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cAMP- and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets.
TLDR
Experiments with 32P-labeled platelets provided evidence that VASP is phosphorylated at the same three identified sites also in intact cells and that selective activation of cAK or cGK primarily increased the phosphorylation of both serine 2 and serine 1 but not threonine. Expand
Cyclic nucleotide analogs as probes of signaling pathways
TLDR
Sp-8-pCPT-2′O-Me-cAMPS, a highly specific, non-hydrolyzable Epac activator in vitro, can under certain conditions enhance cGMP-PKG and cAMPPKA signaling pathways in intact platelets and strongly implied that several of these analogs might, in addition to their primary effects, also cause elevation of cAMP or cG MP indirectly by inhibiting PDEs in the cell. Expand
(Rp)-8-pCPT-cGMPS, a novel cGMP-dependent protein kinase inhibitor.
TLDR
The data obtained suggest that (Rp)-8-pCPT-cGMPS may be a useful tool for studying the role of cGMP in vitro and in intact cells. Expand
Analysis of the functional role of cGMP-dependent protein kinase in intact human platelets using a specific activator 8-para-chlorophenylthio-cGMP.
TLDR
8-pCPT-cGMP is a very potent and selective activator of cGMP-PK in cell extracts and in intact human platelets and, in this respect, is superior to 8-Br-c GMP and other cG MP analogs used for intact cell studies. Expand
Elimination of Protein Kinase MK5/PRAK Activity by Targeted Homologous Recombination
TLDR
It is concluded that the differences between the phenotypes of MK5- and MK2-deficient mice result from clearly different functional properties of both enzymes. Expand
Inhibition of cGMP‐dependent protein kinase by (Rp)‐guanosine 3',5'‐monophosphorothioates
TLDR
Rp‐8‐Cl‐cGMPS appears to be a rather selective inhibitor of the cGMP‐dependent protein kinase and may be a useful tool for studying the role of cG MP in broken and intact cell systems. Expand
Endothelial Nitric-oxide Synthase (Type III) Is Activated and Becomes Calcium Independent upon Phosphorylation by Cyclic Nucleotide-dependent Protein Kinases*
TLDR
New evidence for cAK and cGK stimulation of both Ca2+/CaM-independent and -dependent NOS-III activity is provided, and possible cross-talk between the NO and prostaglandin I2 pathways and a positive feedback mechanism for NO/cGMP signaling is suggested. Expand
Overexpression of LASP-1 mediates migration and proliferation of human ovarian cancer cells and influences zyxin localisation
TLDR
Evidence is provided for an essential role of LASP-1 in tumour cell growth and migration, possibly through influencing zyxin localization, and for a reduced protein level in SKOV-3 cells following transfection with LASp-1-specific siRNA. Expand
Silencing of LASP-1 influences zyxin localization, inhibits proliferation and reduces migration in breast cancer cells.
TLDR
Evidence is provided for an essential role of LASP-1 in tumor cell growth and migration, possibly by influencing the localization of zyxin. Expand
cGMP-dependent Protein Kinase Type II Regulates Basal Level of Aldosterone Production by Zona Glomerulosa Cells without Increasing Expression of the Steroidogenic Acute Regulatory Protein Gene*
TLDR
It is shown that PKG II activity in ZG cells is important for maintaining basal aldosterone production, and the expression and functional role of cGMP-dependent protein kinases in rat adrenal cortex is demonstrated. Expand
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