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Journal of Clinical Laboratory Analysis logoLink to Journal of Clinical Laboratory Analysis
. 1998 Dec 7;11(6):363–368. doi: 10.1002/(SICI)1098-2825(1997)11:6<363::AID-JCLA10>3.0.CO;2-U

Automated measurement of a constitutive isotype of serum amyloid A/SAA4 and comparison with other apolipoproteins

Toshiyuki Yamada 1,, Atsufumi Wada 1, Tetsuji Yamaguchi 1, Yoshihisa Itoh 1, Tadashi Kawai 1
PMCID: PMC6760705  PMID: 9406058

Abstract

A constitutive isotype of serum amyloid A (SAA4) is present mostly in high density lipoprotein (HDL) and a little in other lipoproteins. In this study, we developed an automated method for measuring SAA4 concentration in serum by kinetic nephelometry of anti‐SAA4 antibody‐coated latex agglutination. Rabbit antibodies generated by immunization of recombinant SAA4 were found to have no apparent reactivity with acute phase SAA. The values determined by this method and by the previous enzyme immunoassay showed good agreement (r=0.862). Serum SAA4 values of 26 healthy adults ranged from 37–109 mg/L (mean; 62 mg/L). Their SAA4 concentrations were not significantly related with those of apolipoprotein A‐I, A‐II, B, C‐II, C‐III or E. Also, SAA4 did not correlate with cholesterol in preparation after removal of very low density lipoprotein and low density lipoprotein. These suggest the unique behavior of SAA4 in lipoprotein metabolism, while what contributes to variation of SAA4 levels in serum, especially in HDL, remains to be clarified. J. Clin. Lab. Anal. 11:363–368, 1997. © 1997 Wiley‐Liss, Inc.

Keywords: high density lipoprotein, recombinant protein, latex agglutination, nephelometry, acute phase

References

  • 1. Husby G, Marhaug G, Dowton B, Sletten K, Sipe JD: Serum amyloid A (SAA). biochemistry, genetics and the pathogenesis of AA amyloidosis. Amyloid Int J Exp Clin invest 1: 119–137, 1994. [Google Scholar]
  • 2. Malle E, de Beer FC: Human serum amyloid A (SAA) protein: a prominent acute‐phase reactant for clinical practice. Eur J Clin invest 26: 427–435, 1996. [DOI] [PubMed] [Google Scholar]
  • 3. Dwulet FE, Wallace DK, Benson MD: Amino acid structures of multiple forms of amyloid‐related serum protein SAA from a single individual. Biochemistry 27: 1677–1682, 1988. [DOI] [PubMed] [Google Scholar]
  • 4. Whitehead AS, de Beer MC, Rits M, Lelias JM, Lane WS, de Beer FC: Identification of novel members of serum amyloid A protein superfamily as constitutive apolipoproteins of high density lipoprotein. J Biol Chem 267: 3862–3867, 1992. [PubMed] [Google Scholar]
  • 5. Baba S, Takahashi T, Kasama T, Fujie M, Shirasawa H: A novel polymorphism of human serum amyloid A protein, SAA1, is characterized by alanines at both residues 52 and 57. Biochim Biophys Acta 1180: 195–200, 1992. [DOI] [PubMed] [Google Scholar]
  • 6. Badolato R, Wang JM, Murphy WJ, Lloyd AR, Michiel DF, Bausserman LL, Kelvin DJ, Oppenheim JJ: Serum amyloid A is a chemoattractant: induction of migration, adhesion, and tissue infiltration of monocytes and polymorphonuclear leukocytes. J Exp Med 180: 203–210, 1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 7. Mitchell TI, Coon CI, Brinckerhoff CE: Serum amyloid A (SAA3) produced by rabbit synovial fibroblasts treated with phorbol esters or interleukin 1 induces synthesis of collagenase and is neutralized with specific antiserum. J Clin invest 87: 1177–1185, 1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 8. Zimlichman S, Danon A, Nathan I, Moses G, Shaikin‐Kestenbaum R: Serum amyloid A, an acute phase protein, inhibits platelet activation. J Lab Clin invest 116: 180–186, 1990. [PubMed] [Google Scholar]
  • 9. Kisilevsky R, Subrahmanyan L: Serum amyloid A changes high density lipoproteins cellular affinity. Lab invest 66: 778–785, 1992. [PubMed] [Google Scholar]
  • 10. Yamada T, Kluve‐Beckerman B, Kuster WM, Liepnieks JJ, Benson MD: Measurement of serum amyloid A4 (SAA4). its constitutive presence in serum. Amyloid Int J Exp Clin invest 1: 114–118, 1994. [Google Scholar]
  • 11. Yamada T, Kluve‐Beckerman B, Liepnieks JJ, Benson MD: Fibril formation from recombinant human serum amyloid A. Biochim Biophys Acta 1226: 323–329, 1994. [DOI] [PubMed] [Google Scholar]
  • 12. de Beer MC, Yuan T, Kindy MS, Asztalos BF, Roheim PS, de Beer FC: Characterization of constitutive human serum amyloid A protein (SAA4) as an apolipoprotein. J Lipid Res 36: 526–534, 1995. [PubMed] [Google Scholar]
  • 13. Yamada T, Miida T, Itoh Y, Kawai T, Benson MD: Characteriztion of serum amyloid A4 as a plasma lipoprotein. Clin Chim Acta 251: 105–112, 1996. [DOI] [PubMed] [Google Scholar]
  • 14. Yamada T, Nomata Y, Sugita O, Okada M: A rapid method for measuring serum amyloid A protein by latex agglutination nephelometric immunoassay. Ann Clin Biochem 30: 72–76, 1993. [DOI] [PubMed] [Google Scholar]
  • 15. Hatch FT, Lee RS: Practical methods for plasma lipoprotein analysis. Adv Lipid Res 6: 2–68, 1968. [PubMed] [Google Scholar]
  • 16. Kumon Y, Loose LD, Birbara CA, Sipe JD: Rheumatoid arthritis exhibits reduced acute phase and enhanced constitutive serum amyloid A protein in synovial fluid relative to serum. A comparison with C‐reactive protein. J Rheumatol 24: 14–19, 1997. [PubMed] [Google Scholar]

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