Pathogenesis of Goodpasture Syndrome: A Molecular Perspective

Dorin Bogdan Borza; Eric G. Neilson; Billy G. Hudson

doi:10.1053/S0270-9295(03)00131-1

Pathogenesis of Goodpasture Syndrome: A Molecular Perspective

Dorin Bogdan Borza^*, Eric G. Neilson, Billy G. Hudson

^*Corresponding author for this work

Medicine, Nephrology Division

Research output: Contribution to journal › Article › peer-review

48 Scopus citations

Abstract

Goodpasture (GP) syndrome is a form of anti-glomerular basement membrane (GBM) disease, in which autoantibodies bind to α3(IV) collagen in GBM causing rapidly progressive glomerulonephritis and pulmonary hemorrhage. The conformational GP epitopes have been mapped to 2 regions within the noncollagenous (NC1) domain of the α3(IV) chain. Recently, we described the molecular organization of the autoantigen in the native α3α 4α5(IV) collagen network of the GBM. The crystal structure of the NC1 domain has revealed how the GP epitopes are sequestered in the native GBM. Further insight into the pathogenesis of disease has been obtained from better animal models. These advances provide a foundation for the development of new specific therapies.

Original language	English (US)
Pages (from-to)	522-531
Number of pages	10
Journal	Seminars in nephrology
Volume	23
Issue number	6
DOIs	https://doi.org/10.1053/S0270-9295(03)00131-1
State	Published - Nov 2003

ASJC Scopus subject areas

Nephrology

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title = "Pathogenesis of Goodpasture Syndrome: A Molecular Perspective",

abstract = "Goodpasture (GP) syndrome is a form of anti-glomerular basement membrane (GBM) disease, in which autoantibodies bind to α3(IV) collagen in GBM causing rapidly progressive glomerulonephritis and pulmonary hemorrhage. The conformational GP epitopes have been mapped to 2 regions within the noncollagenous (NC1) domain of the α3(IV) chain. Recently, we described the molecular organization of the autoantigen in the native α3α 4α5(IV) collagen network of the GBM. The crystal structure of the NC1 domain has revealed how the GP epitopes are sequestered in the native GBM. Further insight into the pathogenesis of disease has been obtained from better animal models. These advances provide a foundation for the development of new specific therapies.",

author = "Borza, {Dorin Bogdan} and Neilson, {Eric G.} and Hudson, {Billy G.}",

note = "Funding Information: Supported in part by National Institutes of Health grants DK65123 (D.-B.B.), DK18381 and DK53763 (B.G.H.), DK46282 and DK55926 (E.G.N.), and the 2003 Carl Gottschalk Research Scholar Award from the American Society of Nephrology (D.-B.B.). ",

year = "2003",

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doi = "10.1053/S0270-9295(03)00131-1",

language = "English (US)",

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T2 - A Molecular Perspective

AU - Borza, Dorin Bogdan

AU - Neilson, Eric G.

AU - Hudson, Billy G.

N1 - Funding Information: Supported in part by National Institutes of Health grants DK65123 (D.-B.B.), DK18381 and DK53763 (B.G.H.), DK46282 and DK55926 (E.G.N.), and the 2003 Carl Gottschalk Research Scholar Award from the American Society of Nephrology (D.-B.B.).

PY - 2003/11

Y1 - 2003/11

N2 - Goodpasture (GP) syndrome is a form of anti-glomerular basement membrane (GBM) disease, in which autoantibodies bind to α3(IV) collagen in GBM causing rapidly progressive glomerulonephritis and pulmonary hemorrhage. The conformational GP epitopes have been mapped to 2 regions within the noncollagenous (NC1) domain of the α3(IV) chain. Recently, we described the molecular organization of the autoantigen in the native α3α 4α5(IV) collagen network of the GBM. The crystal structure of the NC1 domain has revealed how the GP epitopes are sequestered in the native GBM. Further insight into the pathogenesis of disease has been obtained from better animal models. These advances provide a foundation for the development of new specific therapies.

AB - Goodpasture (GP) syndrome is a form of anti-glomerular basement membrane (GBM) disease, in which autoantibodies bind to α3(IV) collagen in GBM causing rapidly progressive glomerulonephritis and pulmonary hemorrhage. The conformational GP epitopes have been mapped to 2 regions within the noncollagenous (NC1) domain of the α3(IV) chain. Recently, we described the molecular organization of the autoantigen in the native α3α 4α5(IV) collagen network of the GBM. The crystal structure of the NC1 domain has revealed how the GP epitopes are sequestered in the native GBM. Further insight into the pathogenesis of disease has been obtained from better animal models. These advances provide a foundation for the development of new specific therapies.

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JO - Seminars in Nephrology

JF - Seminars in Nephrology

SN - 0270-9295

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Pathogenesis of Goodpasture Syndrome: A Molecular Perspective

Abstract

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