of the Large Aggregating Proteoglycan from Human Articular Cartilage

Cited by 7 publications

References 12 publications

Immunohistochemical Classification of Primary and Recurrent Macular Corneal Dystrophy in Germany: Subclassification of Immunophenotype I A Using a Novel Keratan Sulfate Antibody

Immunohistochemical Classification of Primary and Recurrent Macular Corneal Dystrophy in Germany: Subclassification of Immunophenotype I A Using a Novel Keratan Sulfate Antibody

Deglycosylation of glycoproteins with trifluoromethanesulphonic acid: elucidation of molecular structure and function

Novel self-epitopes derived from aggrecan, fibrillin, and matrix metalloproteinase-3 drive distinct autoreactive T-cell responses in juvenile idiopathic arthritis and in health

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