Senile cardiac amyloid: evidence that fibrils contain a protein immunologically related to prealbumin
- PMID: 7033114
- PMCID: PMC1554963
Senile cardiac amyloid: evidence that fibrils contain a protein immunologically related to prealbumin
Abstract
Antiserum specific for human prealbumin (HPA) was studied by indirect immunofluorescence on tissue sections of cardiac ventricles containing senile cardiac amyloid. The pattern of reactivity was identical to that previously reported for an antiserum specific for protein ASc1 (formerly designated ASCA present in these tissues. Anti-HPA failed to react with isolated atrial amyloid (IAA), primary amyloid (A lambda I, A lambda IV, A lambda VI), secondary amyloid (AA), amyloid associated with medullary carcinoma of the thyroid (AEt), pancreatic amyloid associated with adult onset diabetes, cerebral amyloid present in Alzheimer's disease or lichen amyloid. THe reaction of anti-HPA was completely blocked by purified human prealbumin but was not influenced by absorption with purified human albumin or proteins extracted from any amyloid types tested. The anti-HPA reaction was also completely blocked by purified protein ASc1, and the reaction of anti-ASc1 was similarly blocked by purified HPA. These studies suggest that senile cardiac amyloid of the ASc1 type contains prealbumin or a protein antigenically closely related to this molecule.
Similar articles
-
Immunohistochemical identification and cross reactions of amyloid fibril proteins in senile heart and amyloid in familial polyneuropathy. Lack of reactivity with cerebral amyloid in Alzheimer's disease.Clin Neuropathol. 1982;1(4):172-82. Clin Neuropathol. 1982. PMID: 6301727
-
Senile cardiac amyloid: demonstration of a unique fibril protein in tissue sections.J Immunol. 1978 Apr;120(4):1385-8. J Immunol. 1978. PMID: 347002
-
Senile aortic amyloid. A third distinctive type of age-related cardiovascular amyloid.Am J Pathol. 1982 Aug;108(2):135-9. Am J Pathol. 1982. PMID: 6765856 Free PMC article.
-
[Fibril-forming proteins: the amyloidosis. New hopes for a disease that cardiologists must know].Ital Heart J Suppl. 2002 Jun;3(6):590-7. Ital Heart J Suppl. 2002. PMID: 12116807 Review. Italian.
-
Systemic amyloidosis: a review with emphasis on pathogenesis.Appl Pathol. 1985;3(1-2):55-68. Appl Pathol. 1985. PMID: 3939490 Review.
Cited by
-
Transthyretin amyloid goiter in a renal allograft recipient.Endocr Pathol. 2008 Spring;19(1):66-73. doi: 10.1007/s12022-008-9020-8. Endocr Pathol. 2008. PMID: 18369743
-
Fibril in senile systemic amyloidosis is derived from normal transthyretin.Proc Natl Acad Sci U S A. 1990 Apr;87(7):2843-5. doi: 10.1073/pnas.87.7.2843. Proc Natl Acad Sci U S A. 1990. PMID: 2320592 Free PMC article.
-
Senile systemic amyloidosis.Am J Pathol. 1984 Dec;117(3):391-9. Am J Pathol. 1984. PMID: 6507586 Free PMC article.
-
Structural Basis for Monoclonal Antibody Therapy for Transthyretin Amyloidosis.Pharmaceuticals (Basel). 2024 Sep 17;17(9):1225. doi: 10.3390/ph17091225. Pharmaceuticals (Basel). 2024. PMID: 39338387 Free PMC article. Review.
-
Amyloid of the seminal vesicles. A distinctive and common localized form of senile amyloidosis.Am J Pathol. 1983 Jan;110(1):64-9. Am J Pathol. 1983. PMID: 6849372 Free PMC article.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Medical
Molecular Biology Databases
Research Materials