Rapid degradation of NAD by retinoic acid-differentiated HL-60 granulocyte membranes prevents ADP ribosylation.
Pertussis and cholera toxins failed to ADP-ribosylate G alpha s and G alpha i in membranes isolated from retinoic acid-differentiated HL-60 granulocytes, although G alpha i subunits were present. NAD was rapidly degraded in the presence of these membranes, primarily to ADP-ribose, to less than 10% of initial activity by 5 min. Metabolism of NAD was heat labile and inhibited by NADP, but not by imidazole or isonicotinic acid hydrazine. Pertussis toxin uncoupled LTB4 receptors from G proteins in intact retinoic acid-differentiated HL-60 cells. Retinoic acid differentiation stimulates expression of a unique NAD-glycohydrolase activity in HL-60 granulocytes which prevents ADP-ribosylation in isolated membranes, but not intact cells.
McLeish
K R
KR
Veterans Administration Medical Center, Louisville, KY.
Jacobs
A A
AA
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D002454:Cell Differentiation / Q000187:drug effects; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism; D002478:Cells, Cultured; D002772:Cholera Toxin / Q000494:pharmacology; D019204:GTP-Binding Proteins / Q000378:metabolism; D006098:Granulocytes / Q000166:cytology / Q000187:drug effects / Q000378:metabolism*; D006801:Humans; D009243:NAD / Q000378:metabolism*; D009244:NAD+ Nucleosidase / Q000378:metabolism; D037342:Pertussis Toxin; D014212:Tretinoin / Q000494:pharmacology; D010566:Virulence Factors, Bordetella / Q000494:pharmacology
D010566:Virulence Factors, Bordetella; D009243:NAD; D000246:Adenosine Diphosphate Ribose; D014212:Tretinoin; D002772:Cholera Toxin; D037342:Pertussis Toxin; D009244:NAD+ Nucleosidase; D019204:GTP-Binding Proteins