Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.11.12 (PKG)
 2,515 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Rat smooth muscle cells (SMCs) stably transfected with the gene for the phenotype regulating protein cyclic guanosine monophosphate-dependent protein kinase (PKG) were used as a cell source in the preparation of three-dimensional (3D) collagen type I vascular constructs. PKG-transfected cells expressed severalfold higher levels of the contractile protein smooth muscle alpha-actin (SMA), relative to untransfected SMCs, both in monolayer culture and in 3D gels. The proliferation rate of PKG-transfected cells was lower than that of untransfected cells in both culture geometries. Three-dimensional collagen constructs made with PKG-transfected cells compacted to a similar degree as those made with untransfected cells, and this compaction could be augmented by biochemical stimulation with platelet-derived growth factor BB (PDGF) or transforming growth factor beta(1) (TGF). Application of cyclic mechanical strain to tubular collagen gels seeded with PKG-transfected cells resulted in a higher degree of gel compaction and circumferential matrix alignment, relative to statically grown controls, but cell proliferation and SMA expression were not affected. These results show that genetic modification of SMCs can be used as a tool to control cell function in vascular tissue engineering, and that the function of such cells can be further modulated by application of biochemical and mechanical stimulation.
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PMID:Genetic modification of smooth muscle cells to control phenotype and function in vascular tissue engineering. 1500 45

The control of vascular smooth muscle contractility enables regulation of blood pressure, which is paramount in physiological adaptation to environmental challenges. Maintenance of stable blood pressure is crucial for health as deregulation (caused by high or low blood pressure) leads to disease progression. Vasotone is principally controlled by the cyclic nucleotide dependent protein kinases A and G, which regulate intracellular calcium and contractile protein calcium sensitivity. The classical pathways for activation of these two kinases are well established and involve the formation and activation by specific cyclic nucleotide second messengers. Recently we reported that both PKA and PKG can be regulated independently of their respective cyclic nucleotides via a mechanism whereby the kinases sense cellular oxidant production using redox active thiols. This novel redox regulation of these kinases is potentially of physiological importance, and may synergise with the classical regulatory mechanisms.
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PMID:Oxidant sensing by protein kinases a and g enables integration of cell redox state with phosphoregulation. 2231 69