Abstract
PDF (573 K)
E-mail Article
Add to my Quick Links
Cited By in Scopus (13)
doi:10.1016/0014-5793(91)80387-I 
Copyright © 1991 Published by Elsevier Science B.V. All rights reserved.
The transthyretin cDNA sequence is normal in transthyretin-derived senile systemic amyloidosis
L. Christmansona, C. Betsholtza, Å. Gustavssonb, B. Johanssonc, K. Slettend and P. Westermarkb, 
Received 31 January 1991.
Abstract
A variety of mutations leading to amino acid substitutions have been described in the transthyretin gene in association with different familial amyloidoses and have been implicated to be involved in the pathogenesis of amyloid deposits. However, there has been disagreement whether or not a transthyretin mutation is present in the most common form of transthyretin-derived amyloid, namely senile systemic amyloidosis. Therefore, the cDNA sequence of liver transthyretin was determined in a 91-year-old patient with typical senile systemic amyloidosis. This sequence was completely normal and lacked any variation. We conclude that in senile systemic amyloidosis factors other than the presence of a sequentially variant transthyretin must determine the amyloid fibril formation.
Author Keywords: Transthyretin; Prealbumin; cDNA; Polymerase chain reaction
Abbreviations: AA, fibril protein in secondary systemic amyloidosis; AL, fibril protein in primary (plasma cell dyscrasia-associated) amyloid; ATTR, amyloid fibril protein derived from TTR; FAP, familial amyloidotic polyneuropathy; SSA, senile systemic amyloidosis; TTR, transthyretin
References
1. E.D. Eanes and G.G. Glenner J. Histochem. Cytochem. 16 (1968), pp. 673–677. View Record in Scopus | Cited By in Scopus (148)
2. P.P. Costa, A.S. Figueira and F.R. Bravo Proc. Natl. Acad. Sci. USA 75 (1978), pp. 4499–4503. View Record in Scopus | Cited By in Scopus (86)
3. M. Nakazato, K. Kangawa, N. Minamino, S. Tawara, H. Matsuo and S. Araki Bichem. Biophys. Res. Commun. 123 (1984), pp. 921–928. Abstract | 
PDF (368 K)
| View Record in Scopus | Cited By in Scopus (7)
4. F.E. Dwulet and M.D. Benson J. Clin. Invest. 78 (1986), pp. 880–886. View Record in Scopus | Cited By in Scopus (36)
5. M. Nordlie, K. Sletten, G. Husby and P.J. Ranlöv Scand. J. Immunol. 27 (1988), pp. 119–122. View Record in Scopus | Cited By in Scopus (14)
6. K. Sletten, P. Westermark and J.B. Natvig Scand. J. Immunol. 12 (1980), pp. 503–506. View Record in Scopus | Cited By in Scopus (12)
7. G.G. Cornwell, III, K. Sletten, B. Johansson and P. Westermark Biochem. Biophys. Res. Commun. 154 (1988), pp. 648–653. Abstract | Article | PDF (526 K)
| View Record in Scopus | Cited By in Scopus (61)
8. S. Tawara, M. Nakazato, K. Kangawa, H. Matsuo and S. Araki Biochem. Biophys. Res. Commun. 116 (1983), pp. 880–888. Abstract | PDF (475 K)
| View Record in Scopus | Cited By in Scopus (99)
9. M.R. Wallace, F.E. Dwulet, P.M. Conneally and M.D. Benson J. Clin. Invest. 78 (1986), pp. 6–12. View Record in Scopus | Cited By in Scopus (31)
10. M.R. Wallace, F.E. Dwulet, E.C. Williams, P.M. Conneally and M.D. Benson J. Clin. Invest. 81 (1988), pp. 189–193. View Record in Scopus | Cited By in Scopus (7)
11. J.R. Wright and E. Calkins J. Am. Geriatr. Soc. 23 (1975), pp. 97–103. View Record in Scopus | Cited By in Scopus (9)
12. P. Pitkänen, P. Westermark and G.G. Cornwell, III Am. J. Path. 117 (1984), pp. 391–399. View Record in Scopus | Cited By in Scopus (39)
13. P.D. Gorevic, F.C. Prelli, J. Wright, M. Pras and B. Frangione J. Clin. Invest. 83 (1989), pp. 836–843. View Record in Scopus | Cited By in Scopus (34)
14. P. Felding, G. Fex, P. Westermark, B.-O. Olofsson, P. Pitkänen and L. Benson Scand. J. Immunol. 21 (1985), pp. 133–140. View Record in Scopus | Cited By in Scopus (12)
15. P. Westermark, K. Sletten, B. Johansson and G.G. Cornwell, III Proc. Natl. Acad. Sci. USA 87 (1990), pp. 2843–2845. View Record in Scopus | Cited By in Scopus (199)
16. G. Blobel and B. Dobberstein J. Cell. Biol. 67 (1975), pp. 835–851. View Record in Scopus | Cited By in Scopus (279)
17. H. Towbin, T. Staehelin and J. Gordon Proc. Natl. Acad. Sci. USA 76 (1983), pp. 4350–4354.
18. C. Auffrey and F. Rorgeon Eur. J. Biochem. 107 (1980), pp. 303–314.
19. S. Mita, S. Maeda, K. Shimada and S. Araki Biochem. Biophys. Res. Commun. 124 (1984), pp. 558–564. Abstract | Article | PDF (364 K)
| View Record in Scopus | Cited By in Scopus (22)
20. L.-G. Öfverstedt, K. Hammarström, N. Balgobin, S. Hjertén, U. Pettersson and J. Chattopadyaya Biochim. Biophys. Acta 782 (1984), pp. 120–126. Abstract | PDF (617 K)
| View Record in Scopus | Cited By in Scopus (24)
21. F. Sanger, S. Micklen and A.R. Coulson Proc. Natl. Acad. Sci. USA 74 (1977), pp. 5463–5467. View Record in Scopus | Cited By in Scopus (20500)
22. H. Sasaki, N. Yoshioka, Y. Takagi and Y. Sakaki Gene 37 (1985), pp. 191–197. View Record in Scopus | Cited By in Scopus (31)
23. F.E. Dwulet and M.D. Benson Proc. Natl. Acad. Sci. USA 81 (1984), pp. 694–698. View Record in Scopus | Cited By in Scopus (32)
24. P. Westermark, K. Sletten and B.-O. Olofsson Clin. Exp. Immunol. 69 (1987), pp. 695–701. View Record in Scopus | Cited By in Scopus (7)
25. D.R. Jacobson, P.D. Gorevic and J.N. Buxbaum Am. J. Hum. Genet. 47 (1990), pp. 127–136. View Record in Scopus | Cited By in Scopus (20)
26. Nichols, W.C., Snyder, E.L., Liepnieks, J.J. and Benson, M.D. in: Familial and Other Transthyretin Related Disorders (Costa, P.P., Falcao de Freitas, A. and Saraiva, M.J.M., Eds) Porto, Arquivos Medicos (in press).
27. Saraiva, M.J.M., Sherman, W., Kyle, R., Gertz, M., Costa, P.P., Figueira, A. and Gawinowicz, M. in: Familial Amyloidotic Polyneuropathy and Other Transthyretin Related Disorders (Costa, P.P., Falcao de Freitas, A. and Saraiva, M.J.M., Eds) Porto, Arquivos Medicos (in press).
