Regulation of human platelet myosin light chain kinase by the catalytic subunit of cyclic AMP-dependent protein kinase

Nature ◽  
1981 ◽  
Vol 291 (5812) ◽  
pp. 252-254 ◽  
Author(s):  
D. R. Hathaway ◽  
C. R. Eaton ◽  
R. S. Adelstein
1986 ◽  
Vol 109 (1) ◽  
pp. 97-100 ◽  
Author(s):  
K. Matsui ◽  
K. Higashi ◽  
T. Yoshimura ◽  
M. Ito ◽  
E. Miyamoto

ABSTRACT Myosin light chain kinase activity in the placental region of the rabbit myometrium on day 28 of gestation was 4·7±0·1 (mean ± s.e.m.) nmol/min per mg protein, which was significantly higher than that (3·6 ± 0·1 nmol/min per mg protein) in the non-placental region. The amount of calmodulin in the placental region was 4·2 ± 0·1 μg/mg protein, which was significantly higher than that (3·2 ± 0·1 μg/mg protein) in the non-placental region. In contrast, cyclic AMP-dependent protein kinase activities showed no difference between the two regions. These findings suggest that calcium- and calmodulin-dependent protein phosphorylation is activated mainly in the placental region, and uterine contractions can occur more strongly in this part than in the non-placental region. Such enzymatic phenomena may be related to the mechanism whereby the placenta separates from the myometrium after delivery of the fetus. J. Endocr. (1986) 109, 97–100


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