Influence of polymorphism on glycosylation of serum amyloid a4 protein
Toshiyuki Yamada1, Jyunji Sato1, Kazuhiko Kotani1
1Department of Clinical Laboratory Medicine, Jichi Medical University, Tochigi 329-0498, Japan.
Abstract:
Serum amyloid A4 (SAA4) is a constitutive apolipoprotein of high-density lipoprotein. It exhibits N-linked glycosylation in its second half. There are both glycosylated and nonglycosylated forms in plasma and the ratio of these two forms varies among individuals. This study was conducted to examine the influence of genetic polymorphism of SAA4 on its glycosylation status. In 55 healthy subjects, SAA4 polymorphism was analyzed by PCR combined direct sequencing and its glycosylation status was analyzed by immunoblotting. The results showed that the percentage of glycosylation in subjects with amino acid substitutions at positions 71 and/or 84 was significantly (P < 0.05) higher than that in subjects with the wild type. The polymorphism had no influence on the plasma concentration of SAA4. These findings suggest that the changes in protein structures alter the efficiency of glycosylation in the SAA4 molecule. The functional implication of this should be of interest.
More Related Videos
Related Concept Videos
Proteoglycans
Protein Glycosylation
Glycosylation occurs in...
Oligosaccharide Assembly
Multiple sugar molecules that may or may...
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Amyloid Fibrils
Pharmacogenetics of Drug Targets: β₂-Adrenergic Receptors, Apo E, Thymidylate Synthase


