Interaction of immune complexes with glomerular heparan sulfate–proteoglycans
Interaction of immune complexes with glomerular heparan sulfate–proteoglycans. The binding characteristics of cationic and more neutral immune complexes with heparan sulfate–proteoglycan enriched anionic sites of glomerular basement membrane and mesangial matrix were studied. Rat kidneys were treate...
Gespeichert in:
| Veröffentlicht in: | Kidney international 1986-12, Vol.30 (6), p.842-851 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 851 |
|---|---|
| container_issue | 6 |
| container_start_page | 842 |
| container_title | Kidney international |
| container_volume | 30 |
| creator | Kanwar, Yashpal S. Caulin–Glaser, Teresa Gallo, Gloria R. Lamm, Michael E. |
| description | Interaction of immune complexes with glomerular heparan sulfate–proteoglycans. The binding characteristics of cationic and more neutral immune complexes with heparan sulfate–proteoglycan enriched anionic sites of glomerular basement membrane and mesangial matrix were studied. Rat kidneys were treated either with buffers alone or buffers containing heparitinase or chondroitinase-ABC followed by perfusion with cationic or native immune complexes. Tissues were processed for immunofluorescence and transmission electron microscopy after fixation with glutaraldehyde or tannic acid glutaraldehyde. Kidneys perfused with radioiodinated immune complexes were processed for light and electron microscopic autoradiography. In addition, glomeruli from kidneys perfused with radioiodinated immune complexes were isolated and counted for radioactivity. By immunofluorescence the cationic immune complexes deposited linearly along the glomerular basement membrane. By electron microscopy, the cationic complexes localized mainly in the inner and outer layers of the glomerular basement membrane and to a certain extent in the mesangial matrix in a distribution that corresponded to previously documented anionic sites. Whereas heparitinase treatment abrogated the binding of cationic immune complexes in both glomerular basement membrane and mesangial matrix, chondroitinase-ABC treatment did not cause any decrease in binding. In contrast, more neutral immune complexes appeared to be nonspecifically trapped in the mesangium, and their distribution was unaffected by both enzymatic treatments. Light and electron microscopic autoradiography and counts of isolated glomeruli confirmed these findings. The results overall indicate that cationic immune complexes bind electrostatically to the heparan sulfate–proteoglycan enriched anionic sites of the glomerular basement membrane and mesangial matrix, while more neutral immune complexes are nonspecifically trapped in the mesangium of the renal glomerulus. |
| doi_str_mv | 10.1038/ki.1986.264 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_77281505</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0085253815338473</els_id><sourcerecordid>77281505</sourcerecordid><originalsourceid>FETCH-LOGICAL-c425t-854a4dfd5f7607445740006703c259a7d12190198db469453e0f3da189ad3bbc3</originalsourceid><addsrcrecordid>eNqFkLtqHTEQhkVIsE_sVKkNW4Q0YY91m5W2NCYXg8FNUgsdadZWrF0dS7u-dHmHvGGeJDLn4CqQahjm45-Zj5D3jK4ZFfr0NqxZr7s17-QrsmLARcsUwGuyolRDy0HoQ_K2lJ-09r2gB-SA90B5p1bk6mKaMVs3hzQ1aWjCOC4TNi6N24iPWJqHMN801zGNmJdoc3ODW5vt1JQlDnbGP79-b3OaMV3HJ2enckzeDDYWfLevR-THl8_fz7-1l1dfL87PLlsnOcytBmmlHzwMqqNKSlCyHtcpKhyH3irPOOtp_cpvZNdLEEgH4S3TvfVis3HiiHzc5dbtdwuW2YyhOIzRTpiWYpTimgGFCn7agS6nUjIOZpvDaPOTYdQ86zO3wTzrM1VfpU_2sctmRP_C7n3V-Yf93BZn41BNuFBeMC000xz-jykNTFQMdhhWU_cBsyku4OTQh4xuNj6Ff175F8jll0Q</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>77281505</pqid></control><display><type>article</type><title>Interaction of immune complexes with glomerular heparan sulfate–proteoglycans</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>Kanwar, Yashpal S. ; Caulin–Glaser, Teresa ; Gallo, Gloria R. ; Lamm, Michael E.</creator><creatorcontrib>Kanwar, Yashpal S. ; Caulin–Glaser, Teresa ; Gallo, Gloria R. ; Lamm, Michael E.</creatorcontrib><description>Interaction of immune complexes with glomerular heparan sulfate–proteoglycans. The binding characteristics of cationic and more neutral immune complexes with heparan sulfate–proteoglycan enriched anionic sites of glomerular basement membrane and mesangial matrix were studied. Rat kidneys were treated either with buffers alone or buffers containing heparitinase or chondroitinase-ABC followed by perfusion with cationic or native immune complexes. Tissues were processed for immunofluorescence and transmission electron microscopy after fixation with glutaraldehyde or tannic acid glutaraldehyde. Kidneys perfused with radioiodinated immune complexes were processed for light and electron microscopic autoradiography. In addition, glomeruli from kidneys perfused with radioiodinated immune complexes were isolated and counted for radioactivity. By immunofluorescence the cationic immune complexes deposited linearly along the glomerular basement membrane. By electron microscopy, the cationic complexes localized mainly in the inner and outer layers of the glomerular basement membrane and to a certain extent in the mesangial matrix in a distribution that corresponded to previously documented anionic sites. Whereas heparitinase treatment abrogated the binding of cationic immune complexes in both glomerular basement membrane and mesangial matrix, chondroitinase-ABC treatment did not cause any decrease in binding. In contrast, more neutral immune complexes appeared to be nonspecifically trapped in the mesangium, and their distribution was unaffected by both enzymatic treatments. Light and electron microscopic autoradiography and counts of isolated glomeruli confirmed these findings. The results overall indicate that cationic immune complexes bind electrostatically to the heparan sulfate–proteoglycan enriched anionic sites of the glomerular basement membrane and mesangial matrix, while more neutral immune complexes are nonspecifically trapped in the mesangium of the renal glomerulus.</description><identifier>ISSN: 0085-2538</identifier><identifier>EISSN: 1523-1755</identifier><identifier>DOI: 10.1038/ki.1986.264</identifier><identifier>PMID: 2950267</identifier><identifier>CODEN: KDYIA5</identifier><language>eng</language><publisher>New York, NY: Elsevier Inc</publisher><subject>Animals ; Antigen-Antibody Complex - immunology ; Antigen-Antibody Complex - metabolism ; Applied sciences ; Autoradiography ; Basement Membrane - analysis ; Basement Membrane - immunology ; Basement Membrane - ultrastructure ; Biological and medical sciences ; Chondroitinases and Chondroitin Lyases - pharmacology ; Exact sciences and technology ; Experimental and animal immunopathology. Animal models ; Fluorescent Antibody Technique ; Glomerular Mesangium - immunology ; Glomerular Mesangium - ultrastructure ; Glycosaminoglycans - immunology ; Heparitin Sulfate - immunology ; Immunopathology ; In Vitro Techniques ; Iodine Radioisotopes ; Kidney Glomerulus - immunology ; Kidney Glomerulus - ultrastructure ; Medical sciences ; Microscopy, Electron ; Other techniques and industries ; Polysaccharide-Lyases - pharmacology ; Protein Binding ; Proteoglycans - immunology ; Rats</subject><ispartof>Kidney international, 1986-12, Vol.30 (6), p.842-851</ispartof><rights>1986 International Society of Nephrology</rights><rights>1987 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c425t-854a4dfd5f7607445740006703c259a7d12190198db469453e0f3da189ad3bbc3</citedby><cites>FETCH-LOGICAL-c425t-854a4dfd5f7607445740006703c259a7d12190198db469453e0f3da189ad3bbc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8378513$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8381825$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2950267$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kanwar, Yashpal S.</creatorcontrib><creatorcontrib>Caulin–Glaser, Teresa</creatorcontrib><creatorcontrib>Gallo, Gloria R.</creatorcontrib><creatorcontrib>Lamm, Michael E.</creatorcontrib><title>Interaction of immune complexes with glomerular heparan sulfate–proteoglycans</title><title>Kidney international</title><addtitle>Kidney Int</addtitle><description>Interaction of immune complexes with glomerular heparan sulfate–proteoglycans. The binding characteristics of cationic and more neutral immune complexes with heparan sulfate–proteoglycan enriched anionic sites of glomerular basement membrane and mesangial matrix were studied. Rat kidneys were treated either with buffers alone or buffers containing heparitinase or chondroitinase-ABC followed by perfusion with cationic or native immune complexes. Tissues were processed for immunofluorescence and transmission electron microscopy after fixation with glutaraldehyde or tannic acid glutaraldehyde. Kidneys perfused with radioiodinated immune complexes were processed for light and electron microscopic autoradiography. In addition, glomeruli from kidneys perfused with radioiodinated immune complexes were isolated and counted for radioactivity. By immunofluorescence the cationic immune complexes deposited linearly along the glomerular basement membrane. By electron microscopy, the cationic complexes localized mainly in the inner and outer layers of the glomerular basement membrane and to a certain extent in the mesangial matrix in a distribution that corresponded to previously documented anionic sites. Whereas heparitinase treatment abrogated the binding of cationic immune complexes in both glomerular basement membrane and mesangial matrix, chondroitinase-ABC treatment did not cause any decrease in binding. In contrast, more neutral immune complexes appeared to be nonspecifically trapped in the mesangium, and their distribution was unaffected by both enzymatic treatments. Light and electron microscopic autoradiography and counts of isolated glomeruli confirmed these findings. The results overall indicate that cationic immune complexes bind electrostatically to the heparan sulfate–proteoglycan enriched anionic sites of the glomerular basement membrane and mesangial matrix, while more neutral immune complexes are nonspecifically trapped in the mesangium of the renal glomerulus.</description><subject>Animals</subject><subject>Antigen-Antibody Complex - immunology</subject><subject>Antigen-Antibody Complex - metabolism</subject><subject>Applied sciences</subject><subject>Autoradiography</subject><subject>Basement Membrane - analysis</subject><subject>Basement Membrane - immunology</subject><subject>Basement Membrane - ultrastructure</subject><subject>Biological and medical sciences</subject><subject>Chondroitinases and Chondroitin Lyases - pharmacology</subject><subject>Exact sciences and technology</subject><subject>Experimental and animal immunopathology. Animal models</subject><subject>Fluorescent Antibody Technique</subject><subject>Glomerular Mesangium - immunology</subject><subject>Glomerular Mesangium - ultrastructure</subject><subject>Glycosaminoglycans - immunology</subject><subject>Heparitin Sulfate - immunology</subject><subject>Immunopathology</subject><subject>In Vitro Techniques</subject><subject>Iodine Radioisotopes</subject><subject>Kidney Glomerulus - immunology</subject><subject>Kidney Glomerulus - ultrastructure</subject><subject>Medical sciences</subject><subject>Microscopy, Electron</subject><subject>Other techniques and industries</subject><subject>Polysaccharide-Lyases - pharmacology</subject><subject>Protein Binding</subject><subject>Proteoglycans - immunology</subject><subject>Rats</subject><issn>0085-2538</issn><issn>1523-1755</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkLtqHTEQhkVIsE_sVKkNW4Q0YY91m5W2NCYXg8FNUgsdadZWrF0dS7u-dHmHvGGeJDLn4CqQahjm45-Zj5D3jK4ZFfr0NqxZr7s17-QrsmLARcsUwGuyolRDy0HoQ_K2lJ-09r2gB-SA90B5p1bk6mKaMVs3hzQ1aWjCOC4TNi6N24iPWJqHMN801zGNmJdoc3ODW5vt1JQlDnbGP79-b3OaMV3HJ2enckzeDDYWfLevR-THl8_fz7-1l1dfL87PLlsnOcytBmmlHzwMqqNKSlCyHtcpKhyH3irPOOtp_cpvZNdLEEgH4S3TvfVis3HiiHzc5dbtdwuW2YyhOIzRTpiWYpTimgGFCn7agS6nUjIOZpvDaPOTYdQ86zO3wTzrM1VfpU_2sctmRP_C7n3V-Yf93BZn41BNuFBeMC000xz-jykNTFQMdhhWU_cBsyku4OTQh4xuNj6Ff175F8jll0Q</recordid><startdate>19861201</startdate><enddate>19861201</enddate><creator>Kanwar, Yashpal S.</creator><creator>Caulin–Glaser, Teresa</creator><creator>Gallo, Gloria R.</creator><creator>Lamm, Michael E.</creator><general>Elsevier Inc</general><general>Nature Publishing</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19861201</creationdate><title>Interaction of immune complexes with glomerular heparan sulfate–proteoglycans</title><author>Kanwar, Yashpal S. ; Caulin–Glaser, Teresa ; Gallo, Gloria R. ; Lamm, Michael E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c425t-854a4dfd5f7607445740006703c259a7d12190198db469453e0f3da189ad3bbc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>Animals</topic><topic>Antigen-Antibody Complex - immunology</topic><topic>Antigen-Antibody Complex - metabolism</topic><topic>Applied sciences</topic><topic>Autoradiography</topic><topic>Basement Membrane - analysis</topic><topic>Basement Membrane - immunology</topic><topic>Basement Membrane - ultrastructure</topic><topic>Biological and medical sciences</topic><topic>Chondroitinases and Chondroitin Lyases - pharmacology</topic><topic>Exact sciences and technology</topic><topic>Experimental and animal immunopathology. Animal models</topic><topic>Fluorescent Antibody Technique</topic><topic>Glomerular Mesangium - immunology</topic><topic>Glomerular Mesangium - ultrastructure</topic><topic>Glycosaminoglycans - immunology</topic><topic>Heparitin Sulfate - immunology</topic><topic>Immunopathology</topic><topic>In Vitro Techniques</topic><topic>Iodine Radioisotopes</topic><topic>Kidney Glomerulus - immunology</topic><topic>Kidney Glomerulus - ultrastructure</topic><topic>Medical sciences</topic><topic>Microscopy, Electron</topic><topic>Other techniques and industries</topic><topic>Polysaccharide-Lyases - pharmacology</topic><topic>Protein Binding</topic><topic>Proteoglycans - immunology</topic><topic>Rats</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kanwar, Yashpal S.</creatorcontrib><creatorcontrib>Caulin–Glaser, Teresa</creatorcontrib><creatorcontrib>Gallo, Gloria R.</creatorcontrib><creatorcontrib>Lamm, Michael E.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Kidney international</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kanwar, Yashpal S.</au><au>Caulin–Glaser, Teresa</au><au>Gallo, Gloria R.</au><au>Lamm, Michael E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interaction of immune complexes with glomerular heparan sulfate–proteoglycans</atitle><jtitle>Kidney international</jtitle><addtitle>Kidney Int</addtitle><date>1986-12-01</date><risdate>1986</risdate><volume>30</volume><issue>6</issue><spage>842</spage><epage>851</epage><pages>842-851</pages><issn>0085-2538</issn><eissn>1523-1755</eissn><coden>KDYIA5</coden><abstract>Interaction of immune complexes with glomerular heparan sulfate–proteoglycans. The binding characteristics of cationic and more neutral immune complexes with heparan sulfate–proteoglycan enriched anionic sites of glomerular basement membrane and mesangial matrix were studied. Rat kidneys were treated either with buffers alone or buffers containing heparitinase or chondroitinase-ABC followed by perfusion with cationic or native immune complexes. Tissues were processed for immunofluorescence and transmission electron microscopy after fixation with glutaraldehyde or tannic acid glutaraldehyde. Kidneys perfused with radioiodinated immune complexes were processed for light and electron microscopic autoradiography. In addition, glomeruli from kidneys perfused with radioiodinated immune complexes were isolated and counted for radioactivity. By immunofluorescence the cationic immune complexes deposited linearly along the glomerular basement membrane. By electron microscopy, the cationic complexes localized mainly in the inner and outer layers of the glomerular basement membrane and to a certain extent in the mesangial matrix in a distribution that corresponded to previously documented anionic sites. Whereas heparitinase treatment abrogated the binding of cationic immune complexes in both glomerular basement membrane and mesangial matrix, chondroitinase-ABC treatment did not cause any decrease in binding. In contrast, more neutral immune complexes appeared to be nonspecifically trapped in the mesangium, and their distribution was unaffected by both enzymatic treatments. Light and electron microscopic autoradiography and counts of isolated glomeruli confirmed these findings. The results overall indicate that cationic immune complexes bind electrostatically to the heparan sulfate–proteoglycan enriched anionic sites of the glomerular basement membrane and mesangial matrix, while more neutral immune complexes are nonspecifically trapped in the mesangium of the renal glomerulus.</abstract><cop>New York, NY</cop><pub>Elsevier Inc</pub><pmid>2950267</pmid><doi>10.1038/ki.1986.264</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0085-2538 |
| ispartof | Kidney international, 1986-12, Vol.30 (6), p.842-851 |
| issn | 0085-2538 1523-1755 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77281505 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Animals Antigen-Antibody Complex - immunology Antigen-Antibody Complex - metabolism Applied sciences Autoradiography Basement Membrane - analysis Basement Membrane - immunology Basement Membrane - ultrastructure Biological and medical sciences Chondroitinases and Chondroitin Lyases - pharmacology Exact sciences and technology Experimental and animal immunopathology. Animal models Fluorescent Antibody Technique Glomerular Mesangium - immunology Glomerular Mesangium - ultrastructure Glycosaminoglycans - immunology Heparitin Sulfate - immunology Immunopathology In Vitro Techniques Iodine Radioisotopes Kidney Glomerulus - immunology Kidney Glomerulus - ultrastructure Medical sciences Microscopy, Electron Other techniques and industries Polysaccharide-Lyases - pharmacology Protein Binding Proteoglycans - immunology Rats |
| title | Interaction of immune complexes with glomerular heparan sulfate–proteoglycans |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-20T19%3A37%3A24IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Interaction%20of%20immune%20complexes%20with%20glomerular%20heparan%20sulfate%E2%80%93proteoglycans&rft.jtitle=Kidney%20international&rft.au=Kanwar,%20Yashpal%20S.&rft.date=1986-12-01&rft.volume=30&rft.issue=6&rft.spage=842&rft.epage=851&rft.pages=842-851&rft.issn=0085-2538&rft.eissn=1523-1755&rft.coden=KDYIA5&rft_id=info:doi/10.1038/ki.1986.264&rft_dat=%3Cproquest_cross%3E77281505%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=77281505&rft_id=info:pmid/2950267&rft_els_id=S0085253815338473&rfr_iscdi=true |