Cyclic AMP-dependent phosphorylation, Ca2+ and calmodulin: possible influences on acyltransferases and pyruvate dehydrogenase activities of rat mammary gland
Autor: | T. W. Keenan, H. Mohammed Valivullah |
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Rok vydání: | 1986 |
Předmět: |
medicine.medical_specialty
Pyruvate dehydrogenase kinase Calmodulin Pyruvate Dehydrogenase Complex Biology Pyruvate dehydrogenase phosphatase Biochemistry Mammary Glands Animal Pregnancy Internal medicine Lactation medicine Cyclic AMP Animals Phosphorylation Protein kinase A Rats Inbred Strains DNA Pyruvate dehydrogenase complex Rats medicine.anatomical_structure Endocrinology Acyltransferase biology.protein CAMP binding Calcium Female Protein Kinases Acyltransferases Protein Binding |
Zdroj: | The International journal of biochemistry. 18(5) |
ISSN: | 0020-711X |
Popis: | 1. 1. Specific activities of diacylglycerol acyltransferase, glycerol 3-phosphate acyltransferase and pyruvate dehydrogenase were studied in virgin, pregnant, lactating and involuting rat mammary glands. 2. 2. An inverse relationship was evident between cAMP binding to protein kinase(s) and the activities of the above enzymes in lactating rat mammary glands. 3. 3. Results suggested that free Ca 2+ concentration may also contribute to control of the activity of pyruvate dehydrogenase in these glands. 4. 4. However, no consistent change was observed between the activities of these enzymes and cAMP binding in young, pregnant and involuting rat mammary glands. Calmodulin levels paralleled bound Ca 2+ except in lactating rats. 5. 5. Almost all parameters studied peaked on day 8 of lactation. |
Databáze: | OpenAIRE |
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