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Plasma membrane cyclic AMP-dependent protein phosphorylation system in L6 myoblasts
Biochimica Et Biophysica Acta
|June 2, 1978
Summary
Researchers isolated plasma membranes and discovered a tightly bound protein kinase. This enzyme
Area of Science:
- Cell Biology
- Biochemistry
- Molecular Biology
Background:
- Plasma membranes are crucial for cellular functions.
- Understanding membrane protein phosphorylation is key to cellular regulation.
Purpose of the Study:
- To characterize the protein phosphorylation system in purified plasma membranes from L6 myoblasts.
- To investigate the role of cyclic nucleotides in regulating plasma membrane-bound protein kinase activity.
Main Methods:
- Plasma membrane isolation using the vesiculation technique.
- Assay of protein kinase activity using exogenous and endogenous substrates.
- Analysis of protein phosphorylation by SDS-polyacrylamide gel electrophoresis.
Main Results:
- Purified plasma membranes contain a tightly bound protein kinase.
- Cyclic AMP (cAMP) dose-dependently stimulates this protein kinase activity up to 4-fold.
- Both cAMP-dependent and -independent phosphorylation of endogenous membrane proteins occurs.
Conclusions:
- Plasma membranes possess endogenous cAMP-dependent and -independent protein phosphorylating systems.
- These systems may regulate membrane functions, including cellular differentiation.