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Regulation by Dibutyryl Cyclic AMP of Carnosine Synthesis in Astroglia‐Rich Primary Cultures Kept in Serum‐Free Medium
Author(s) -
Schulz Michael,
Hamprecht Bernd,
Kleinkauf Horst,
Bauer Karl
Publication year - 1989
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1989.tb10921.x
Subject(s) - forskolin , activator (genetics) , carnosine , cyclic nucleotide phosphodiesterase , adenylate kinase , phosphodiesterase inhibitor , medicine , endocrinology , phosphodiesterase , cyclase , chemistry , phorbol , protein kinase a , biochemistry , protein kinase c , biology , kinase , enzyme , stimulation , receptor
The synthesis of carnosine (β‐Ala‐His) by astroglia‐rich primary cultures was much higher if the cells were cultivated in Ham's nutrient mixture F‐12 than if they were grown in Dulbecco's modified Eagle's medium. Carnosine synthesis was not affected by the presence of insulin, trans‐ferrin. phorbol myristate acetate, or dexamethasone. However. dibutyryl cyclic AMP and other agents that can, directly or ndirectly, activate cyclic AMP‐dependent protein kinases strongly lower the rate of carnosine synthesis. The depression of carnosine synthesis was dependent on the concentration of dibutyryl cyclic AMP. The effect was maximal (approximately 80% inhibition) in cultures preincubated with 1 m M dibutyryl cyclic AMP for 4 days. The adenylate cyclase activator forskolin, the phosphodiesterase inhibitor 3‐isobutyl‐1‐methylxanthine, and 8‐bromo‐cyclic AMP caused the same depression as dibutyryl cyclic AMP, whereas neither butyrate nor dibutyryl cyclic GMP elicited any effect.