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[Nonenzymatic deamidation as a factor in protein aging]
Voprosy Biokhimii Mozga
|January 1, 1978
Summary
Protein amidation decreases in aging rats, linked to unstable asparagine amide groups. This deamidation may facilitate protein breakdown in aging tissues.
Area of Science:
- Biochemistry
- Gerontology
- Molecular Biology
Background:
- Protein structure and function change with age.
- Amide groups in proteins play crucial roles.
- Aging is associated with molecular alterations in tissues.
Purpose of the Study:
- To investigate age-related changes in protein amidation.
- To identify the specific amino acids involved in altered amidation.
- To explore the functional consequences of protein deamidation in aging.
Main Methods:
- Quantification of protein amidation in brain, heart, and liver fractions from young and senile rats.
- Analysis of amide group stability.
- Investigation of nonenzymatic deamidation and proteinase activity.
Main Results:
- A 15-21% decrease in protein amidation was observed in senile rats compared to young rats.
- Unstable amide groups, primarily from asparagine, were identified as responsible for the decrease.
- Deaminated proteins showed increased susceptibility to proteinase degradation.
Conclusions:
- Aging leads to a reduction in protein amidation, particularly involving asparagine residues.
- Nonenzymatic deamidation of proteins may contribute to the breakdown of aging proteins.
- These findings offer insights into the molecular mechanisms of aging.