Biochemical Genetics

, Volume 24, Issue 11–12, pp 795–803 | Cite as

DNA sequence evidence for polymorphic forms of human serum amyloid A (SAA)

  • Barbara Kluve-Beckerman
  • George L. Long
  • Merrill D. Benson
Article

Abstract

Serum amyloid A (SAA) is an acute-phase reactant and precursor to amyloid A protein, the major constituent of the fibril deposits of reactive amyloidosis. The factors determining whether the 104-amino acid SAA molecule is converted into the 76-amino acid amyloid A protein and deposited as fibrils are not known. As an initial step toward investigating the possibility that a particular primary structure of SAA is involved in amyloid formation, we have cloned and determined the nucleotide sequence of human SAA-specific cDNAs. The first clone, selected using an oligonucleotide probe, was shown to encode the signal peptide and amino-terminal region of SAA. The cDNA of this clone served as probe in the selection of two distinct, full-length SAA cDNAs, initially differentiated by the presence (pSAA21) or absence (pSAA82) of a PstI site in the coding sequence. The complete nucleotide sequence of pSAA82 cDNA was determined. Since there appear to be multiple human SAA alleles, it is conceivable that their differential expression is important to amyloid formation.

Key words

serum amyloid A amyloidosis cDNA clone polymorphism 

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Copyright information

© Plenum Publishing Corporation 1986

Authors and Affiliations

  • Barbara Kluve-Beckerman
    • 1
  • George L. Long
    • 2
  • Merrill D. Benson
    • 1
  1. 1.Departments of Medicine and Medical Genetics, Rheumatology DivisionIndiana University School of Medicine, Richard L. Roudebush Veterans Administration Medical CenterIndianapolis
  2. 2.Division of Molecular and Cellular BiologyLilly Research LaboratoriesIndianapolis

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