Specific glycosylation of [alpha]1-acid glycoprotein characterises patients with familial Mediterranean fever and obligatory carriers of MEFV
BACKGROUND Familial Mediterranean fever (FMF) is a periodic febrile disorder, characterised by fever and serositis. The acute phase response during attacks of FMF results from the release of cytokines, which in turn induce increased expression and changed glycosylation of acute phase proteins. A rec...
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| Veröffentlicht in: | Annals of the rheumatic diseases 2001-08, Vol.60 (8), p.777 |
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| creator | Poland, D C W Drenth, J P H Rabinovitz, E Livneh, A Bijzet, J van het Hof, B van Dijk, W |
| description | BACKGROUND Familial Mediterranean fever (FMF) is a periodic febrile disorder, characterised by fever and serositis. The acute phase response during attacks of FMF results from the release of cytokines, which in turn induce increased expression and changed glycosylation of acute phase proteins. A recent study indicated that attacks in FMF are accompanied by a rise of plasma concentrations of serum amyloid A (SAA) and C reactive protein (CRP), which remain significantly raised during remission relative to healthy controls. Another study suggested that obligatory heterozygotes also display an inflammatory acute phase response. OBJECTIVE To determine the state of inflammation in homozygotic and heterozygotic MEFV genotypes. METHODS CRP and SAA were studied by enzyme linked immunosorbent assay (ELISA). The glycosylation of the acute phase protein, α1 -acid glycoprotein (AGP), was visualised with crossed affinoimmunoelectrophoresis with concanavalin A as diantennary glycan-specific component and Aleuria aurantia lectin as fucose-specific affinity component. RESULTS FMF attacks were associated with an increase (p |
| doi_str_mv | 10.1136/ard.60.8.777 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest</sourceid><recordid>TN_cdi_proquest_journals_1778067176</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>4008341341</sourcerecordid><originalsourceid>FETCH-proquest_journals_17780671763</originalsourceid><addsrcrecordid>eNqNjc1KxDAUhYMoWH92PsAF162JHZK6lhnczMrBjchwTW-md4hJTTJKH8J3tqIP4OpwON_hE-JKyUapVt9g6hstm64xxhyJSi10V99KLY9FJaVs68WdNqfiLOf9XGWnukp8PY5k2bGFnZ9szJPHwjFAdPCMfhzwRdVouf-dxxQLcQA7YEJbKHGmDON8oVAyfHIZwOEbe0YPa-p5RhIGwgCOPigBhh7iq-cdlpgmsJgSU8o_uvVy9XQhThz6TJd_eS6uV8vN_UM9i98PlMt2Hw8pzNNWGdNJbZTR7f-ob-m5XHA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1778067176</pqid></control><display><type>article</type><title>Specific glycosylation of [alpha]1-acid glycoprotein characterises patients with familial Mediterranean fever and obligatory carriers of MEFV</title><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><creator>Poland, D C W ; Drenth, J P H ; Rabinovitz, E ; Livneh, A ; Bijzet, J ; van het Hof, B ; van Dijk, W</creator><creatorcontrib>Poland, D C W ; Drenth, J P H ; Rabinovitz, E ; Livneh, A ; Bijzet, J ; van het Hof, B ; van Dijk, W</creatorcontrib><description>BACKGROUND Familial Mediterranean fever (FMF) is a periodic febrile disorder, characterised by fever and serositis. The acute phase response during attacks of FMF results from the release of cytokines, which in turn induce increased expression and changed glycosylation of acute phase proteins. A recent study indicated that attacks in FMF are accompanied by a rise of plasma concentrations of serum amyloid A (SAA) and C reactive protein (CRP), which remain significantly raised during remission relative to healthy controls. Another study suggested that obligatory heterozygotes also display an inflammatory acute phase response. OBJECTIVE To determine the state of inflammation in homozygotic and heterozygotic MEFV genotypes. METHODS CRP and SAA were studied by enzyme linked immunosorbent assay (ELISA). The glycosylation of the acute phase protein, α1 -acid glycoprotein (AGP), was visualised with crossed affinoimmunoelectrophoresis with concanavalin A as diantennary glycan-specific component and Aleuria aurantia lectin as fucose-specific affinity component. RESULTS FMF attacks were associated with an increase (p<0.05) in the serum inflammation parameters CRP, SAA, and AGP. The glycosylation of AGP showed an increase (p<0.05) in fucosylated AGP glycoforms, whereas the branching of the glycans remained unaffected. The glycosylation of AGP in the MEFV carrier group, compared with that in a healthy control group, was characterised by a significant increase (p<0.05) in branching of the glycans, whereas the fucosylation remained unaffected. CONCLUSION The findings suggest an FMF-specific release of cytokines, resulting in a different glycosylation of AGP between a homozygotic and heterozygotic MEFV genotype.</description><identifier>ISSN: 0003-4967</identifier><identifier>EISSN: 1468-2060</identifier><identifier>DOI: 10.1136/ard.60.8.777</identifier><identifier>CODEN: ARDIAO</identifier><language>eng</language><publisher>Kidlington: Elsevier Limited</publisher><subject>Blood ; Cytokines ; Diabetes ; Fever ; Inflammation ; Proteins</subject><ispartof>Annals of the rheumatic diseases, 2001-08, Vol.60 (8), p.777</ispartof><rights>Copyright: 2001 Annals of the Rheumatic Diseases</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids></links><search><creatorcontrib>Poland, D C W</creatorcontrib><creatorcontrib>Drenth, J P H</creatorcontrib><creatorcontrib>Rabinovitz, E</creatorcontrib><creatorcontrib>Livneh, A</creatorcontrib><creatorcontrib>Bijzet, J</creatorcontrib><creatorcontrib>van het Hof, B</creatorcontrib><creatorcontrib>van Dijk, W</creatorcontrib><title>Specific glycosylation of [alpha]1-acid glycoprotein characterises patients with familial Mediterranean fever and obligatory carriers of MEFV</title><title>Annals of the rheumatic diseases</title><description>BACKGROUND Familial Mediterranean fever (FMF) is a periodic febrile disorder, characterised by fever and serositis. The acute phase response during attacks of FMF results from the release of cytokines, which in turn induce increased expression and changed glycosylation of acute phase proteins. A recent study indicated that attacks in FMF are accompanied by a rise of plasma concentrations of serum amyloid A (SAA) and C reactive protein (CRP), which remain significantly raised during remission relative to healthy controls. Another study suggested that obligatory heterozygotes also display an inflammatory acute phase response. OBJECTIVE To determine the state of inflammation in homozygotic and heterozygotic MEFV genotypes. METHODS CRP and SAA were studied by enzyme linked immunosorbent assay (ELISA). The glycosylation of the acute phase protein, α1 -acid glycoprotein (AGP), was visualised with crossed affinoimmunoelectrophoresis with concanavalin A as diantennary glycan-specific component and Aleuria aurantia lectin as fucose-specific affinity component. RESULTS FMF attacks were associated with an increase (p<0.05) in the serum inflammation parameters CRP, SAA, and AGP. The glycosylation of AGP showed an increase (p<0.05) in fucosylated AGP glycoforms, whereas the branching of the glycans remained unaffected. The glycosylation of AGP in the MEFV carrier group, compared with that in a healthy control group, was characterised by a significant increase (p<0.05) in branching of the glycans, whereas the fucosylation remained unaffected. CONCLUSION The findings suggest an FMF-specific release of cytokines, resulting in a different glycosylation of AGP between a homozygotic and heterozygotic MEFV genotype.</description><subject>Blood</subject><subject>Cytokines</subject><subject>Diabetes</subject><subject>Fever</subject><subject>Inflammation</subject><subject>Proteins</subject><issn>0003-4967</issn><issn>1468-2060</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNqNjc1KxDAUhYMoWH92PsAF162JHZK6lhnczMrBjchwTW-md4hJTTJKH8J3tqIP4OpwON_hE-JKyUapVt9g6hstm64xxhyJSi10V99KLY9FJaVs68WdNqfiLOf9XGWnukp8PY5k2bGFnZ9szJPHwjFAdPCMfhzwRdVouf-dxxQLcQA7YEJbKHGmDON8oVAyfHIZwOEbe0YPa-p5RhIGwgCOPigBhh7iq-cdlpgmsJgSU8o_uvVy9XQhThz6TJd_eS6uV8vN_UM9i98PlMt2Hw8pzNNWGdNJbZTR7f-ob-m5XHA</recordid><startdate>20010801</startdate><enddate>20010801</enddate><creator>Poland, D C W</creator><creator>Drenth, J P H</creator><creator>Rabinovitz, E</creator><creator>Livneh, A</creator><creator>Bijzet, J</creator><creator>van het Hof, B</creator><creator>van Dijk, W</creator><general>Elsevier Limited</general><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BTHHO</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9-</scope><scope>K9.</scope><scope>LK8</scope><scope>M0R</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope></search><sort><creationdate>20010801</creationdate><title>Specific glycosylation of [alpha]1-acid glycoprotein characterises patients with familial Mediterranean fever and obligatory carriers of MEFV</title><author>Poland, D C W ; Drenth, J P H ; Rabinovitz, E ; Livneh, A ; Bijzet, J ; van het Hof, B ; van Dijk, W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-proquest_journals_17780671763</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Blood</topic><topic>Cytokines</topic><topic>Diabetes</topic><topic>Fever</topic><topic>Inflammation</topic><topic>Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Poland, D C W</creatorcontrib><creatorcontrib>Drenth, J P H</creatorcontrib><creatorcontrib>Rabinovitz, E</creatorcontrib><creatorcontrib>Livneh, A</creatorcontrib><creatorcontrib>Bijzet, J</creatorcontrib><creatorcontrib>van het Hof, B</creatorcontrib><creatorcontrib>van Dijk, W</creatorcontrib><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>BMJ Journals</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>Consumer Health Database (Alumni Edition)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Consumer Health Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><jtitle>Annals of the rheumatic diseases</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Poland, D C W</au><au>Drenth, J P H</au><au>Rabinovitz, E</au><au>Livneh, A</au><au>Bijzet, J</au><au>van het Hof, B</au><au>van Dijk, W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Specific glycosylation of [alpha]1-acid glycoprotein characterises patients with familial Mediterranean fever and obligatory carriers of MEFV</atitle><jtitle>Annals of the rheumatic diseases</jtitle><date>2001-08-01</date><risdate>2001</risdate><volume>60</volume><issue>8</issue><spage>777</spage><pages>777-</pages><issn>0003-4967</issn><eissn>1468-2060</eissn><coden>ARDIAO</coden><abstract>BACKGROUND Familial Mediterranean fever (FMF) is a periodic febrile disorder, characterised by fever and serositis. The acute phase response during attacks of FMF results from the release of cytokines, which in turn induce increased expression and changed glycosylation of acute phase proteins. A recent study indicated that attacks in FMF are accompanied by a rise of plasma concentrations of serum amyloid A (SAA) and C reactive protein (CRP), which remain significantly raised during remission relative to healthy controls. Another study suggested that obligatory heterozygotes also display an inflammatory acute phase response. OBJECTIVE To determine the state of inflammation in homozygotic and heterozygotic MEFV genotypes. METHODS CRP and SAA were studied by enzyme linked immunosorbent assay (ELISA). The glycosylation of the acute phase protein, α1 -acid glycoprotein (AGP), was visualised with crossed affinoimmunoelectrophoresis with concanavalin A as diantennary glycan-specific component and Aleuria aurantia lectin as fucose-specific affinity component. RESULTS FMF attacks were associated with an increase (p<0.05) in the serum inflammation parameters CRP, SAA, and AGP. The glycosylation of AGP showed an increase (p<0.05) in fucosylated AGP glycoforms, whereas the branching of the glycans remained unaffected. The glycosylation of AGP in the MEFV carrier group, compared with that in a healthy control group, was characterised by a significant increase (p<0.05) in branching of the glycans, whereas the fucosylation remained unaffected. CONCLUSION The findings suggest an FMF-specific release of cytokines, resulting in a different glycosylation of AGP between a homozygotic and heterozygotic MEFV genotype.</abstract><cop>Kidlington</cop><pub>Elsevier Limited</pub><doi>10.1136/ard.60.8.777</doi></addata></record> |
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| subjects | Blood Cytokines Diabetes Fever Inflammation Proteins |
| title | Specific glycosylation of [alpha]1-acid glycoprotein characterises patients with familial Mediterranean fever and obligatory carriers of MEFV |
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