We previously observed that HL-60 cells treated with manganese (Mn) during differentiation displayed an enhanced oxidative burst. Since a Mn-dependent kinase has been identified and phosphorylation is involved in burst activation, the objective of this research was to identify proteins in retinoic a
A nuclear cAMP binding protein in retinoic acid-treated HL-60 cells
β Scribed by Robert C. Briggs; Susan B. Casey
- Publisher
- John Wiley and Sons
- Year
- 1988
- Tongue
- English
- Weight
- 438 KB
- Volume
- 136
- Category
- Article
- ISSN
- 0021-9541
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β¦ Synopsis
A cAMP binding protein was detected in HL-60 cells using photoaffinity labeling with 8-azido ["PIcAMP. The binding protein was found i n 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.
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