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A novel amyloid fibril protein isolated from senescence-accelerated mice
Abstract:
A protein was isolated from amyloid fibrils extracted from the liver of an inbred strain of mice (senescence-accelerated mouse) characterized by a high frequency of age-associated systemic amyloidosis. This 5200-dalton protein has a different electrophoretic mobility from the murine protein AA. Its amino acid composition also differs from that of murine protein AA and from the amyloid protein in SJL/J, the only strain for which the spontaneous occurring amyloid has been characterized biochemically and immunochemically. Sequence analysis of the protein also revealed a blocked N-terminus. Immunochemically, the protein did not react with antisera against mouse immunoglobulin components. The antiserum against the protein did not react with murine protein AA, mouse immunoglobulin components, or with mouse normal liver protein. Thus, we have characterized an amyloid protein that is distinguishable from previously reported murine amyloid proteins and is not related to immunoglobulins. The possible relationship between this protein, designated ASSAM, and ASc in human senile cardiac amyloidosis is considered.
Insights
Researchers isolated a novel amyloid protein, ASSAM, from the livers of aging mice with systemic amyloidosis. This protein is distinct from known murine amyloid proteins and immunoglobulins.
Area of Science:
- Biochemistry
- Immunology
- Gerontology
Background:
- Systemic amyloidosis is common in senescence-accelerated mice.
- Amyloid protein characterization is crucial for understanding age-associated diseases.
- Previous murine amyloid protein studies focused on specific strains.
Purpose of the Study:
- To isolate and characterize a novel amyloid protein from senescence-accelerated mice.
- To determine if this protein is related to known murine amyloid proteins or immunoglobulins.
- To investigate potential links to human amyloidosis.
Main Methods:
- Protein isolation from liver amyloid fibrils.
- Electrophoretic mobility analysis.
- Amino acid composition and sequence analysis.
- Immunochemical assays using antisera.
Main Results:
- A 5200-dalton protein, designated ASSAM, was isolated.
- ASSAM exhibits different electrophoretic mobility and amino acid composition compared to murine protein AA.
- Sequence analysis revealed a blocked N-terminus.
- ASSAM showed no cross-reactivity with murine protein AA, immunoglobulins, or normal liver proteins.
Conclusions:
- ASSAM is a novel amyloid protein distinct from previously identified murine amyloid proteins.
- ASSAM is not related to immunoglobulins.
- Further research is needed to explore ASSAM's relationship with human senile cardiac amyloidosis (ASc).