Sera from patients with poststreptococcal glomerulonephritis contain antibodies to glomerular heparan sulfate proteoglycan

Antibodies, found in human sera from patients with poststreptococcal glomerulonephritis, against proteoglycans (PG) derived from bovine and human glomeruli were investigated. PG were isolated by 4 M guanidine-HCl extraction of whole glomeruli, followed by DEAE-Sepharose CL-6B ion exchange chromatogr...

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Veröffentlicht in:The Journal of experimental medicine 1985-02, Vol.161 (2), p.277-289
Hauptverfasser: FILLIT, H, DAMLE, S. P, GREGORY, J. D, VOLIN, C, POON-KING, T, ZABRISKIE, J
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container_issue 2
container_start_page 277
container_title The Journal of experimental medicine
container_volume 161
creator FILLIT, H
DAMLE, S. P
GREGORY, J. D
VOLIN, C
POON-KING, T
ZABRISKIE, J
description Antibodies, found in human sera from patients with poststreptococcal glomerulonephritis, against proteoglycans (PG) derived from bovine and human glomeruli were investigated. PG were isolated by 4 M guanidine-HCl extraction of whole glomeruli, followed by DEAE-Sepharose CL-6B ion exchange chromatography. The anionic fractions were further purified by chromatography on Sepharose CL-4B. Biochemical analysis of the two resulting peaks revealed the presence of high molecular weight anionic material containing protein, uronic acid, glucosamine, and galactosamine. Enzymatic and chemical susceptibilities indicated the presence of heparan sulfate PG and a galactosamine-containing PG. Immunologic studies revealed the presence of anti-PG antibodies to both PG peaks of the Sepharose CL-4B column in glomerulonephritis sera. Inhibition studies using an ELISA demonstrated that heparan sulfate was a major antigenic determinant. Cross-reactivity with both mammalian and streptococcal hyaluronate was noted. Inhibition studies also indicated the presence of a second antigenic site containing N-acetylgalactosamine, possibly representing chondroitin or dermatan sulfate PG.
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P ; GREGORY, J. D ; VOLIN, C ; POON-KING, T ; ZABRISKIE, J</creator><creatorcontrib>FILLIT, H ; DAMLE, S. P ; GREGORY, J. D ; VOLIN, C ; POON-KING, T ; ZABRISKIE, J</creatorcontrib><description>Antibodies, found in human sera from patients with poststreptococcal glomerulonephritis, against proteoglycans (PG) derived from bovine and human glomeruli were investigated. PG were isolated by 4 M guanidine-HCl extraction of whole glomeruli, followed by DEAE-Sepharose CL-6B ion exchange chromatography. The anionic fractions were further purified by chromatography on Sepharose CL-4B. Biochemical analysis of the two resulting peaks revealed the presence of high molecular weight anionic material containing protein, uronic acid, glucosamine, and galactosamine. Enzymatic and chemical susceptibilities indicated the presence of heparan sulfate PG and a galactosamine-containing PG. Immunologic studies revealed the presence of anti-PG antibodies to both PG peaks of the Sepharose CL-4B column in glomerulonephritis sera. Inhibition studies using an ELISA demonstrated that heparan sulfate was a major antigenic determinant. Cross-reactivity with both mammalian and streptococcal hyaluronate was noted. Inhibition studies also indicated the presence of a second antigenic site containing N-acetylgalactosamine, possibly representing chondroitin or dermatan sulfate PG.</description><identifier>ISSN: 0022-1007</identifier><identifier>EISSN: 1540-9538</identifier><identifier>DOI: 10.1084/jem.161.2.277</identifier><identifier>PMID: 3156204</identifier><identifier>CODEN: JEMEAV</identifier><language>eng</language><publisher>New York, NY: Rockefeller University Press</publisher><subject>Acute Disease ; Animals ; Antigen-Antibody Reactions ; Autoantibodies - analysis ; Biological and medical sciences ; Cattle ; Chemical Phenomena ; Chemistry, Physical ; Chondroitin Sulfate Proteoglycans - analysis ; Chondroitin Sulfate Proteoglycans - immunology ; Chondroitin Sulfate Proteoglycans - isolation &amp; purification ; Enzyme-Linked Immunosorbent Assay ; Glomerulonephritis ; Glomerulonephritis - etiology ; Glomerulonephritis - immunology ; Glycosaminoglycans - immunology ; Heparan Sulfate Proteoglycans ; Heparitin Sulfate - analysis ; Heparitin Sulfate - immunology ; Heparitin Sulfate - isolation &amp; purification ; Hexosamines - isolation &amp; purification ; Humans ; Kidney Glomerulus - immunology ; Medical sciences ; Nephrology. 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P</creatorcontrib><creatorcontrib>GREGORY, J. D</creatorcontrib><creatorcontrib>VOLIN, C</creatorcontrib><creatorcontrib>POON-KING, T</creatorcontrib><creatorcontrib>ZABRISKIE, J</creatorcontrib><title>Sera from patients with poststreptococcal glomerulonephritis contain antibodies to glomerular heparan sulfate proteoglycan</title><title>The Journal of experimental medicine</title><addtitle>J Exp Med</addtitle><description>Antibodies, found in human sera from patients with poststreptococcal glomerulonephritis, against proteoglycans (PG) derived from bovine and human glomeruli were investigated. PG were isolated by 4 M guanidine-HCl extraction of whole glomeruli, followed by DEAE-Sepharose CL-6B ion exchange chromatography. The anionic fractions were further purified by chromatography on Sepharose CL-4B. Biochemical analysis of the two resulting peaks revealed the presence of high molecular weight anionic material containing protein, uronic acid, glucosamine, and galactosamine. Enzymatic and chemical susceptibilities indicated the presence of heparan sulfate PG and a galactosamine-containing PG. Immunologic studies revealed the presence of anti-PG antibodies to both PG peaks of the Sepharose CL-4B column in glomerulonephritis sera. Inhibition studies using an ELISA demonstrated that heparan sulfate was a major antigenic determinant. Cross-reactivity with both mammalian and streptococcal hyaluronate was noted. 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Urinary tract diseases</subject><subject>Nephropathies. Renovascular diseases. Renal failure</subject><subject>Proteins - isolation &amp; purification</subject><subject>Proteoglycans - immunology</subject><subject>Rabbits</subject><subject>Streptococcal Infections - immunology</subject><subject>Uronic Acids - isolation &amp; purification</subject><issn>0022-1007</issn><issn>1540-9538</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkU2LFDEQhoMo6zh69CjkIN56TDpf3RdBFr9gwYN6DtXp6pks6U6bpF3WX29kh0FPObwPb1XqIeQlZwfOOvn2FucD1_zQHlpjHpEdV5I1vRLdY7JjrG0bzph5Sp7lfMsYl1LpK3IluNItkzvy-xsmoFOKM12heFxKpne-nOgac8kl4Vqii85BoMcQZ0xbiAuup-SLz9TFpYBfKCzFD3H0mGmJFxASPeEKCRaatzBBQbqmWDAew72D5Tl5MkHI-OL87smPjx--X39ubr5--nL9_qZxkvPS6F5xYQxMeuwH04-mBzlwrYSSUkKHnRRCCeFUL0FqY9jgDDA94iCFUi2IPXn30Ltuw4yjq39MEOya_Azp3kbw9v9k8Sd7jL9syzuj6qA9eXMuSPHnhrnY2WeHIcCCccvWaMYk73gFmwfQpZhzwukyhDP7V5atsmyVZVtbZVX-1b-bXeiznZq_PueQq4GpXtL5fMH6uqCqNX8AY8qhRQ</recordid><startdate>19850201</startdate><enddate>19850201</enddate><creator>FILLIT, H</creator><creator>DAMLE, S. 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D ; VOLIN, C ; POON-KING, T ; ZABRISKIE, J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c411t-6951377af6d9b79d79a4b16535444a8e8433533c594a46770bc7a06deb43552a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Acute Disease</topic><topic>Animals</topic><topic>Antigen-Antibody Reactions</topic><topic>Autoantibodies - analysis</topic><topic>Biological and medical sciences</topic><topic>Cattle</topic><topic>Chemical Phenomena</topic><topic>Chemistry, Physical</topic><topic>Chondroitin Sulfate Proteoglycans - analysis</topic><topic>Chondroitin Sulfate Proteoglycans - immunology</topic><topic>Chondroitin Sulfate Proteoglycans - isolation &amp; purification</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Glomerulonephritis</topic><topic>Glomerulonephritis - etiology</topic><topic>Glomerulonephritis - immunology</topic><topic>Glycosaminoglycans - immunology</topic><topic>Heparan Sulfate Proteoglycans</topic><topic>Heparitin Sulfate - analysis</topic><topic>Heparitin Sulfate - immunology</topic><topic>Heparitin Sulfate - isolation &amp; purification</topic><topic>Hexosamines - isolation &amp; purification</topic><topic>Humans</topic><topic>Kidney Glomerulus - immunology</topic><topic>Medical sciences</topic><topic>Nephrology. Urinary tract diseases</topic><topic>Nephropathies. Renovascular diseases. Renal failure</topic><topic>Proteins - isolation &amp; purification</topic><topic>Proteoglycans - immunology</topic><topic>Rabbits</topic><topic>Streptococcal Infections - immunology</topic><topic>Uronic Acids - isolation &amp; purification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>FILLIT, H</creatorcontrib><creatorcontrib>DAMLE, S. P</creatorcontrib><creatorcontrib>GREGORY, J. 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D</au><au>VOLIN, C</au><au>POON-KING, T</au><au>ZABRISKIE, J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Sera from patients with poststreptococcal glomerulonephritis contain antibodies to glomerular heparan sulfate proteoglycan</atitle><jtitle>The Journal of experimental medicine</jtitle><addtitle>J Exp Med</addtitle><date>1985-02-01</date><risdate>1985</risdate><volume>161</volume><issue>2</issue><spage>277</spage><epage>289</epage><pages>277-289</pages><issn>0022-1007</issn><eissn>1540-9538</eissn><coden>JEMEAV</coden><abstract>Antibodies, found in human sera from patients with poststreptococcal glomerulonephritis, against proteoglycans (PG) derived from bovine and human glomeruli were investigated. PG were isolated by 4 M guanidine-HCl extraction of whole glomeruli, followed by DEAE-Sepharose CL-6B ion exchange chromatography. The anionic fractions were further purified by chromatography on Sepharose CL-4B. Biochemical analysis of the two resulting peaks revealed the presence of high molecular weight anionic material containing protein, uronic acid, glucosamine, and galactosamine. Enzymatic and chemical susceptibilities indicated the presence of heparan sulfate PG and a galactosamine-containing PG. Immunologic studies revealed the presence of anti-PG antibodies to both PG peaks of the Sepharose CL-4B column in glomerulonephritis sera. Inhibition studies using an ELISA demonstrated that heparan sulfate was a major antigenic determinant. Cross-reactivity with both mammalian and streptococcal hyaluronate was noted. Inhibition studies also indicated the presence of a second antigenic site containing N-acetylgalactosamine, possibly representing chondroitin or dermatan sulfate PG.</abstract><cop>New York, NY</cop><pub>Rockefeller University Press</pub><pmid>3156204</pmid><doi>10.1084/jem.161.2.277</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record>
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subjects Acute Disease
Animals
Antigen-Antibody Reactions
Autoantibodies - analysis
Biological and medical sciences
Cattle
Chemical Phenomena
Chemistry, Physical
Chondroitin Sulfate Proteoglycans - analysis
Chondroitin Sulfate Proteoglycans - immunology
Chondroitin Sulfate Proteoglycans - isolation & purification
Enzyme-Linked Immunosorbent Assay
Glomerulonephritis
Glomerulonephritis - etiology
Glomerulonephritis - immunology
Glycosaminoglycans - immunology
Heparan Sulfate Proteoglycans
Heparitin Sulfate - analysis
Heparitin Sulfate - immunology
Heparitin Sulfate - isolation & purification
Hexosamines - isolation & purification
Humans
Kidney Glomerulus - immunology
Medical sciences
Nephrology. Urinary tract diseases
Nephropathies. Renovascular diseases. Renal failure
Proteins - isolation & purification
Proteoglycans - immunology
Rabbits
Streptococcal Infections - immunology
Uronic Acids - isolation & purification
title Sera from patients with poststreptococcal glomerulonephritis contain antibodies to glomerular heparan sulfate proteoglycan
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