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Differential Regulation of Human Serum Amyloid a Isoforms

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Amyloid and Amyloidosis 1990

Abstract

Significantly more SAA1 than SAA2 is routinely purified from the plasma of patients studied by this laboratory. Investigating the reason for this disparity, we have compared mRNA levels for SAAl and SAA2 in a patient whose ratio of purified SAA1/SAA2 was approximately six. Relative levels of SAA1 and SAA2 mRNA were determined by Northern analysis using isotype-specific oligonucleotide probes. Scanning densitometry of the resulting autoradiographs revealed a 2-fold predominance of SAA1 over SAA2 mRNA. Thus, a higher steady state level of SAA1 mRNA explains in part the predominance of the SAA1 isotype.

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References

  1. Hoffman, J.S., Ericsson, L.H., Eriksen, N., Walsh, K.A., and Benditt, P. (1984), ‘Murine tissue amyloid protein AA. NH-terminal sequence identity with only one of two serum amyloid protein (ApoSAA) gene products’, J. Exp. Med. 159, 641–646.

    Article  PubMed  CAS  Google Scholar 

  2. Meek, R.L., Hoffman, J.S., and Benditt, E.P. (1986), ‘Amyloidogenesis: One serum isotype is selectively removed from the circulation’, J. Exp. Med. 163, 499–510.

    Article  PubMed  CAS  Google Scholar 

  3. Shiroo, M., Kawahara, E., Nakanishi, I., and Migita, S. (1987), ‘Specific deposition of serum amyloid A protein 2 in the mouse’, Scand. J. Immunol. 26, 709–716.

    Article  PubMed  CAS  Google Scholar 

  4. Liepnieks, J.J., Leagre, C., Kluve-Beckerman, B., and Benson, M.D. (1990), ‘Predominance of one SAA isotype (SAAI) in human reactive amyloid’, VIth International Symposium on Amyloidosis, Oslo, Norway.

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  5. Chirgwin, J.M., Przybyla, A.E., MacDonald, R.J. and Rutter, W.J. (1979), ‘Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease’, Biochemistry 18, 5294–5299.

    Article  PubMed  CAS  Google Scholar 

  6. Kluve-Beckerman, B., Dwulet, F.E., and Benson, M.D. (1988), ‘Human serum amyloid A: Three hepatic mRNAs and the corresponding proteins in one person’, J. Clin. Invest. 82, 1670–1675.

    Article  PubMed  CAS  Google Scholar 

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© 1991 Springer Science+Business Media Dordrecht

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Kluve-Beckerman, B., Liepnieks, J., Benson, M.D. (1991). Differential Regulation of Human Serum Amyloid a Isoforms. In: Natvig, J.B., et al. Amyloid and Amyloidosis 1990. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-3284-8_31

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  • DOI: https://doi.org/10.1007/978-94-011-3284-8_31

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-5450-8

  • Online ISBN: 978-94-011-3284-8

  • eBook Packages: Springer Book Archive

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