New insights into the role of serum amyloid P component, a novel lipopolysaccharide-binding protein
Serum amyloid P component (SAP) is a highly preserved plasma protein named for its ubiquitous presence in amyloid deposits. Although SAP is described to bind many ligands, no clear biological function has been ascribed to it as yet. This review summarizes the current knowledge about the protein SAP,...
Gespeichert in:
| Veröffentlicht in: | FEMS immunology and medical microbiology 1999-12, Vol.26 (3), p.197-202 |
|---|---|
| 1. Verfasser: | |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 202 |
|---|---|
| container_issue | 3 |
| container_start_page | 197 |
| container_title | FEMS immunology and medical microbiology |
| container_volume | 26 |
| creator | de Haas, Carla J.C |
| description | Serum amyloid P component (SAP) is a highly preserved plasma protein named for its ubiquitous presence in amyloid deposits. Although SAP is described to bind many ligands, no clear biological function has been ascribed to it as yet. This review summarizes the current knowledge about the protein SAP, its ligands and functional properties. Finally, the author focuses on the recent finding of the binding of SAP to lipopolysaccharide (LPS) and Gram-negative bacteria and the possible functional consequences of these interactions. |
| doi_str_mv | 10.1016/S0928-8244(99)00148-0 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_69332959</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0928824499001480</els_id><sourcerecordid>17402493</sourcerecordid><originalsourceid>FETCH-LOGICAL-c392t-1be07ea0b993c634fc7ebed9b7fbf60210c85baf703d1a2323a59f33168c45593</originalsourceid><addsrcrecordid>eNqNkU9L5TAUxYM46PONH0HJShSsc9MkbbMaBvEfiA6MgruQpre-DG1Skz7lfXurT8TdzOrexe-cA-cQssfghAErfvwBlVdZlQtxqNQRABNVBhtkxmQpskLJh00y-0S2yU5KfwFAKIAtss1AlpJxmBF7gy_U-eQeF2OanjHQcYE0hg5paGnCuOyp6VddcA39TW3oh-DRj8fUUB-esaOdG8IQulUy1i5MdA1mtfON8490iGFE57-Tb63pEu5-3Dm5Pz-7O73Mrm8vrk5_XWeWq3zMWI1QooFaKW4LLlpbYo2Nqsu2bgvIGdhK1qYtgTfM5DznRqqWc1ZUVkip-JwcrH2n3KclplH3LlnsOuMxLJMuFOe5-g-QlQJyMdFzItegjSGliK0eoutNXGkG-m0G_T6DfutYK6XfZ9Aw6fY_ApZ1j80X1br3Cfi5BnDq49lh1Mk69BYbF9GOugnuHxGvOC-YWw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>17402493</pqid></control><display><type>article</type><title>New insights into the role of serum amyloid P component, a novel lipopolysaccharide-binding protein</title><source>MEDLINE</source><source>Access via Wiley Online Library</source><source>Oxford University Press Journals All Titles (1996-Current)</source><source>Alma/SFX Local Collection</source><creator>de Haas, Carla J.C</creator><creatorcontrib>de Haas, Carla J.C</creatorcontrib><description>Serum amyloid P component (SAP) is a highly preserved plasma protein named for its ubiquitous presence in amyloid deposits. Although SAP is described to bind many ligands, no clear biological function has been ascribed to it as yet. This review summarizes the current knowledge about the protein SAP, its ligands and functional properties. Finally, the author focuses on the recent finding of the binding of SAP to lipopolysaccharide (LPS) and Gram-negative bacteria and the possible functional consequences of these interactions.</description><identifier>ISSN: 0928-8244</identifier><identifier>EISSN: 1574-695X</identifier><identifier>DOI: 10.1016/S0928-8244(99)00148-0</identifier><identifier>PMID: 10575130</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Alzheimer’s disease ; Animals ; Gram-Negative Bacteria - metabolism ; Gram-negative bacterium ; Humans ; Lipopolysaccharide binding ; Lipopolysaccharide neutralization ; Lipopolysaccharides - metabolism ; Pentraxin ; Serum amyloid P component ; Serum Amyloid P-Component - physiology</subject><ispartof>FEMS immunology and medical microbiology, 1999-12, Vol.26 (3), p.197-202</ispartof><rights>1999 Federation of European Microbiological Societies</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c392t-1be07ea0b993c634fc7ebed9b7fbf60210c85baf703d1a2323a59f33168c45593</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10575130$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>de Haas, Carla J.C</creatorcontrib><title>New insights into the role of serum amyloid P component, a novel lipopolysaccharide-binding protein</title><title>FEMS immunology and medical microbiology</title><addtitle>FEMS Immunol Med Microbiol</addtitle><description>Serum amyloid P component (SAP) is a highly preserved plasma protein named for its ubiquitous presence in amyloid deposits. Although SAP is described to bind many ligands, no clear biological function has been ascribed to it as yet. This review summarizes the current knowledge about the protein SAP, its ligands and functional properties. Finally, the author focuses on the recent finding of the binding of SAP to lipopolysaccharide (LPS) and Gram-negative bacteria and the possible functional consequences of these interactions.</description><subject>Alzheimer’s disease</subject><subject>Animals</subject><subject>Gram-Negative Bacteria - metabolism</subject><subject>Gram-negative bacterium</subject><subject>Humans</subject><subject>Lipopolysaccharide binding</subject><subject>Lipopolysaccharide neutralization</subject><subject>Lipopolysaccharides - metabolism</subject><subject>Pentraxin</subject><subject>Serum amyloid P component</subject><subject>Serum Amyloid P-Component - physiology</subject><issn>0928-8244</issn><issn>1574-695X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU9L5TAUxYM46PONH0HJShSsc9MkbbMaBvEfiA6MgruQpre-DG1Skz7lfXurT8TdzOrexe-cA-cQssfghAErfvwBlVdZlQtxqNQRABNVBhtkxmQpskLJh00y-0S2yU5KfwFAKIAtss1AlpJxmBF7gy_U-eQeF2OanjHQcYE0hg5paGnCuOyp6VddcA39TW3oh-DRj8fUUB-esaOdG8IQulUy1i5MdA1mtfON8490iGFE57-Tb63pEu5-3Dm5Pz-7O73Mrm8vrk5_XWeWq3zMWI1QooFaKW4LLlpbYo2Nqsu2bgvIGdhK1qYtgTfM5DznRqqWc1ZUVkip-JwcrH2n3KclplH3LlnsOuMxLJMuFOe5-g-QlQJyMdFzItegjSGliK0eoutNXGkG-m0G_T6DfutYK6XfZ9Aw6fY_ApZ1j80X1br3Cfi5BnDq49lh1Mk69BYbF9GOugnuHxGvOC-YWw</recordid><startdate>19991201</startdate><enddate>19991201</enddate><creator>de Haas, Carla J.C</creator><general>Elsevier B.V</general><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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19991201</creationdate><title>New insights into the role of serum amyloid P component, a novel lipopolysaccharide-binding protein</title><author>de Haas, Carla J.C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c392t-1be07ea0b993c634fc7ebed9b7fbf60210c85baf703d1a2323a59f33168c45593</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Alzheimer’s disease</topic><topic>Animals</topic><topic>Gram-Negative Bacteria - metabolism</topic><topic>Gram-negative bacterium</topic><topic>Humans</topic><topic>Lipopolysaccharide binding</topic><topic>Lipopolysaccharide neutralization</topic><topic>Lipopolysaccharides - metabolism</topic><topic>Pentraxin</topic><topic>Serum amyloid P component</topic><topic>Serum Amyloid P-Component - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>de Haas, Carla J.C</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>FEMS immunology and medical microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>de Haas, Carla J.C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>New insights into the role of serum amyloid P component, a novel lipopolysaccharide-binding protein</atitle><jtitle>FEMS immunology and medical microbiology</jtitle><addtitle>FEMS Immunol Med Microbiol</addtitle><date>1999-12-01</date><risdate>1999</risdate><volume>26</volume><issue>3</issue><spage>197</spage><epage>202</epage><pages>197-202</pages><issn>0928-8244</issn><eissn>1574-695X</eissn><abstract>Serum amyloid P component (SAP) is a highly preserved plasma protein named for its ubiquitous presence in amyloid deposits. Although SAP is described to bind many ligands, no clear biological function has been ascribed to it as yet. This review summarizes the current knowledge about the protein SAP, its ligands and functional properties. Finally, the author focuses on the recent finding of the binding of SAP to lipopolysaccharide (LPS) and Gram-negative bacteria and the possible functional consequences of these interactions.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>10575130</pmid><doi>10.1016/S0928-8244(99)00148-0</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0928-8244 |
| ispartof | FEMS immunology and medical microbiology, 1999-12, Vol.26 (3), p.197-202 |
| issn | 0928-8244 1574-695X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_69332959 |
| source | MEDLINE; Access via Wiley Online Library; Oxford University Press Journals All Titles (1996-Current); Alma/SFX Local Collection |
| subjects | Alzheimer’s disease Animals Gram-Negative Bacteria - metabolism Gram-negative bacterium Humans Lipopolysaccharide binding Lipopolysaccharide neutralization Lipopolysaccharides - metabolism Pentraxin Serum amyloid P component Serum Amyloid P-Component - physiology |
| title | New insights into the role of serum amyloid P component, a novel lipopolysaccharide-binding protein |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-23T15%3A38%3A40IST&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=New%20insights%20into%20the%20role%20of%20serum%20amyloid%20P%20component,%20a%20novel%20lipopolysaccharide-binding%20protein&rft.jtitle=FEMS%20immunology%20and%20medical%20microbiology&rft.au=de%20Haas,%20Carla%20J.C&rft.date=1999-12-01&rft.volume=26&rft.issue=3&rft.spage=197&rft.epage=202&rft.pages=197-202&rft.issn=0928-8244&rft.eissn=1574-695X&rft_id=info:doi/10.1016/S0928-8244(99)00148-0&rft_dat=%3Cproquest_cross%3E17402493%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=17402493&rft_id=info:pmid/10575130&rft_els_id=S0928824499001480&rfr_iscdi=true |