Influence of Polymorphism on Glycosylation of Serum Amyloid A4 Protein

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...

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Main Authors: Toshiyuki Yamada, Jyunji Sato, Kazuhiko Kotani, Masafumi Tanaka
Format: Article
Language:English
Published: Wiley 2014-01-01
Series:Biochemistry Research International
Online Access:http://dx.doi.org/10.1155/2014/527254
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author Toshiyuki Yamada
Jyunji Sato
Kazuhiko Kotani
Masafumi Tanaka
author_facet Toshiyuki Yamada
Jyunji Sato
Kazuhiko Kotani
Masafumi Tanaka
author_sort Toshiyuki Yamada
collection DOAJ
description 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.
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publishDate 2014-01-01
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series Biochemistry Research International
spelling doaj-art-dfdf911fdcb64898a07b18ebee68a6dd2025-02-03T01:22:20ZengWileyBiochemistry Research International2090-22472090-22552014-01-01201410.1155/2014/527254527254Influence of Polymorphism on Glycosylation of Serum Amyloid A4 ProteinToshiyuki Yamada0Jyunji Sato1Kazuhiko Kotani2Masafumi Tanaka3Department of Clinical Laboratory Medicine, Jichi Medical University, Tochigi 329-0498, JapanDepartment of Clinical Laboratory Medicine, Jichi Medical University, Tochigi 329-0498, JapanDepartment of Clinical Laboratory Medicine, Jichi Medical University, Tochigi 329-0498, JapanDepartment of Biophysical Chemistry, Kobe Pharmaceutical University, Hyogo 658-8558, JapanSerum 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.http://dx.doi.org/10.1155/2014/527254
spellingShingle Toshiyuki Yamada
Jyunji Sato
Kazuhiko Kotani
Masafumi Tanaka
Influence of Polymorphism on Glycosylation of Serum Amyloid A4 Protein
Biochemistry Research International
title Influence of Polymorphism on Glycosylation of Serum Amyloid A4 Protein
title_full Influence of Polymorphism on Glycosylation of Serum Amyloid A4 Protein
title_fullStr Influence of Polymorphism on Glycosylation of Serum Amyloid A4 Protein
title_full_unstemmed Influence of Polymorphism on Glycosylation of Serum Amyloid A4 Protein
title_short Influence of Polymorphism on Glycosylation of Serum Amyloid A4 Protein
title_sort influence of polymorphism on glycosylation of serum amyloid a4 protein
url http://dx.doi.org/10.1155/2014/527254
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