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A nuclear cAMP binding protein in retinoic acid‐treated HL‐60 cells
Author(s) -
Briggs Robert C.,
Casey Susan B.
Publication year - 1988
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041360127
Subject(s) - retinoic acid , protein subunit , protein kinase a , nuclear protein , photoaffinity labeling , binding protein , retinoic acid inducible orphan g protein coupled receptor , retinoic acid receptor , tretinoin , retinoic acid receptor gamma , microbiology and biotechnology , chemistry , biochemistry , biology , kinase , binding site , transcription factor , gene
A cAMP binding protein was detected in HL‐60 cells using photoaffinity labeling with 8‐azido [ 32 P]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.