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Article ; Online: Impact of left atrial appendage morphology on thrombus formation after successful left atrial appendage occlusion: Assessment with cardiac-computed-tomography.

Dieker, Wulf / Behnes, Michael / Fastner, Christian / Sartorius, Benjamin / Wenke, Annika / Sing-Gill, Ishar / El-Battrawy, Ibrahim / Kuschyk, Jürgen / Papavassiliu, Theano / Hoffmann, Ursula / Mashayekhi, Kambis / Schoenberg, Stefan O / Borggrefe, Martin / Henzler, Thomas / Akin, Ibrahim

Scientific reports

2018 Volume 8, Issue 1, Page(s) 1670

Abstract: A standardized imaging algorithm by cardiac computed tomography angiography (cCTA) (LOVE-view) was used in 30 patients to evaluate the influence of different left atrial appendage (LAA) morphologies on development of thrombosis in the LAA 6 months after ... ...

Abstract	A standardized imaging algorithm by cardiac computed tomography angiography (cCTA) (LOVE-view) was used in 30 patients to evaluate the influence of different left atrial appendage (LAA) morphologies on development of thrombosis in the LAA 6 months after implantation of an occlusion device (Watchman or Amplatzer-Cardiac-Plug) in patients with non-valvular atrial fibrillation, CHA
MeSH term(s)	Aged ; Aged, 80 and over ; Animals ; Atrial Appendage/anatomy & histology ; Atrial Appendage/diagnostic imaging ; Atrial Fibrillation/surgery ; Female ; Humans ; Male ; Postoperative Complications/epidemiology ; Prostheses and Implants/adverse effects ; Thrombosis/epidemiology ; Tomography, X-Ray Computed
Language	English
Publishing date	2018-01-26
Publishing country	England
Document type	Journal Article
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-018-19385-z
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Deranged removal of apoptotic cells: its role in the genesis of lupus.

Dieker, Jürgen W C / van der Vlag, Johan / Berden, Jo H M

Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association

2003 Volume 19, Issue 2, Page(s) 282–285

MeSH term(s)	Animals ; Apoptosis/immunology ; Apoptosis/physiology ; Autoantibodies/immunology ; Autoantibodies/physiology ; Cell Survival ; Female ; Humans ; Lupus Nephritis/immunology ; Lupus Nephritis/pathology ; Lupus Nephritis/physiopathology ; Male ; Mice ; Phagocytosis/immunology ; Phagocytosis/physiology ; Prognosis ; Risk Assessment
Chemical Substances	Autoantibodies
Language	English
Publishing date	2003-07-11
Publishing country	England
Document type	Comparative Study ; Editorial ; Research Support, Non-U.S. Gov't
ZDB-ID	90594-x
ISSN	1460-2385 ; 0931-0509
ISSN (online)	1460-2385
ISSN	0931-0509
DOI	10.1093/ndt/gfg485
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Zs.A 2198: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 329: Show issues

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Article ; Online: Lupus-derived monoclonal autoantibodies against apoptotic chromatin recognize acetylated conformational epitopes.

van Bavel, Casandra C / Dieker, Jürgen W / Tamboer, Wim P / van der Vlag, Johan / Berden, Jo H

Molecular immunology

2010 Volume 48, Issue 1-3, Page(s) 248–256

Abstract: Objective: Nuclear components targeted by autoantibodies are a characteristic feature of the autoimmune disease systemic lupus erythematosus (SLE). The nucleosome, a major autoantigen, is released in patients with SLE as a result of a disturbed ... ...

Abstract	Objective: Nuclear components targeted by autoantibodies are a characteristic feature of the autoimmune disease systemic lupus erythematosus (SLE). The nucleosome, a major autoantigen, is released in patients with SLE as a result of a disturbed apoptosis and/or an insufficient clearance of apoptotic debris. During apoptosis the nucleosome is modified, thereby creating more immunogenic epitopes. Subsequently, epitope spreading will lead to the formation of autoantibodies against unmodified chromatin components. However, characterization of B cell epitopes specific for apoptotic chromatin modifications is hampered by the fact that the existing monoclonal antibodies (mAbs) were originally selected on non-apoptotic chromatin. Here, we describe a novel approach for generating mAbs from lupus mice that are specific for apoptosis-induced chromatin modifications. Methods: Hybridomas were generated from pre-diseased and diseased lupus mice using standard fusion methods. Selection occurred on isolated apoptotic chromatin. Antibodies were further characterized by ELISA, western blot and immunofluorescence staining with apoptotic and non-apoptotic chromatin/cells. In addition, reactivity was determined with subnucleosomal complexes and with nucleosomes treated with trypsin or DNase I. Finally, reactivity was determined with cells treated with the histone deacetylase inhibitor TSA. Results: Most generated mAbs appeared to be nucleosome specific with a clear preference for apoptotic nucleosomes compared to normal nucleosomes. Although the exact elucidation of the epitopes of these mAbs specific for apoptosis-associated nucleosome modifications remains a major challenge, the epitopes contain both DNA and histones, whereby the histone tails play a role in establishing the epitopes. Most importantly, the conformational epitopes of these nucleosome-specific antibodies seem to contain acetylated residues. Conclusions: Our approach, yielding a new panel of anti-apoptotic-chromatin antibodies, should facilitate the discovery of more apoptosis-induced chromatin modifications and their identification as key autoantigens in the pathogenesis of SLE.
MeSH term(s)	Acetylation ; Animals ; Antibodies, Monoclonal/immunology ; Apoptosis/immunology ; Autoantibodies/immunology ; Autoantigens/immunology ; Blotting, Western ; Chromatin/immunology ; Chromatin/metabolism ; Enzyme-Linked Immunosorbent Assay ; Epitopes, B-Lymphocyte/immunology ; Female ; Fluorescent Antibody Technique ; Lupus Erythematosus, Systemic/immunology ; Lupus Erythematosus, Systemic/metabolism ; Lupus Erythematosus, Systemic/pathology ; Mice ; Mice, Inbred MRL lpr ; Mice, Inbred NZB ; Nucleosomes/immunology
Chemical Substances	Antibodies, Monoclonal ; Autoantibodies ; Autoantigens ; Chromatin ; Epitopes, B-Lymphocyte ; Nucleosomes
Language	English
Publishing date	2010-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	424427-8
ISSN	1872-9142 ; 0161-5890
ISSN (online)	1872-9142
ISSN	0161-5890
DOI	10.1016/j.molimm.2010.08.003
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Zs.A 166: Show issues

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Article ; Online: Apoptosis-induced histone H3 methylation is targeted by autoantibodies in systemic lupus erythematosus.

van Bavel, Casandra C / Dieker, Jürgen W / Kroeze, Yvet / Tamboer, Wim P / Voll, Reinhard / Muller, Sylviane / Berden, Jo H / van der Vlag, Johan

Annals of the rheumatic diseases

2011 Volume 70, Issue 1, Page(s) 201–207

Abstract: Objectives: In systemic lupus erythematosus (SLE) apoptotic chromatin is present extracellularly, which is most likely the result of disturbed apoptosis and/or insufficient removal. Released chromatin, modified during apoptosis, activates the immune ... ...

Abstract	Objectives: In systemic lupus erythematosus (SLE) apoptotic chromatin is present extracellularly, which is most likely the result of disturbed apoptosis and/or insufficient removal. Released chromatin, modified during apoptosis, activates the immune system resulting in the formation of autoantibodies. A study was undertaken to identify apoptosis-induced histone modifications that play a role in SLE. Methods: The lupus-derived monoclonal antibody BT164, recently established by selection using apoptotic nucleosomes, was analysed by ELISA, western blot analysis and immunofluorescence staining using chromatin, cells, plasma and renal sections. Random peptide phage display and peptide inhibition ELISA were used to identify precisely the epitope of BT164. The reactivity of plasma samples from lupus mice and patients with SLE with the epitope of BT164 was investigated by peptide ELISA. Results: The epitope of BT164 was mapped in the N-terminal tail of histone H3 (27-KSAPAT-32) and included the apoptosis-induced trimethylation of K27. siRNA-mediated silencing of histone demethylases in cultured cells resulted in hypermethylation of H3K27 and increased nuclear reactivity of BT164. This apoptosis-induced H3K27me3 is a target for autoantibodies in patients and mice with SLE and is present in plasma and in glomerular deposits. Conclusion: In addition to previously identified acetylation of histone H4, H2A and H2B, this study shows that trimethylation of histone H3 on lysine 27 is induced by apoptosis and associated with autoimmunity in SLE. This finding is important for understanding the autoimmune response in SLE and for the development of translational strategies.
MeSH term(s)	Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/immunology ; Apoptosis/immunology ; Autoantibodies/immunology ; Chromatin/immunology ; Epitope Mapping/methods ; Histones/genetics ; Histones/immunology ; Histones/metabolism ; Humans ; Lupus Erythematosus, Systemic/genetics ; Lupus Erythematosus, Systemic/immunology ; Lupus Nephritis/immunology ; Methylation ; Mice ; Mice, Inbred MRL lpr ; Molecular Sequence Data ; Sequence Alignment ; Tumor Cells, Cultured
Chemical Substances	Antibodies, Monoclonal ; Autoantibodies ; Chromatin ; Histones
Language	English
Publishing date	2011-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	7090-7
ISSN	1468-2060 ; 0003-4967
ISSN (online)	1468-2060
ISSN	0003-4967
DOI	10.1136/ard.2010.129320
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Uh III Zs.114: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
Zs.MO 167: Show issues

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Article: Mimotopes for lupus-derived anti-DNA and nucleosome-specific autoantibodies selected from random peptide phage display libraries: facts and follies.

Dieker, Jürgen W / Sun, Yong-Jiang / Jacobs, Cor W / Putterman, Chaim / Monestier, Marc / Muller, Sylviane / van der Vlag, Johan / Berden, Jo H

Journal of immunological methods

2005 Volume 296, Issue 1-2, Page(s) 83–93

Abstract: Autoantibodies against chromatin are the most characteristic serological feature in SLE patients. Anti-dsDNA and nucleosome-specific antibodies are associated with glomerulonephritis, the most serious manifestation of SLE. Identification of peptides ... ...

Abstract	Autoantibodies against chromatin are the most characteristic serological feature in SLE patients. Anti-dsDNA and nucleosome-specific antibodies are associated with glomerulonephritis, the most serious manifestation of SLE. Identification of peptides mimicking conformational epitopes (so-called mimotopes) on the nucleosome recognized by these antibodies is of considerable interest. Using an approach similar to that used previously to characterize mimotopes for anti-DNA autoantibodies, we have selected and identified a mimotope for a nucleosome-specific autoantibody (#32) by screening a random peptide phage display library. However, the reactivity of monoclonal antibody (mAb) #32 with the selected mimotope (MIMO#0) in ELISA was dependent on the blocking reagents used. Using nonfat dry milk (5%), mAb #32 clearly bound to MIMO#0, but using fetal bovine calf serum (FCS) (5%), there was no binding. Furthermore, again dependent on the blocking reagent used in ELISA, the selected mimotope MIMO#0 was not only recognized by the selecting antibody mAb #32, but also by a large number of other monoclonal anti-DNA, anti-histone and nucleosome-specific autoantibodies (NSA). We could demonstrate that the selected mimotope was able to bind directly to nucleosomal material (DNA/histone complexes) and labeled DNA. This finding was extended to other previously identified mimotopes for anti-DNA autoantibodies. We conclude that nucleosomal material (DNA/histone complexes), derived from reagents used during the mimotope selection procedure, resulted in the selection of DNA-binding peptides from the phage display library, rather than mimotopes. In addition, we could demonstrate that blocking reagents greatly influence the reactivity of anti-DNA, anti-histone and nucleosome-specific autoantibodies in ELISA. Development of blocking reagents devoid of nucleosomal material (DNA/histone complexes) is urgently needed for assay systems in which anti-nuclear autoantibodies are tested.
MeSH term(s)	Amino Acid Motifs/immunology ; Antibodies, Antinuclear/immunology ; Binding Sites, Antibody/immunology ; DNA/immunology ; Humans ; Immunodominant Epitopes/immunology ; Lupus Erythematosus, Systemic/immunology ; Lupus Nephritis/immunology ; Molecular Mimicry/immunology ; Nucleosomes/immunology ; Peptide Library ; Peptides/immunology ; Peptides/isolation & purification
Chemical Substances	Antibodies, Antinuclear ; Immunodominant Epitopes ; Nucleosomes ; Peptide Library ; Peptides ; DNA (9007-49-2)
Language	English
Publishing date	2005-01
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	120142-6
ISSN	1872-7905 ; 0022-1759
ISSN (online)	1872-7905
ISSN	0022-1759
DOI	10.1016/j.jim.2004.10.010
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Zs.A 795: Show issues

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Article: Lupus nephritis: a nucleosome waste disposal defect?

Berden, Jo H M / Grootscholten, Cecile / Jürgen, W C Dieker / van der Vlag, Johan

Journal of nephrology

2002 Volume 15 Suppl 6, Page(s) S1–10

Abstract: Formation of anti-nuclear autoantibodies is a cardinal characteristic of systemic lupus erythematosus (SLE). In recent years the nucleosome has been identified as the major autoantigen, since nucleosome specific T cells have been identified, which also ... ...

Abstract	Formation of anti-nuclear autoantibodies is a cardinal characteristic of systemic lupus erythematosus (SLE). In recent years the nucleosome has been identified as the major autoantigen, since nucleosome specific T cells have been identified, which also drive the formation of anti-dsDNA and anti-histone antibodies. Nucleosome specific autoantibodies are present in a large majority of SLE patients and lupus mice. Nucleosomes are formed during apoptosis by organized cleavage of chromatin. These nucleosomes together with other lupus autoantigens cluster in apoptotic bodies at the surface of apoptotic cells. Systemic release of these autoantigens is normally prevented by swift removal of apoptotic cels. However, if the rate of apoptosis overflows the removal capacity and/or the cleaning machinery is reduced, nucleosomes are released. Furthermore, during apoptosis autoantigens can be modified, which makes them more immunogenic. Nucleosomes also play a pivotal role in the evolution of tissue lesions, especially glomerulonephritis. In lupus nephritis nucleosomes, anti-nucleosome autoantibodies and nucleosome/Ig complexes have been identified in the glomerular immune deposits. Via their cationic histone part nucleosomes can bind to heparan sulfate, a strong anionic constituent of the glomerular basement membrane.
MeSH term(s)	Animals ; Apoptosis/genetics ; Apoptosis/immunology ; Autoantibodies/genetics ; Autoantibodies/immunology ; Disease Models, Animal ; Humans ; Lupus Nephritis/genetics ; Lupus Nephritis/immunology ; Mice ; Nucleosomes/genetics ; Nucleosomes/immunology
Chemical Substances	Autoantibodies ; Nucleosomes
Language	English
Publishing date	2002-11
Publishing country	Italy
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1093991-x
ISSN	1724-6059 ; 1121-8428 ; 1120-3625
ISSN (online)	1724-6059
ISSN	1121-8428 ; 1120-3625
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Zs.A 3369: Show issues

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Article: A prospective study of anti-chromatin and anti-C1q autoantibodies in patients with proliferative lupus nephritis treated with cyclophosphamide pulses or azathioprine/methylprednisolone.

Grootscholten, Cecile / Dieker, Jürgen W C / McGrath, Fabian D / Roos, Anja / Derksen, Ronald H W M / van der Vlag, Johan / Daha, Mohamed R / Berden, Jo H M

Annals of the rheumatic diseases

2007 Volume 66, Issue 5, Page(s) 693–696

Abstract: Objective: To study the prevalence and course of anti-chromatin (anti-nucleosome, anti-double-stranded (ds) DNA and anti-histone) and anti-C1q autoantibodies in patients with proliferative lupus nephritis (LN), treated in a randomised controlled trial ... ...

Abstract	Objective: To study the prevalence and course of anti-chromatin (anti-nucleosome, anti-double-stranded (ds) DNA and anti-histone) and anti-C1q autoantibodies in patients with proliferative lupus nephritis (LN), treated in a randomised controlled trial with either cyclophosphamide or azathioprine plus methylprednisolone. Methods: Autoantibody levels were measured and analysed in 52 patients with proliferative LN, during their first year of treatment. Levels in both treatment arms were compared and associations with clinical, serological and outcome parameters were studied. Results: At study entry, prevalences for anti-nucleosome, anti-dsDNA, anti-histone and anti-C1q autoantibodies were 81%, 96%, 23% and 65%, respectively. Anti-chromatin autoantibodies correlated with each other, but not with anti-C1q levels. If patients were divided for their autoantibody titre at the start of treatment above or below the median, the only significant differences were higher SLE disease activity index with higher anti-nucleosome, and higher creatinine with higher anti-C1q autoantibodies. During the first year, a comparable rapid decline in the levels of anti-nucleosome, anti-dsDNA and anti-C1q autoantibodies was seen in both treatment arms. Anti-histone autoantibody levels were low and did not change. Renal flares were not preceded by rises in autoantibody titres. Conclusions: These results indicate that measurement of anti-chromatin and anti-C1q autoantibodies is useful for diagnosing LN, but not for monitoring disease course.
MeSH term(s)	Anti-Inflammatory Agents/administration & dosage ; Autoantibodies/immunology ; Azathioprine/administration & dosage ; Biomarkers/blood ; Chromatin/immunology ; Complement C1q/immunology ; Cyclophosphamide/administration & dosage ; DNA/immunology ; Drug Therapy, Combination ; Humans ; Immunosuppressive Agents/administration & dosage ; Lupus Nephritis/blood ; Lupus Nephritis/drug therapy ; Lupus Nephritis/immunology ; Methylprednisolone/administration & dosage ; Nucleosomes/immunology ; Prospective Studies
Chemical Substances	Anti-Inflammatory Agents ; Autoantibodies ; Biomarkers ; Chromatin ; Immunosuppressive Agents ; Nucleosomes ; Complement C1q (80295-33-6) ; Cyclophosphamide (8N3DW7272P) ; DNA (9007-49-2) ; Azathioprine (MRK240IY2L) ; Methylprednisolone (X4W7ZR7023)
Language	English
Publishing date	2007-05
Publishing country	England
Document type	Journal Article ; Randomized Controlled Trial ; Research Support, Non-U.S. Gov't
ZDB-ID	7090-7
ISSN	1468-2060 ; 0003-4967
ISSN (online)	1468-2060
ISSN	0003-4967
DOI	10.1136/ard.2006.065425
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Uh III Zs.114: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
Zs.MO 167: Show issues

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Article: Apoptosis-induced acetylation of histones is pathogenic in systemic lupus erythematosus.

Dieker, Jürgen W / Fransen, Justin H / van Bavel, Casandra C / Briand, Jean-Paul / Jacobs, Cor W / Muller, Sylviane / Berden, Jo H / van der Vlag, Johan

Arthritis and rheumatism

2007 Volume 56, Issue 6, Page(s) 1921–1933

Abstract: Objective: In systemic lupus erythematosus (SLE), inadequate removal of apoptotic cells may lead to challenge of the immune system with immunogenic self antigens that have been modified during apoptosis. We undertook this study to evaluate whether ... ...

Abstract	Objective: In systemic lupus erythematosus (SLE), inadequate removal of apoptotic cells may lead to challenge of the immune system with immunogenic self antigens that have been modified during apoptosis. We undertook this study to evaluate whether apoptosis-induced histone modifications are targets for the immune system in SLE. Methods: The epitope of KM-2, a monoclonal antihistone autoantibody derived from a lupus mouse, was mapped by random peptide phage display. The reactivity of KM-2 and plasma with (acetylated) histone H4 (H4) peptides and with nonapoptotic, apoptotic, and hyperacetylated histones was determined by immunofluorescence staining, enzyme-linked immunosorbent assay, and Western blotting. Results: KM-2 recognized apoptosis-induced acetylation of H4 at lysines 8, 12, and 16. The majority of plasma samples from SLE patients and lupus mice showed higher reactivity with triacetylated H4 peptide (residues 1-22) and with hyperacetylated and apoptotic histones than with nonacetylated H4 peptide and normal histones. Importantly, administration of triacetylated H4 peptide to lupus-prone mice before disease onset accelerated the disease by enhancing mortality and aggravating proteinuria, skin lesions, and glomerular IgG deposition, while the nonacetylated H4 peptide had no pathogenic effect. The delayed-type hypersensitivity response in lupus mice against the triacetylated H4 peptide was higher than that against the nonacetylated H4 peptide. Bone marrow-derived dendritic cells (DCs) cultured in the presence of hyperacetylated nucleosomes showed increased expression/production of CD40, CD86, interleukin-6 (IL-6), and tumor necrosis factor alpha compared with DCs cultured in the presence of normal nucleosomes. Finally, DCs cultured in the presence of hyperacetylated nucleosomes were able to activate syngeneic T cells, because IL-2 production increased. Conclusion: Apoptosis-induced acetylation of nucleosomes may represent an important driving force in the development of lupus.
MeSH term(s)	Acetylation ; Animals ; Antibodies, Monoclonal/immunology ; Apoptosis/physiology ; Autoantibodies/immunology ; Chromatin/immunology ; Dendritic Cells/cytology ; Dendritic Cells/physiology ; Epitopes/immunology ; Histones/immunology ; Histones/metabolism ; Humans ; Immune System/immunology ; Jurkat Cells ; Lupus Erythematosus, Systemic/metabolism ; Lupus Erythematosus, Systemic/physiopathology ; Mice ; Mice, Inbred BALB C ; Mice, Inbred MRL lpr ; Nucleosomes/physiology ; T-Lymphocytes/physiology ; U937 Cells
Chemical Substances	Antibodies, Monoclonal ; Autoantibodies ; Chromatin ; Epitopes ; Histones ; Nucleosomes
Language	English
Publishing date	2007-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	127294-9
ISSN	1529-0131 ; 0004-3591 ; 2326-5191
ISSN (online)	1529-0131
ISSN	0004-3591 ; 2326-5191
DOI	10.1002/art.22646
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Zs.A 24: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 523: Show issues

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Article: Albuminuria in mice after injection of antibodies against aminopeptidase A: role of angiotensin II.

Gerlofs-Nijland, Miriam E / Assmann, Karel J M / Dijkman, Henry B P M / Dieker, Jürgen W C / van Son, Jacco P H F / Mentzel, Stef / van Kats, Jorge P / Danser, A H Jan / Smithies, Oliver / Groenen, Patricia J T A / Wetzels, Jack F M

Journal of the American Society of Nephrology : JASN

2001 Volume 12, Issue 12, Page(s) 2711–2720

Abstract: ... of the nephritogenic combinations ASD-3/37 and ASD-37/41 in BALB/c mice induced albuminuria, whereas the non ...

Abstract	It has been shown that injection of combinations of anti-aminopeptidase A (APA) monoclonal antibodies (mAb) that inhibit the enzyme activity induces an acute albuminuria in mice. This albuminuria is not dependent on inflammatory cells, complement, or the coagulation system. APA is an important regulator of the renin-angiotensin system because it is involved in the degradation of angiotensin II (Ang II). This study examined the potential role of glomerular Ang II in the induction of albuminuria. The relation among renal Ang II, glomerular APAX enzyme activity, and albuminuria was examined first. Injection of the nephritogenic combinations ASD-3/37 and ASD-37/41 in BALB/c mice induced albuminuria, whereas the non-nephritogenic combination ASD-3/41 had no effect. There was no clear relation between the inhibition of glomerular APA activity and albuminuria, yet it was evident that intrarenal Ang II levels were significantly increased in albuminuric mice and not in nonalbuminuric mice. As a next step, anti-APA mAb were administered to angiotensinogen-deficient mice that do not produce Ang II, and kidney morphology and albuminuria were determined. Angiotensinogen-deficient mice also developed albuminuria upon ASD-37/41 administration. Altogether, these findings clearly demonstrate that Ang II is not required for the induction of albuminuria upon injection of enzyme-inhibiting anti-APA mAb.
MeSH term(s)	Albuminuria/immunology ; Aminopeptidases/immunology ; Angiotensin II/physiology ; Angiotensinogen/deficiency ; Angiotensinogen/genetics ; Animals ; Antibodies, Monoclonal/immunology ; Glutamyl Aminopeptidase ; Injections ; Kidney/pathology ; Mice ; Mice, Inbred BALB C ; Mice, Knockout/genetics ; Microscopy, Electron
Chemical Substances	Antibodies, Monoclonal ; Angiotensinogen (11002-13-4) ; Angiotensin II (11128-99-7) ; Aminopeptidases (EC 3.4.11.-) ; Glutamyl Aminopeptidase (EC 3.4.11.7)
Language	English
Publishing date	2001-10-30
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1085942-1
ISSN	1533-3450 ; 1046-6673
ISSN (online)	1533-3450
ISSN	1046-6673
DOI	10.1681/ASN.V12122711
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Zs.A 3344: Show issues

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