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A single autoantigen in Goodpasture's syndrome identified by a monoclonal antibody to human glomerular basement membrane.
Lab Invest. 1987 Jan; 56(1):23-31.LI

Abstract

A mouse monoclonal antibody (P1) to the autoantigenic component of human glomerular basement membrane (GBM) was used to study the immunochemistry and tissue distribution of the Goodpasture antigen and the specificity of the human autoimmune response in Goodpasture's syndrome (anti-GBM disease). In solid phase assays, monoclonal antibody P1 bound to collagenase-solubilized human GBM (the ligand used in assays for human autoantibody), but not to other biochemically defined components of basement membrane. On Western blotting, P1 bound to the same 6 bands in solubilized GBM (between 26 and 58 kilodaltons with major bands at 26 and 54 kilodaltons) that were recognized by sera from all 42 patients studied with anti-GBM disease. Preincubation with sera from 8/8 patients blocked the subsequent binding of P1 from 83 to 89% on densitometer scanning of the Western blot; and preincubation with P1 blocked the binding of sera from 6/6 patients from 58 to 89%. Indirect immunofluorescence and immunoperoxidase studies revealed that the pattern of binding of P1 was identical to that of antibody eluted from the kidneys of a patient with Goodpasture's syndrome; there was linear binding to GBM, Bowman's capsule, and distal tubular basement membrane. In addition, P1 bound to basement membranes in lung and choroid plexus, and to membranes of the lens capsule, choroid, and retina of the eye and cochlea, but not to other organs studied. It is concluded that there is a single major autoantigenic component of human GBM (the Goodpasture antigen), which is present on fragments of different molecular weight in the collagenase digest. This antigen is distributed throughout well-defined basement membranes known to be involved in both Goodpasture's and Alport's syndromes. Human anti-GBM antibodies bind to the same (or closely related) determinants which are recognized by P1, demonstrating that the autoimmune response in Goodpasture's syndrome is of highly restricted specificity.

Authors

No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

3540450

Citation

Pusey, C D., et al. "A Single Autoantigen in Goodpasture's Syndrome Identified By a Monoclonal Antibody to Human Glomerular Basement Membrane." Laboratory Investigation; a Journal of Technical Methods and Pathology, vol. 56, no. 1, 1987, pp. 23-31.
Pusey CD, Dash A, Kershaw MJ, et al. A single autoantigen in Goodpasture's syndrome identified by a monoclonal antibody to human glomerular basement membrane. Lab Invest. 1987;56(1):23-31.
Pusey, C. D., Dash, A., Kershaw, M. J., Morgan, A., Reilly, A., Rees, A. J., & Lockwood, C. M. (1987). A single autoantigen in Goodpasture's syndrome identified by a monoclonal antibody to human glomerular basement membrane. Laboratory Investigation; a Journal of Technical Methods and Pathology, 56(1), 23-31.
Pusey CD, et al. A Single Autoantigen in Goodpasture's Syndrome Identified By a Monoclonal Antibody to Human Glomerular Basement Membrane. Lab Invest. 1987;56(1):23-31. PubMed PMID: 3540450.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A single autoantigen in Goodpasture's syndrome identified by a monoclonal antibody to human glomerular basement membrane. AU - Pusey,C D, AU - Dash,A, AU - Kershaw,M J, AU - Morgan,A, AU - Reilly,A, AU - Rees,A J, AU - Lockwood,C M, PY - 1987/1/1/pubmed PY - 1987/1/1/medline PY - 1987/1/1/entrez SP - 23 EP - 31 JF - Laboratory investigation; a journal of technical methods and pathology JO - Lab Invest VL - 56 IS - 1 N2 - A mouse monoclonal antibody (P1) to the autoantigenic component of human glomerular basement membrane (GBM) was used to study the immunochemistry and tissue distribution of the Goodpasture antigen and the specificity of the human autoimmune response in Goodpasture's syndrome (anti-GBM disease). In solid phase assays, monoclonal antibody P1 bound to collagenase-solubilized human GBM (the ligand used in assays for human autoantibody), but not to other biochemically defined components of basement membrane. On Western blotting, P1 bound to the same 6 bands in solubilized GBM (between 26 and 58 kilodaltons with major bands at 26 and 54 kilodaltons) that were recognized by sera from all 42 patients studied with anti-GBM disease. Preincubation with sera from 8/8 patients blocked the subsequent binding of P1 from 83 to 89% on densitometer scanning of the Western blot; and preincubation with P1 blocked the binding of sera from 6/6 patients from 58 to 89%. Indirect immunofluorescence and immunoperoxidase studies revealed that the pattern of binding of P1 was identical to that of antibody eluted from the kidneys of a patient with Goodpasture's syndrome; there was linear binding to GBM, Bowman's capsule, and distal tubular basement membrane. In addition, P1 bound to basement membranes in lung and choroid plexus, and to membranes of the lens capsule, choroid, and retina of the eye and cochlea, but not to other organs studied. It is concluded that there is a single major autoantigenic component of human GBM (the Goodpasture antigen), which is present on fragments of different molecular weight in the collagenase digest. This antigen is distributed throughout well-defined basement membranes known to be involved in both Goodpasture's and Alport's syndromes. Human anti-GBM antibodies bind to the same (or closely related) determinants which are recognized by P1, demonstrating that the autoimmune response in Goodpasture's syndrome is of highly restricted specificity. SN - 0023-6837 UR - https://www.unboundmedicine.com/medline/citation/3540450/A_single_autoantigen_in_Goodpasture's_syndrome_identified_by_a_monoclonal_antibody_to_human_glomerular_basement_membrane_ L2 - https://www.lens.org/lens/search/patent/list?q=citation_id:3540450 DB - PRIME DP - Unbound Medicine ER -