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Anti-α 1(IV) Collagen Autoantibodies Associated with Lung Adenocarcinoma Presenting as the Goodpasture Syndrome

Raghu Kalluri, PhD; Savas Petrides, MD; Curtis B. Wilson, MD; John E. Tomaszewski, MD; Harold I. Palevsky, MD; Michael A. Grippi, MD; Michael P. Madaio, MD; and Eric G. Neilson, MD
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From the University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania; and The Scripps Research Institute, La Jolla, California. Acknowledgments: The authors thank Marilyn Salcheider for technical assistance; Michael Rosen, MD, for referring the patient to the Hospital of University of Pennsylvania; and Dr. Billy G. Hudson for providing the Goodpasture antibodies. Grant Support: In part by National Institutes of Health grants DK-07006, DK-30280, DK-45191, and DK-20043 and the DCI RED fund. Requests for Reprints: Eric G. Neilson, MD, 700 Clinical Research Building, Penn Center for Molecular Studies of Kidney Diseases, Renal Electrolyte and Hypertension Division, University of Pennsylvania, 422 Curie Boulevard, Philadelphia, PA 19104-6144. Current Author Addresses: Drs. Kalluri, Petrides, Madaio, and Neilson: 700 Clinical Research Building, Renal Electrolyte and Hypertension Division, Department of Medicine, University of Pennsylvania, 422 Curie Boulevard, Philadelphia, PA 19104-6144. Dr. Wilson: Department of Immunology, The Scripps Research Institute, 10666 North Torrey Pines Road, La Jolla, CA 92037. Dr. Tomaszewski: Department of Pathology and Laboratory Medicine, Hospital of the University of Pennsylvania, Philadelphia, PA 19104.


Copyright ©2004 by the American College of Physicians


Ann Intern Med. 1996;124(7):651-653. doi:10.7326/0003-4819-124-7-199604010-00005
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We report a case of adenocarcinoma of the lung with hemoptysis that was mistaken for the Goodpasture syndrome on the basis of a serologic test for antiglomerular basement membrane antibodies. Antiglomerular basement membrane antibodies are characteristic of the Goodpasture syndrome, some forms of rapidly progressive glomerulonephritis, and isolated instances of pulmonary hemorrhage. Antiglomerular basement membrane antibodies from patients with traditional Goodpasture syndrome react with the α 3(IV) chain, one of the six known chains of type IV collagen that form an integrative lattice called basement membrane [12]. Evaluation of the antiglomerular basement membrane antibodies in our patient showed the presence of anti-α 1(IV) rather than anti-α 3(IV) reactivity.

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Figure 1.
Identification of the type IV collagen chains that bind to the patient's (AG) autoantibodies. Top.Middle.Bottom.

Enzyme-linked immunosorbent assay (ELISA) with bovine antigens. The results show that AG's antibody binds to the α 1(IV) noncollagenous domain 1 (NC1) domain with minimal binding to the α 3(IV) NC1 domain. The antibody of the patient with the Goodpasture syndrome (LL) shows specific binding to the α 3(IV) NC1 domain and minimal binding to the α 1(IV) NC1 domain. The control antibodies show no specific binding to type IV collagen. The dimers represent the α 3(IV) NC1 domain in dimeric form. Results of ELISA with recombinant human type IV collagen NC1 domains. AG's antibody binds strongly to the recombinant α 1(IV) NC1 domain and binds much more weakly to the α 3(IV) NC1 and α 6(IV) NC1 domains. The Goodpasture antibodies (LL) bind predominantly to the α 3(IV) NC1 domain. The control antibodies do not specifically bind to any of the recombinants. Immunoblot analysis of the antibodies from AG and LL using the recombinant human type IV collagen NC1 domains. AG's antibody binds predominantly to the α 1(IV) NC1 domain, and LL's antibodies bind predominantly to the α 3(IV) NC1 domain. The dilution of the antibodies used in all assays was 1:200. The 405-nm absorbance values shown in the graphs are each a mean of two separate readings.

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Figure 2.
Tissue immunohistochemistry.Left.Middle.Right.

Lung biopsy specimen. Binding of the patient (AG) antibodies to the glomerular basement membrane and mesangial matrix of the normal human kidney section. Binding of the Goodpasture (LL) antibodies to the glomerular basement membrane of the normal human kidney section predominantly in a linear fashion. The control serum specimen did not show any binding (data not shown). The dilution of the antibodies used was 1:50. The control serum specimen did not bind to any of the recombinant or bovine noncollagenous domain 1 domains.

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