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Modification of protein kinase pattern in human placentae during gestation
Placenta
|September 1, 1984
Summary
Histone kinase activity in placental tissue increases significantly by full term, primarily due to the selective activation of the Type II cAMP-dependent enzyme in the cytosol.
Area of Science:
- Biochemistry
- Molecular Biology
- Reproductive Biology
Background:
- Histone kinases play crucial roles in cellular processes.
- Understanding their activity in placental development is vital.
- Subcellular localization and gestational age influence kinase activity.
Purpose of the Study:
- To investigate cAMP-dependent and independent histone kinase activity in human placental cytosol and particulate fractions.
- To determine how kinase activity and distribution change with gestational age.
- To characterize the specific isoenzymes involved in placental maturation.
Main Methods:
- Studied histone kinases in placental cytosol and particulate fractions from different gestational ages.
- Assessed total protein kinase activity and its distribution.
- Utilized DEAE-cellulose chromatography and sucrose-gradient ultracentrifugation to identify isoenzymes.
Main Results:
- Total protein kinase activity increased significantly in term placentae, with greater increases in cAMP-dependent kinases.
- The cytosol showed a higher increase in activity compared to the particulate fraction in term placentae.
- Type II cAMP-dependent isoenzyme was predominant and selectively activated in term placentae, while Type I remained unchanged.
Conclusions:
- Placental histone kinase activity, particularly Type II cAMP-dependent kinase in the cytosol, is upregulated during late gestation.
- This suggests a critical role for specific histone kinases in placental maturation and function.
- Kinase patterns remain stable in vitro, indicating inherent tissue stability.