Abstract
Aortic tissues from 22 elderly patients were analyzed by Congo red staining for amyloid deposits. All samples contained amyloid, which was resistant to the potassium permanganate reaction. Tryptophan was present in all amyloid deposits. The amyloid failed to react with antiserums to amyloid fibril protein ASc1 or human prealbumin, proteins previous demonstrated in generalized senile cardiac amyloid. It also differed from age-related isolated atrial amyloid, which has been shown to lack tryptophan. Deposits did not react with antiserums specific for amyloid fibril proteins of the A lambda IV, A lambda VI, AA, or AEt types. These results indicate that senile aortic amyloid is distinct from amyloid present in primary and secondary amyloidosis and appears to represent a third form of cardiovascular amyloid associated with the aging process.
Full text
PDF
Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- ADAMS C. W. A p-dimethylaminobenzaldehyde-nitrite method for the histochemical demonstration of tryptophane and related compounds. J Clin Pathol. 1957 Feb;10(1):56–62. doi: 10.1136/jcp.10.1.56. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Battaglia S., Trentini G. P. Aortenamyloidose im Erwachsenenalter. Virchows Arch A Pathol Anat Histol. 1978 Jun 2;378(2):153–159. doi: 10.1007/BF00432359. [DOI] [PubMed] [Google Scholar]
- Breathnach S. M., Melrose S. M., Bhogal B., de Beer F. C., Dyck R. F., Tennent G., Black M. M., Pepys M. B. Amyloid P component is located on elastic fibre microfibrils in normal human tissue. Nature. 1981 Oct 22;293(5834):652–654. doi: 10.1038/293652a0. [DOI] [PubMed] [Google Scholar]
- Cornwell G. G., 3rd, Husby G., Westermark P., Natvig J. B., Michaelsen T. E., Skogen B. Identification and characterization of different amyloid fibril proteins in tissue sections. Scand J Immunol. 1977;6(11):1071–1080. doi: 10.1111/j.1365-3083.1977.tb00344.x. [DOI] [PubMed] [Google Scholar]
- Cornwell G. G., 3rd, Natvig J. B., Westermark P., Husby G. Senile cardiac amyloid: demonstration of a unique fibril protein in tissue sections. J Immunol. 1978 Apr;120(4):1385–1388. [PubMed] [Google Scholar]
- Cornwell G. G., 3rd, Westermark P., Natvig J. B., Murdoch W. Senile cardiac amyloid: evidence that fibrils contain a protein immunologically related to prealbumin. Immunology. 1981 Nov;44(3):447–452. [PMC free article] [PubMed] [Google Scholar]
- Cornwell G. G., 3rd, Westermark P. Senile amyloidosis: a protean manifestation of the aging process. J Clin Pathol. 1980 Dec;33(12):1146–1152. doi: 10.1136/jcp.33.12.1146. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Puchtler H., Sweat F. Congo red as a stain for fluorescence microscopy of amyloid. J Histochem Cytochem. 1965 Nov-Dec;13(8):693–694. doi: 10.1177/13.8.693. [DOI] [PubMed] [Google Scholar]
- Sletten K., Westermark P., Natvig J. B. Senile cardiac amyloid is related to prealbumin. Scand J Immunol. 1980;12(6):503–506. doi: 10.1111/j.1365-3083.1980.tb00098.x. [DOI] [PubMed] [Google Scholar]
- Westermark P., Johansson B., Natvig J. B. Senile cardiac amyloidosis: evidence of two different amyloid substances in the ageing heart. Scand J Immunol. 1979;10(4):303–308. doi: 10.1111/j.1365-3083.1979.tb01355.x. [DOI] [PubMed] [Google Scholar]
- Westermark P., Natvig J. B., Johansson B. Characterization of an amyloid fibril protein from senile cardiac amyloid. J Exp Med. 1977 Aug 1;146(2):631–636. doi: 10.1084/jem.146.2.631. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wright J. R., Calkins E., Humphrey R. L. Potassium permanganate reaction in amyloidosis. A histologic method to assist in differentiating forms of this disease. Lab Invest. 1977 Mar;36(3):274–281. [PubMed] [Google Scholar]
- Wright J. R., Calkins E. Relationship of amyloid deposits in the human aorta to aortic atherosclerosis. A postmortem study of 100 individuals over 60 years of age. Lab Invest. 1974 Jun;30(6):767–773. [PubMed] [Google Scholar]