A nuclear cAMP binding protein in retinoic acid-treated HL-60 cells.
A cAMP binding protein was detected in HL-60 cells using photoaffinity labeling with 8-azido [32P]cAMP. The binding protein was found in a 0.35 M NaCl nuclear protein extract from untreated HL-60 cells and from the HL-60 cells induced to mature with retinoic acid. While the quantity of the cAMP binding protein did not change following the induced differentiation, a second form of the subunit, altered in charge, was present at 3 and 5 days after retinoic acid treatment. The findings indicate that the regulatory subunit of the type II cAMP-dependent protein kinase could be involved in nuclear functions associated with human myeloid cell differentiation.
Briggs
R C
RC
Department of Pathology, A.B. Hancock, Jr. Memorial Laboratory, Vanderbilt University Cancer Center, Nashville, Tennessee.
Casey
S B
SB
D001386:Azides / Q000378:metabolism; D002352:Carrier Proteins / Q000378:metabolism*; D002467:Cell Nucleus / Q000378:metabolism; D000242:Cyclic AMP / Q000031:analogs & derivatives / Q000378:metabolism; D002373:Cyclic AMP Receptor Protein; D006801:Humans; D015470:Leukemia, Myeloid, Acute / Q000378:metabolism*; D008970:Molecular Weight; D011494:Protein Kinases / Q000378:metabolism; D014212:Tretinoin / Q000494:pharmacology*
D001386:Azides; D002352:Carrier Proteins; D002373:Cyclic AMP Receptor Protein; C017042:8-azidoadenosine-3',5'-monophosphate; D014212:Tretinoin; D000242:Cyclic AMP; D011494:Protein Kinases