Extended report
Specific glycosylation of 
1-acid glycoprotein
characterises patients with familial Mediterranean fever and obligatory
carriers of MEFV
D C W Polanda, J P H Drenthb, E Rabinovitzc, A Livnehc, J Bijzetd, B van het Hofa, W van Dijka
a Department of
Medical Chemistry, Institute for Inflammation and Inflammatory
Diseases, Faculty of Medicine, Vrije Universiteit, Amsterdam, The
Netherlands, b Department of Medicine, Division of
Gastroenterology, University Medical Centre St Radboud, Nijmegen, The
Netherlands, c Heller
Institute of Medical Research, Sheba Medical Centre, Tel Hashomer and
Sackler School of Medicine, Tel Aviv, Israel, d Division
of Rheumatology, Department of Medicine, University Hospital,
Groningen, The Netherlands
Correspondence to: Dr W Van Dijk, Department of Medical Chemistry, Institute for Immunology and Inflammatory Diseases, Faculty of Medicine, Vrije Universiteit, Van der Boechorststraat 7, 1081 BT Amsterdam, The Netherlands w.van_dijk.medchem{at}med.vu.nl
Accepted for publication 23 January
2001
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.
OBJECTIVETo determine
the state of inflammation in homozygotic and heterozygotic MEFV genotypes.
METHODSCRP and SAA
were studied by enzyme linked immunosorbent assay (ELISA). The
glycosylation of the acute phase protein, 
1-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.
RESULTSFMF 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.
CONCLUSIONThe
findings suggest an FMF-specific release of cytokines, resulting in a
different glycosylation of AGP between a homozygotic and heterozygotic
MEFV genotype.
© 2001 by Annals of the Rheumatic Diseases
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