Specific glycosylation of α1-acid glycoprotein characterises patients with familial Mediterranean fever and obligatory carriers of MEFV

• Published in: Annals of the rheumatic diseases 2001-08, Vol.60 (8), p.777-780
• Main Authors: Poland, D C W, Drenth, J P H, Rabinovitz, E, Livneh, A, Bijzet, J, van het Hof, B, van Dijk, W
• Format: Article
• Language: English
• Subjects: Biological and medical sciences; C reactive protein; Extended Report; familial Mediterranean fever; Medical sciences; Sarcoidosis. Granulomatous diseases of unproved etiology. Connective tissue diseases. Elastic tissue diseases. Vasculitis; serum amyloid A; α1-acid glycoprotein
• ISSN: 0003-4967; 1468-2060
• DOI: 10.1136/ard.60.8.777

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