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[Protein amidation in the aging organism]
Ukrainskii Biokhimicheskii Zhurnal (1978)
|November 1, 1979
Summary
Aging causes deamidation of asparagine in rat proteins, making them more susceptible to proteinase attack. Glutamine levels remain stable, but decreased amidation degree contributes to age-related protein degradation.
Area of Science:
- Biochemistry
- Molecular Biology
- Gerontology
Background:
- Protein structure and function are crucial for cellular processes.
- Ageing is associated with molecular changes in proteins.
- Protein amide groups play roles in protein stability and interactions.
Purpose of the Study:
- To investigate the role of protein amide groups in organism ageing.
- To examine age-related changes in asparagine and glutamine deamidation in rat tissues.
- To understand the impact of amidation degree on protein susceptibility to proteolysis during ageing.
Main Methods:
- Analysis of protein amide groups (asparagine and glutamine) in water-soluble and water-insoluble proteins.
- Comparative study of protein from young and old rats (brain, liver, heart).
- Assessment of proteinase activity on tissue proteins from different age groups.
Main Results:
- Asparagine deamidation increases in rat brain, liver, and heart proteins with ageing.
- Glutamine content remains unchanged in old rat tissues compared to young rats.
- Proteins from old rats are more readily degraded by broad-specificity proteinases than proteins from young rats.
- Reduced amidation degree of old animal proteins contributes to increased non-specific proteinase attack.
Conclusions:
- Ageing-associated asparagine deamidation reduces protein stability.
- Decreased protein amidation degree in aged rats enhances susceptibility to non-specific proteinases.
- These molecular changes in proteins may contribute to the ageing process.