Abstract
Amyloid fibrils were isolated from spleen and thyroid obtained at autopsy from one patient (S.K.O.) of Jewish origin with familial amyloidotic polyneuropathy. Gel filtration on Sephadex G100 after solubilization in 5 M guanidine HCl yielded three major components with 14,000, 9,000, and 5,000 mol wt, respectively. The two larger components shared antigenic determinants with human prealbumin. Amino acid analysis and amino terminal sequence studies revealed the 14,000- mol wt protein to be an intact prealbumin subunit. The 9,000-mol wt fragment obtained in highest yield encompassed the region from position 49-127 and the 5,000 mol wt fraction encompassed the amino terminal of prealbumin (position 1-48). An amino acid substitution (Gly/Thr) was detected at position 49, where enzymatic cleavage occurred. Thus, several prealbumin-derived fragments, predominantly the carboxyl end, constitute the amyloid fibrils in a heredofamilial amyloidosis syndrome of dominant inheritance.
Full Text
The Full Text of this article is available as a PDF (341.3 KB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Andrade C., Araki S., Block W. D., Cohen A. S., Jackson C. E., Kuroiwa Y., Nissim J., Sohar E., McKusick V. A., Van Allen M. W. Hereditary amyloidosis. Arthritis Rheum. 1970 Nov-Dec;13(6):902–915. doi: 10.1002/art.1780130622. [DOI] [PubMed] [Google Scholar]
- Benson M. D. Partial amino acid sequence homology between an heredofamilial amyloid protein and human plasma prealbumin. J Clin Invest. 1981 Apr;67(4):1035–1041. doi: 10.1172/JCI110114. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Blake C. C., Geisow M. J., Oatley S. J., Rérat B., Rérat C. Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 A. J Mol Biol. 1978 May 25;121(3):339–356. doi: 10.1016/0022-2836(78)90368-6. [DOI] [PubMed] [Google Scholar]
- Chou P. Y., Fasman G. D. Prediction of protein conformation. Biochemistry. 1974 Jan 15;13(2):222–245. doi: 10.1021/bi00699a002. [DOI] [PubMed] [Google Scholar]
- Costa P. P., Figueira A. S., Bravo F. R. Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy. Proc Natl Acad Sci U S A. 1978 Sep;75(9):4499–4503. doi: 10.1073/pnas.75.9.4499. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Glenner G. G. Amyloid deposits and amyloidosis. The beta-fibrilloses (first of two parts). N Engl J Med. 1980 Jun 5;302(23):1283–1292. doi: 10.1056/NEJM198006053022305. [DOI] [PubMed] [Google Scholar]
- Glenner G. G., Terry W., Harada M., Isersky C., Page D. Amyloid fibril proteins: proof of homology with immunoglobulin light chains by sequence analyses. Science. 1971 Jun 11;172(3988):1150–1151. doi: 10.1126/science.172.3988.1150. [DOI] [PubMed] [Google Scholar]
- Kanda Y., Goodman D. S., Canfield R. E., Morgan F. J. The amino acid sequence of human plasma prealbumin. J Biol Chem. 1974 Nov 10;249(21):6796–6805. [PubMed] [Google Scholar]
- Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
- Levin M., Franklin E. C., Frangione B., Pras M. The amino acid sequence of a major nonimmunoglobulin component of some amyloid fibrils. J Clin Invest. 1972 Oct;51(10):2773–2776. doi: 10.1172/JCI107098. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Michaelsen T. E., Frangione B., Franklin E. C. Primary structure of the "hinge" region of human IgG3. Probable quadruplication of a 15-amino acid residue basic unit. J Biol Chem. 1977 Feb 10;252(3):883–889. [PubMed] [Google Scholar]
- Pras M., Schubert M., Zucker-Franklin D., Rimon A., Franklin E. C. The characterization of soluble amyloid prepared in water. J Clin Invest. 1968 Apr;47(4):924–933. doi: 10.1172/JCI105784. [DOI] [PMC free article] [PubMed] [Google Scholar]