Granulocytic differentiation induced by retinoic acid in HL-60 cells is associated with changes in adenylate cyclase activity.
The effect of all-trans Retinoic Acid (RA) on the activity of membrane bound adenylate cyclase (AC) of human malignant cell lines (HL-60 and U-937) was studied. Granulocytic terminal differentiation of the HL-60 cells was correlated to an increase of AC activity and to a potentiation of guanosine 5' triphosphate (GTP) inhibitory effects on the enzyme activity. No direct in vitro effect of RA on HL-60 membranes was found. Monocytic terminal differentiation obtained on 1 B-D arabinofuranosyl cytosine (Ara-C) treated HL-60 cells, or on RA treated U-937 cells, did not modify AC activity. The results here reported suggest relations between the modification of GTP binding protein activity and RA induced granulocytic differentiation of malignant cells.
D000262:Adenylyl Cyclases / Q000032:analysis*; D002454:Cell Differentiation / Q000187:drug effects; D002460:Cell Line; D005576:Colforsin / Q000494:pharmacology; D003561:Cytarabine / Q000494:pharmacology; D019204:GTP-Binding Proteins / Q000032:analysis; D006098:Granulocytes / Q000473:pathology*; D006160:Guanosine Triphosphate / Q000494:pharmacology; D006801:Humans; D015470:Leukemia, Myeloid, Acute / Q000473:pathology*; D014212:Tretinoin / Q000494:pharmacology*
D003561:Cytarabine; D005576:Colforsin; D014212:Tretinoin; D006160:Guanosine Triphosphate; D019204:GTP-Binding Proteins; D000262:Adenylyl Cyclases