Search results for "Goodpasture"

Structures of collagen IV globular domains: insight into associated pathologies, folding and network assembly

2018

15 páginas, 6 figuras, 1 tabla.

IgG Subclass Distribution of Autoantibodies to Glomerular Basement Membrane in Goodpasture’s Syndrome Compared to Other Autoantibodies

1988

The IgG subclass distribution of autoantibodies to glomerular basement membrane (anti-GBM antibodies) was investigated and compared to the distribution of liver-kidney microsomal (LKM) autoantibodies in chronic active hepatitis, to antimitochondrial autoantibodies (AMA) in primary biliary cirrhosis, and to the subclass distribution of total serum IgG within a healthy population. Solid phase assays for the demonstration of these autoantibodies were performed with four mouse monoclonal antibodies specific for each human subclass to provide quantitative data for the autoantibodies. In addition, the subclass distribution of total IgG in these sera was analyzed. IgG1 accounted for 75% of the tot…

Goodpasture's Syndrome

1998

Precise mapping of the Goodpasture epitope(s) using phage display, site-directed mutagenesis, and surface plasmon resonance.

2013

Goodpasture disease is an autoimmune disorder mediated by circulating autoantibodies against the noncollagenous-1 (NC1) domain of the alpha 3 chain of type IV collagen (alpha 3(IV)NC1). The structure of Goodpasture epitope(s) has been previously mapped into two main binding regions (E-A and E-B) of the alpha 3(IV)NC1 domain using a residue mutation approach on the highly related alpha 1(IV)NC1 domain. Here we combined phage display and surface plasmon resonance technology to more precisely localize the pathogenic binding sites. Peptides mimicking the Goodpasture epitope(s) were used to identify residues involved in autoantibody binding and found involvement of eight residues previously unre…

Characterization and Expression of Multiple Alternatively Spliced Transcripts of the Goodpasture Antigen Gene Region. Goodpasture Antibodies Recogniz…

1995

Collagen IV, the major component of basement membranes, is composed of six distinct alpha chains (alpha 1-alpha 6). Atypically among the collagen IV genes, the exons encoding the carboxyl-terminal region of the human alpha 3(IV) chain undergo alternative splicing. This region has been designated as the Goodpasture antigen because of its reactivity in the kidney and lung with the pathogenic autoantibodies causing Goodpasture syndrome. The data presented in this report demonstrate that, in human kidney, the gene region encompassing the Goodpasture antigen generates at least six alternatively spliced transcripts predicting five distinct proteins that differ in their carboxyl-terminus and retai…

Structures of collagen IV globular domains: insight into associated pathologies, folding and network assembly. Corrigendum

2020

The article by Casino et al. [IUCrJ (2018). 5, 765–779] is corrected.

Increased Goodpasture antigen-binding protein expression induces type IV collagen disorganization and deposit of immunoglobulin A in glomerular basem…

2007

Increased expression of Goodpasture antigen-binding protein (GPBP), a protein that binds and phosphorylates basement membrane collagen, has been associated with immune complex-mediated pathogenesis. However, recent reports have questioned this biological function and proposed that GPBP serves as a cytosolic ceramide transporter (CERTL). Thus, the role of GPBP in vivo remains unknown. New Zealand White (NZW) mice are considered healthy animals although they convey a genetic predisposition for immune complex-mediated glomerulonephritis. Here we show that NZW mice developed age-dependent lupus-prone autoimmune response and immune complex-mediated glomerulonephritis characterized by elevated GP…

Absence of Anti-Glomerular Basement Membrane Antibodies in 200 Patients With Systemic Lupus Erythematosus With or Without Lupus Nephritis: Results of…

2020

IntroductionAnti-glomerular basement membrane (GBM) antibodies are pathogenic antibodies first detected in renal-limited anti-GBM disease and in Goodpasture disease, the latter characterized by rapidly progressive crescentic glomerulonephritis combined with intra-alveolar hemorrhage. Studies have suggested that anti-GBM antibody positivity may be of interest in lupus nephritis (LN). Moreover, severe anti-GBM vasculitis cases in patients with systemic lupus erythematosus (SLE) have been described in the literature, but few studies have assessed the incidence of anti-GBM antibodies in SLE patients.ObjectiveThe main study objective was to determine if positive anti-GBM antibodies were present …

Dot-immunobinding assay with the globular domain of collagen type IV for antiglomerular basement membrane antibodies

1988

A dot-immunobinding assay for the detection of antiglomerular basement membrane antibodies has been developed. The globular domain NC1 of basement membrane collagen type IV was used as antigen. The assay proved to be specific, sensitive, and reproducible. Circulating antibodies in each of 12 sera from patients with florid Goodpasture's syndrome could be demonstrated, whereas sera from patients with Goodpasture's syndrome in clinical remission and various control sera showed no reactivity. The advantages of the dot-blot assay are: the usage of the purified Goodpasature target antigen NCI reduces unspecific binding of IgG; only minimal amounts of antigen are required to give a positive signal…

Hacia la caracterización del epítopo del autoantígeno en el Síndrome de Goodpasture

2014

El síndrome de Goodpasture (GP) es un desorden autoinmune que cursa con glomerulonefritis rápidamente progresiva y hemorragia pulmonar. El ataque inmunológico se lleva a cabo mediante (auto)-anticuerpos (anticuerpos GP) dirigidos contra el dominio C terminal, no colagenoso (NC1), de la cadena α3 del colágeno IV, presente en la membrana basal glomerular (GBM), así como en la membrana basal alveolar. Tres cadenas α se asocian para construir una molécula de colágeno IV, que recibe el nombre de protómero, dos protómeros de colágeno IV se unen a través de sus extremos NC1 para formar una estructura cuaternaria de naturaleza hexamérica (hexámero) en la red de colágeno IV. Estudios cristalográfico…