PMID- 8160779
OWN - NLM
STAT- MEDLINE
DCOM- 19940516
LR  - 20181113
IS  - 0002-9440 (Print)
IS  - 1525-2191 (Electronic)
IS  - 0002-9440 (Linking)
VI  - 144
IP  - 4
DP  - 1994 Apr
TI  - Antibodies to glycolipids activate complement and promote proteinuria in passive 
      Heymann nephritis.
PG  - 807-19
AB  - Passive Heymann nephritis is an experimental rat model of human membranous 
      nephropathy induced by injection of antisera against crude renal cortical 
      fractions such as Fx1A or rat tubular microvilli. This results in the formation 
      of subepithelial immune deposits, the activation of the C5b-9 membrane attack 
      complex of complement, and severe proteinuria. While the formation of immune 
      deposits is attributed to in situ immune complex formation with antibodies 
      specific for the gp330-Heymann nephritis antigenic complex (HNAC), activation of 
      complement and proteinuria appear to be caused by at least one additional 
      antibody species present in anti-Fx1A sera. We have separated by affinity 
      absorption polyspecific antisera against Fx1A and rat microvilli into one IgG 
      fraction directed specifically against microvillar proteins (anti-Fx1A-prot) and 
      another IgG fraction specific for glycolipids (ant-Fx1A-lip) of tubular 
      microvilli. When injected into rats, the anti-Fx1A-prot fraction induced immune 
      deposits but failed to activate complement or produce proteinuria, similar to 
      results obtained with affinity-purified anti-gp330 IgG. When the antibodies of 
      the anti-Fx1A-lip fraction were injected alone they did not bind to glomeruli. By 
      contrast, when the IgGs specific for the Fx1A-prot fraction (or for gp330-HNAC) 
      were combined with those directed against the Fx1A-lip glycolipid preparation, 
      immune deposits were formed, in situ complement activation was observed, and also 
      proteinuria was induced. It is concluded that within anti-Fx1A and 
      anti-microvillar sera there are at least two IgG fractions of relevance for the 
      development of PHN: one directed against the gp330-HNAC complex which is 
      responsible for the development of immune deposits, and a second specific for 
      glycolipid antigen(s) which activate(s) the complement cascade.
FAU - Susani, M
AU  - Susani M
AD  - Division of Ultrastructural Pathology and Cell Biology, University of Vienna, 
      Austria.
FAU - Schulze, M
AU  - Schulze M
FAU - Exner, M
AU  - Exner M
FAU - Kerjaschki, D
AU  - Kerjaschki D
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Am J Pathol
JT  - The American journal of pathology
JID - 0370502
RN  - 0 (Autoantibodies)
RN  - 0 (Autoantigens)
RN  - 0 (Complement Membrane Attack Complex)
RN  - 0 (Glycolipids)
RN  - 0 (Heymann Nephritis Antigenic Complex)
RN  - 0 (Immunoglobulin G)
RN  - 0 (Membrane Glycoproteins)
SB  - IM
CIN - Am J Pathol. 1994 Apr;144(4):651-8. PMID: 8160766
MH  - Animals
MH  - Autoantibodies/*immunology
MH  - Autoantigens/immunology/isolation & purification
MH  - Complement Activation/*immunology
MH  - Complement Membrane Attack Complex/immunology
MH  - Glomerulonephritis/*immunology/pathology
MH  - Glycolipids/*immunology/isolation & purification
MH  - Heymann Nephritis Antigenic Complex
MH  - Immunoglobulin G/immunology/isolation & purification
MH  - Kidney Glomerulus/immunology
MH  - Male
MH  - Membrane Glycoproteins/immunology/isolation & purification
MH  - Proteinuria/*etiology/pathology
MH  - Rabbits
MH  - Rats
MH  - Rats, Sprague-Dawley
PMC - PMC1887236
EDAT- 1994/04/01 00:00
MHDA- 1994/04/01 00:01
PMCR- 1994/10/01
CRDT- 1994/04/01 00:00
PHST- 1994/04/01 00:00 [pubmed]
PHST- 1994/04/01 00:01 [medline]
PHST- 1994/04/01 00:00 [entrez]
PHST- 1994/10/01 00:00 [pmc-release]
PST - ppublish
SO  - Am J Pathol. 1994 Apr;144(4):807-19.