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Activation of protein kinase A is a pivotal step involved in both BMP‐2‐ and cyclic AMP‐induced chondrogenesis
Author(s) -
Lee YunShain,
Chuong ChengMing
Publication year - 1997
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/(sici)1097-4652(199702)170:2<153::aid-jcp7>3.0.co;2-n
Subject(s) - chondrogenesis , creb , protein kinase a , microbiology and biotechnology , chemistry , phosphorylation , cyclic amp response element binding protein , protein kinase c , signal transduction , kinase , biology , biochemistry , in vitro , transcription factor , gene
We studied the roles of protein kinase A (PKA) activation and cyclic AMP response element binding protein (CREB) phosphorylation in chondrogenesis using serum‐free chicken limb bud micromass cultures as a model system. We showed the following points: (1) in micromass cultures, activation of PKA enhances chondrogenesis and increases the phosphorylation of CREB; (2) BMP‐2, a chondrogenic stimulator, increases PKA activity and the level of phosphorylated CREB (P‐CREB); (3) H8, a PKA inhibitor, inhibits chondrogenesis; (4) the chondrogenic activities of BMP‐2 and cAMP are suppressed by H8; and (5) long‐term TPA treatment (a protein kinase C (PKC) modulator) inhibits chondrogenesis and decreases the levels of CREB and P‐CREB. These results suggest that activation of PKA is a physiological event during chondrogenesis that is involved in the chondrogenic effects of both BMP‐2 and cyclic AMP (cAMP)‐dependent pathways. J. Cell. Physiol. 170:153–165, 1997. © 1997 Wiley‐Liss, Inc.