cAMP induces phosphorylation of a 40-kDa nuclear protein which is distinct from CREB during chondrogenesis of chick limb bud mesenchymal cells in vitro

Sun Young Park, Jae Chang Jung, Soo Dong Kim, Young Sup Lee, Tae Kyu Park, Shin Sung Kang

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

We examined the effect of cAMP on the phosphorylation of intracellular proteins in cultured chondroblasts to understand the stimulatory role of intracellular cAMP in chondrogenesis of chick limb bud mesenchymal cells. A 40-kDa protein was remarkably phosphorylated by cAMP and the phosphorylation was completely blocked by an inhibitor of cAMP-dependent protein kinase. The phosphorylation of the 40-kDa protein was maximum at early stage of chondrogenesis (i.e., 24 hr of culture) which is consistent with the changes in the level of intracellular cAMP. The 40-kDa phosphoprotein was exclusively located in the nuclear parts of chondroblast but distinct from cAMP response element binding protein.

Original languageEnglish
Pages (from-to)16-20
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume212
Issue number1
DOIs
StatePublished - 1995

Fingerprint

Dive into the research topics of 'cAMP induces phosphorylation of a 40-kDa nuclear protein which is distinct from CREB during chondrogenesis of chick limb bud mesenchymal cells in vitro'. Together they form a unique fingerprint.

Cite this