scholarly journals Possible involvement of Cyclic-GMP-dependent protein kinase on matrix metalloproteinase-2 expression in rat aortic smooth muscle cells

2012 ◽  
Vol 368 (1-2) ◽  
pp. 27-35 ◽  
Author(s):  
Nupur B. Dey ◽  
Thomas M. Lincoln
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase ◽  
Matrix Metalloproteinase ◽  
Smooth Muscle Cells ◽  
Cyclic Gmp ◽  
Muscle Cells ◽  
Matrix Metalloproteinase 2 ◽  
Dependent Protein Kinase ◽  
Aortic Smooth Muscle ◽  
Dependent Protein

scholarly journals The smooth muscle 132 kDa cyclic GMP-dependent protein kinase substrate is not myosin light chain kinase or caldesmon

1990 ◽  
Vol 271 (2) ◽  
pp. 493-499 ◽  
Author(s):  
B Sarcevic ◽  
P J Robinson ◽  
R B Pearson ◽  
B E Kemp
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase ◽  
Smooth Muscle Cells ◽  
Cyclic Gmp ◽  
Muscle Cells ◽  
Dependent Protein Kinase ◽  
Aortic Smooth Muscle Cells ◽  
Kinase Substrate ◽  
Aortic Smooth Muscle ◽  
Dependent Protein

Atrial natriuretic peptide (ANP) stimulates the phosphorylation of three cyclic GMP-dependent protein kinase substrate proteins of 225, 132, and 11 kDa (P225, P132 and P11 respectively) in the particulate fraction of cultured rat aortic smooth muscle cells [Sarcevic, Brookes, Martin, Kemp & Robinson (1989) J. Biol. Chem. 264, 20648-20654]. Vrolix, Raeymaekers, Wuytack, Hofmann & Casteels [(1988) Biochem. J. 255, 855-863] have reported the presence of a 130 kDa cyclic GMP-dependent protein kinase substrate protein in the membrane fraction of pig aorta or stomach, and suggested that it may be myosin light chain kinase (MLCK). The aim of the present study was to determine whether P132 from rat aorta was MLCK or caldesmon. Although P132 co-migrates with purified chicken gizzard MLCK on SDS/polyacrylamide gels, it is distinct from rat aortic MLCK. Partially purified MLCK from rat aorta migrated as a 145 kDa protein on SDS/polyacrylamide gels. Immunoblotting the partially purified rat aortic MLCK with antibody to bovine tracheal MLCK identified rat aortic MLCK (145 kDa) and a corresponding 145 kDa protein in the particulate fraction of cultured rat aortic smooth muscle cells, but did not detect the 132 kDa protein. Phosphopeptide maps of purified rat aortic MLCK prepared by digestion with Staphylococcus aureus V8 protease were distinct from those of P132. P132 was not caldesmon, since antibodies to caldesmon cross-reacted with 136 and 76 kDa proteins in the particulate fraction of rat aortic cells, but not with P132. Furthermore, caldesmon was partially extracted from the particulate into the soluble fraction by heating at 90 degrees C, whereas P132 was not. These results demonstrate that the ANP-responsive cyclic GMP-dependent protein kinase substrate of 132 kDa from rat aortic smooth muscle cells is not MLCK or caldesmon.

scholarly journals Cyclic GMP–Dependent Protein Kinase Inhibits Osteopontin and Thrombospondin Production in Rat Aortic Smooth Muscle Cells

1998 ◽  
Vol 82 (2) ◽  
pp. 139-146 ◽  
Author(s):  
Nupur B. Dey ◽  
Nancy J. Boerth ◽  
Joanne E. Murphy-Ullrich ◽  
Pi-Ling Chang ◽  
Charles W. Prince ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase ◽  
Smooth Muscle Cells ◽  
Cyclic Gmp ◽  
Muscle Cells ◽  
Dependent Protein Kinase ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle ◽  
Dependent Protein

cGMP-dependent protein kinase mediates the reduction of Ca2+ by cAMP in vascular smooth muscle cells

1990 ◽  
Vol 258 (3) ◽  
pp. C399-C407 ◽  
Author(s):  
T. M. Lincoln ◽  
T. L. Cornwell ◽  
A. E. Taylor
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase ◽  
Smooth Muscle Cells ◽  
Muscle Cells ◽  
Dependent Protein Kinase ◽  
Aortic Smooth Muscle ◽  
Cyclic Monophosphate ◽  
Cgmp Dependent Protein Kinase ◽  
Camp Dependent Protein Kinase ◽  
Dependent Protein

The major action of forskolin, the diterpine activator of adenylate cyclase, in primary (unpassaged) rat aortic smooth muscle cells is to reduce vasopressin-stimulated Ca2+ concentrations. In repetitively passaged cells, however, forskolin by itself increased Ca2+ levels by apparently stimulating Ca2+ uptake into the cell and had much smaller effects on inhibiting vasopressin-stimulated Ca2+ elevations. Both primary and passaged smooth muscle cells contained adenosine 3',5'-cyclic monophosphate (cAMP)-dependent protein kinase. Guanosine 3',5'-cyclic monophosphate (cGMP)-dependent protein kinase was greatly reduced or absent in passaged smooth muscle cells. The introduction of purified cGMP-dependent protein kinase into the cytoplasm of passaged cells prevented forskolin from elevating intracellular Ca2+ and restored the capacity of forskolin to reduce vasopressin-stimulated Ca2+ mobilization. Similar effects were observed for isoproterenol in passaged smooth muscle cells. When introduced into cells, the active catalytic subunit of the cAMP-dependent protein kinase did not lead to reductions in Ca2+ levels. These results suggest that cAMP elevations lead to profound changes in Ca2+ metabolism through activation of both cAMP- and cGMP-dependent protein kinases. Activation of cGMP-dependent protein kinase by cAMP leads to the reduction in intracellular Ca2+, whereas activation of cAMP-dependent protein kinase may only mediate the uptake of Ca2+ from extracellular sources.

scholarly journals Steroid-sensitive Gene 1 Is a Novel Cyclic GMP-dependent Protein Kinase I Substrate in Vascular Smooth Muscle Cells

2013 ◽  
Vol 288 (34) ◽  
pp. 24972-24983 ◽  
Author(s):  
Guang-rong Wang ◽  
Howard K. Surks ◽  
K. Mary Tang ◽  
Yan Zhu ◽  
Michael E. Mendelsohn ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Vascular Smooth Muscle Cells ◽  
Cyclic Gmp ◽  
Muscle Cells ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
Steroid Sensitive
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