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HnRNP CBP35.CBP67 interaction during stress response and ageing
1Institut für Physiologische Chemie, Abteilung für Angewandte Molekularbiologie, Mainz, Germany.
Mechanisms of Ageing and Development
|August 15, 1993
Summary
Stress increases nuclear carbohydrate binding proteins (CBP35) bound to CBP67 in mature rats. This association, crucial for guiding ribonucleoprotein complexes, was not detected in older rats, suggesting age-related changes in stress response.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Nuclear carbohydrate binding proteins (CBP35, CBP67, CBP70) are involved in nuclear ribonucleoprotein (RNP) complexes.
- CBP35 has domains homologous to heterogeneous nuclear RNP and beta-galactoside-specific lectins.
- CBP35 and CBP67 are proposed to facilitate RNP complex transport through the nuclear pore.
Purpose of the Study:
- To investigate the effect of stress on nuclear CBP35 and CBP67 association in mature rats.
- To examine age-related differences in the stress response of nuclear CBP35.CBP67 interactions.
Main Methods:
- Analysis of nuclear extracts from stressed and control mature rats.
- Assessment of CBP35.CBP67 binding using immobilized glucose.
- Comparison with nuclear extracts from aged rats.
Main Results:
- Stress exposure in mature rats significantly increased nuclear CBP35 bound to CBP67.
- This stress-induced CBP35.CBP67 complex was retained on immobilized glucose.
- No detectable stress response or CBP35.CBP67 association was observed in nuclear extracts from old rats.
Conclusions:
- Stress induces a measurable increase in the nuclear CBP35.CBP67 complex in mature rats.
- The absence of this response in old rats indicates potential age-related decline in nuclear transport regulation.
- Findings provide insights into the dynamic role of carbohydrate binding proteins in cellular stress responses and aging.