Apparent increases in phospholipid degradation and turnover during combined treatment with protein synthesis inhibitors and adrenocorticotropin.
Inhibitors of protein synthesis, cycloheximide and puromycin, blocked ACTH (adrenocorticotropin)-induced increases in phospholipid mass, including phosphatidylinositol, but paradoxically increase 32P-labelling (but not [3H]glycerol-labelling) therein. Cycloheximide also provoked an initial rapid decrease in 32P-prelabelled phospholipids, followed by an increase in [32P]Pi incorporation. These effects of cycloheximide and puromycin occurred in ACTH-treated (but not in control) cells. It appears that inhibition of protein synthesis during ACTH action provokes an increase in phospholipid degradation, followed by partial resynthesis of the phospholipid head groups.
D000324:Adrenocorticotropic Hormone / Q000494:pharmacology*; D000818:Animals; D003513:Cycloheximide / Q000494:pharmacology*; D005990:Glycerol / Q000378:metabolism; D066298:In Vitro Techniques; D010710:Phosphates / Q000378:metabolism; D010713:Phosphatidylcholines / Q000378:metabolism; D010714:Phosphatidylethanolamines / Q000378:metabolism; D010716:Phosphatidylinositols / Q000378:metabolism; D010743:Phospholipids / Q000378:metabolism*; D011691:Puromycin / Q000494:pharmacology*; D051381:Rats
D010710:Phosphates; D010713:Phosphatidylcholines; D010714:Phosphatidylethanolamines; D010716:Phosphatidylinositols; D010743:Phospholipids; D011691:Puromycin; D000324:Adrenocorticotropic Hormone; D003513:Cycloheximide; D005990:Glycerol