TY - JOUR
T1 - Bovine skeletal growth factor stimulates protein phosphorylation of chicken bone cells in vitro
AU - William Lau, K. H.
AU - Jennings, John C.
AU - Baylink, David J.
N1 - Funding Information:
Acknowledgements--We thank Leticia Ortloff for her technical assistance, Dr John R. Farley for his suggestions and criticisms throughout the study and the Medical Media staff of the Jerry L. Pettis V.A. Hospital for their assistance in the preparation of this manuscript. This work is supported by the Veterans Administration and the Department of Medicine, Loma Linda University.
PY - 1988/12
Y1 - 1988/12
N2 - 1. 1. Bovine skeletal growth factor (SGF), a potent bone cell mitogen, stimulated protein phosphorylation in cultured chicken calvarial cells. 2. 2. SDS-PAGE followed by autoradiographic analysis of the cellular proteins indicated that [32P] incorporation was enhanced in several proteins in response to 10 ng/ml of SGF (the maximum stimulatory mitogenic dose for these cells). 3. 3. Under conditions favoring tyrosine kinases, SGF stimulated phosphorylation of at least 6 proteins in crude calvarial cell membrane fraction, and caused a time-dependent stimulation of phosphorylation of angiotensin II by crude calvarial cell membrane fractions. 4. 4. Thus, our data demonstrate that SGF stimulates protein phosphorylation in bone cells, and suggest that at least some of the protein phosphorylation involves tyrosine residues.
AB - 1. 1. Bovine skeletal growth factor (SGF), a potent bone cell mitogen, stimulated protein phosphorylation in cultured chicken calvarial cells. 2. 2. SDS-PAGE followed by autoradiographic analysis of the cellular proteins indicated that [32P] incorporation was enhanced in several proteins in response to 10 ng/ml of SGF (the maximum stimulatory mitogenic dose for these cells). 3. 3. Under conditions favoring tyrosine kinases, SGF stimulated phosphorylation of at least 6 proteins in crude calvarial cell membrane fraction, and caused a time-dependent stimulation of phosphorylation of angiotensin II by crude calvarial cell membrane fractions. 4. 4. Thus, our data demonstrate that SGF stimulates protein phosphorylation in bone cells, and suggest that at least some of the protein phosphorylation involves tyrosine residues.
UR - https://www.scopus.com/pages/publications/0024204071
UR - https://www.scopus.com/pages/publications/0024204071#tab=citedBy
U2 - 10.1016/S0020-711X(98)90014-3
DO - 10.1016/S0020-711X(98)90014-3
M3 - Article
C2 - 3243378
SN - 0020-711X
VL - 20
SP - 1443
EP - 1450
JO - International Journal of Biochemistry
JF - International Journal of Biochemistry
IS - 12
ER -