Literature DB >> 14640028

Slower clearance of human SAA1.5 in mice: implications for allele specific variation of SAA concentration in human.

Toshiyuki Yamada1, Atsufumi Wada.   

Abstract

Serum amyloid A (SAA), the serum precursor of the fibrillar component (AA proteins) in reactive amyloid deposits, is a multigene product. SAA1, the prominent acute phase isotype in serum and also the dominant fibril precursor, has several allelic variants. In Japan, each of the three major alleles (1.1, 1.3 and 1.5) appears with approximately equal frequency. Recent research suggested that allele 1.5 has a positive influence on the serum SAA concentration. To clarify this, in the present study, recombinant human SAA1.1, SAA1.3 and SAA1.5 were produced in an E. coli expression system and those species of reconstituted high density lipoprotein were injected into mice to examine plasma clearance. SAA1.5 disappeared from plasma more slowly than the other two isotypes. This may account for the positive influence of allele 1.5 on the serum SAA concentration.

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Year:  2003        PMID: 14640028     DOI: 10.3109/13506120308998996

Source DB:  PubMed          Journal:  Amyloid        ISSN: 1350-6129            Impact factor:   7.141


  1 in total

1.  Influence of polymorphism on glycosylation of serum amyloid a4 protein.

Authors:  Toshiyuki Yamada; Jyunji Sato; Kazuhiko Kotani; Masafumi Tanaka
Journal:  Biochem Res Int       Date:  2014-05-15
  1 in total

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