Amyloidosis pp 61-68 | Cite as

Human Serum Amyloid Genes — Molecular Characterization

  • George H. SackJr.
  • John J. Lease

Abstract

Three clones containing human genes for serum amyloid A protein (SAA) have been isolated and characterized. Each of two clones, GSAA 1 and 2 (of 12.8 and 15.9 kilobases, respectively), contains two exons, accouting for amino acids 12–58 and 58–103 of mature SAA; the extreme 5′ termini and 5′ untranslated regions have not yet been defined but are anticipated to be close based on studies of murine SAA genes. Initial amino acid sequence comparisons show 78/89 identical residues. At 4 of the 11 discrepant residues, the amino acid specified by the codon is the same as the corresponding residue in murine SAA. Identification of regions containing coding regions has permitted use of selected subclones for blot hybridization studies of larger human SAA chromosomal gene organization. The third clone, GSAA 3 also contains SAA coding information by DNA sequence analysis but has a different organization which has not yet been fully described.

We have reported the isolation of clones of human DNA hybridizing with pRS48 — a plasmid containing a complementary DNA (cDNA) clone for murine serum amyloid A (SAA; 1, 2). We now present more detailed data confirming the identity and defining some of the organizational features of these clones.

Keywords

Codon Nucleoside Triphosphate Amyloidosis Photography 

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References

  1. 1.
    G. H. Sack, Jr., Gene 21, 19 (1983).PubMedCrossRefGoogle Scholar
  2. 2.
    J. F. Morrow, R. S. Stearman, C. G. Peltzman, and D. A. Potter, Proc. Natl. Acad. Sci. U.S.A., 78, 4718 (1981).PubMedCrossRefGoogle Scholar
  3. 3.
    K. J. Danna, G. H. Sack, Jr., and D. Nathans, J. Mol. Biol., 78, 363 (1973).PubMedCrossRefGoogle Scholar
  4. 4.
    E. M. Southern, J. Mol. Biol., 98, 503 (1975).PubMedCrossRefGoogle Scholar
  5. 5.
    P. H. Schreier and R. Cortese, J. Mol. Biol., 129, 169 (1979).PubMedCrossRefGoogle Scholar
  6. 6.
    A. J. H. Smith, in: Methods in Enzymology (L. Grossman and K. Moldave, eds.), New York (1980), p. 65, 560.Google Scholar
  7. 7.
    M. Zasloff and T. Santos, Proc. Natl. Acad. Sci. U.S.A., 77, 5668 (1980).PubMedCrossRefGoogle Scholar
  8. 8.
    R. M. Lawn, E. F. Fritsch, R. C. Parker, G. Blake, and T. Maniatis, Cell, 15, 1157 (1978).PubMedCrossRefGoogle Scholar
  9. 9.
    E. P. Benditt, N. Eriksen, M. A. Hermodson, and L. H. Ericsson, FEBS Lett., 19, 169 (1971).PubMedCrossRefGoogle Scholar
  10. 10.
    D. Ein, S. Kimura, W. D. Terry, J. Magnotta, and G. G. Glenner, J. Biol. Chem., 247, 5653 (1972).PubMedGoogle Scholar
  11. 11.
    M. Levin, E. C. Franklin, B. Frangione, and M. Pras, J. Clin. Invest., 51, 2773 (1972).PubMedCrossRefGoogle Scholar
  12. 12.
    L. L. Bausserman, P. N. Herbert, and K. P. W. J. McAdam, J. Exp. Med., 152, 641 (1980).PubMedCrossRefGoogle Scholar
  13. 13.
    G. Husby and K. Sletten, in: Amyloid and Amyloidosis (G. G. Glenner, P. P. e Costa, and A. F. deFreitas, eds. ), Amsterdam (1980), p. 266.Google Scholar
  14. 14.
    G. Marhaug and G. Husby, Clin. Exp. Immunol., 46, 97 (1981).Google Scholar
  15. 15.
    P. Westermark, Biochim. Biophys. Acta, 701, 19 (1982).PubMedCrossRefGoogle Scholar
  16. 16.
    K. Sletten and G. Husby, Eur. J. Biochem., 41, 117 (1974).PubMedCrossRefGoogle Scholar
  17. 17.
    R. F. Anders, J. B. Natvig, K. Sletten, G. Husby, and K. Nordstoga, J. Immunol., 118, 229 (1977).PubMedGoogle Scholar
  18. 18.
    P. C. Gorevic, Y. Levo, B. Frangione, and E. C. Franklin, J. Immunol., 121, 138 (1978).PubMedGoogle Scholar
  19. 19.
    R. S. Stearman, C. A. Lowell, W. R. Pearson, and J. F. Morrow, Ann. N. Y. Acad. Sci., 389, 106 (1982).PubMedCrossRefGoogle Scholar
  20. 20.
    S. M. Mount, Nucl. Acids Res., 10, 459 (1982).PubMedCrossRefGoogle Scholar
  21. 21.
    C. A. Lowell, J. F. Morrow, personal communication.Google Scholar

Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • George H. SackJr.
    • 1
    • 2
    • 3
    • 4
    • 5
  • John J. Lease
    • 1
    • 2
    • 3
    • 4
    • 5
  1. 1.Department of MedicineThe John Hopkins University School of MedicineUSA
  2. 2.Department of Biological ChemistryThe John Hopkins University School of MedicineUSA
  3. 3.Department of OrthopedicsThe John Hopkins University School of MedicineUSA
  4. 4.Department of PediatricsThe John Hopkins University School of MedicineUSA
  5. 5.The John F. Kennedy InstituteBaltimoreUSA

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