Search results for: Recombinant Human PPP1R14A Proteins
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A functional interaction between CPI-17 and RACK1 proteins in bronchial smooth muscle cells.CPI-17 is a phosphorylation-dependent inhibitor of smooth muscle myosin light chain. Using yeast two-hybrid system, we have identified the receptor for activated C kinase 1 (RACK1) as a novel interaction partner of CPI-17. The direct interaction and co-localization of CPI-17 with RACK1 were confirmed by immunoprecipitation and confocal microscopy analysis, respectively. An in vitro assay system using recombinant/purified proteins revealed that the PKC-mediated phosphorylation of CPI-17 was augmented in the presence of RACK1. These results suggest that RACK1 may play a role in PKC/CPI-17 signaling pathway.
2435 related Products with: A functional interaction between CPI-17 and RACK1 proteins in bronchial smooth muscle cells.PIK3R1 & SHC1 Protein Pro HSPB1 & EGFR Protein Prot PDGFRB & STAT5A Protein P GRAP2 & CSF1R Protein Pro PIK3R1 & CTNNB1 Protein P Recombinant Human Inhibin BID & FAS Protein Protein CDC42 & MAP3K4 Protein Pr VEGFB & VEGFA Protein Pro CASP3 & MLH1 Protein Prot CRK & SHC1 Protein Protei Recombinant Canine ApoJ C
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Functional role of PKC in contraction of cultured human prostatic stromal cells.The contractile activity of prostatic stromal cells contributes to symptoms of benign prostatic hyperplasia (BPH). However, the mechanisms for this contraction have not yet been fully elucidated. In this study, we investigated the role of protein kinase C (PKC) in prostatic contraction by measuring the isometric tension development of cultured human prostatic stromal cells (CHPSCs) derived from BPH patients. Fresh human BPH tissue was used only in a Western blot analysis. A ring preparation made of CHPSCs and collagen gel could develop an isometric tension during activation with various agonists. Phorbol 12,13 dibutyrate (PDBu), a PKC activator, induced a relaxation. A Western blot analysis revealed the expression of PKC-potentiated protein phosphatase-1 inhibitory protein (CPI-17) in both CHPSCs and fresh human BPH tissue to be much lower than that in the rabbit aorta. When CPI-17 was over-expressed, PDBu induced a large contraction, but the agonist-induced contraction did not become larger than expected. In alpha-toxin permeabilized preparations, PDBu induced a relaxation in control CHPSCs, while it induced a contraction at a constant [Ca2+]i in CPI-17 over-expressing CHPSCs. These results indicated that the activation of PKC in CHPSCs induces a relaxation probably due to low expression level of CPI-17 and also that the PKC-CPI-17 pathway does not appear to play a major role in the agonist-induced contraction even when CPI-17 was over-expressed.
2651 related Products with: Functional role of PKC in contraction of cultured human prostatic stromal cells.Human Internal Mammary Ar Human Large Intestine Mic Epidermal Growth Factor ( Macrophage Colony Stimula GFP Expressing Human Inte AccuPrep Genomic DNA Extr Anti beta3 AR Human, Poly Human Small Intestine Mic Macrophage Colony Stimula Epidermal Growth Factor ( Goat Anti-Human LRP6, (in Goat Anti-Human APOB, (in
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Role of CPI-17 in the regulation of endothelial cytoskeleton.We have previously shown that myosin light chain (MLC) phosphatase (MLCP) is critically involved in the regulation of agonist-mediated endothelial permeability and cytoskeletal organization (Verin AD, Patterson CE, Day MA, and Garcia JG. Am J Physiol Lung Cell Mol Physiol 269: L99-L108, 1995). The molecular mechanisms of endothelial MLCP regulation, however, are not completely understood. In this study we found that, similar to smooth muscle, lung microvascular endothelial cells expressed specific endogenous inhibitor of MLCP, CPI-17. To elucidate the role of CPI-17 in the regulation of endothelial cytoskeleton, full-length CPI-17 plasmid was transiently transfected into pulmonary artery endothelial cells, where the background of endogenous protein is low. CPI-17 had no effect on cytoskeleton under nonstimulating conditions. However, stimulation of transfected cells with direct PKC activator PMA caused a dramatic increase in F-actin stress fibers, focal adhesions, and MLC phosphorylation compared with untransfected cells. Inflammatory agonist histamine and, to a much lesser extent, thrombin were capable of activating CPI-17. Histamine caused stronger CPI-17 phosphorylation than thrombin. Inhibitory analysis revealed that PKC more significantly contributes to agonist-induced CPI-17 phosphorylation than Rho-kinase. Dominant-negative PKC-alpha abolished the effect of CPI-17 on actin cytoskeleton, suggesting that the PKC-alpha isoform is most likely responsible for CPI-17 activation in the endothelium. Depletion of endogenous CPI-17 in lung microvascular endothelial cell significantly attenuated histamine-induced increase in endothelial permeability. Together these data suggest the potential importance of PKC/CPI-17-mediated pathway in histamine-triggered cytoskeletal rearrangements leading to lung microvascular barrier compromise.
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Phosphoprotein inhibitor CPI-17 specificity depends on allosteric regulation of protein phosphatase-1 by regulatory subunits.Inhibition of myosin phosphatase is critical for agonist-induced contractility of vascular smooth muscle. The protein CPI-17 is a phosphorylation-dependent inhibitor of myosin phosphatase and, in response to agonists, Thr-38 is phosphorylated by protein kinase C, producing a >1,000-fold increase in inhibitory potency. Here, we addressed how CPI-17 could selectively inhibit myosin phosphatase among other protein phosphatase-1 (PP1) holoenzymes. PP1 in cell lysates was separated by sequential affinity chromatography into at least two fractions, one bound specifically to thiophospho-CPI-17, and another bound specifically to inhibitor-2. The MYPT1 regulatory subunit of myosin phosphatase was concentrated only in the fraction bound to thiophospho-CPI-17. This binding was eliminated by addition of excess microcystin-LR to the lysate, showing that binding at the active site of PP1 is required. Phospho-CPI-17 failed to inhibit glycogen-bound PP1 from skeletal muscle, composed primarily of PP1 with the striated muscle glycogen-targeting subunit (G(M)) regulatory subunit. Phospho-CPI-17 was dephosphorylated during assay of glycogen-bound PP1, not MYPT1-associated PP1, even though these two holoenzymes have the same PP1 catalytic subunit. Phosphorylation of CPI-17 in rabbit arteries was enhanced by calyculin A but not okadaic acid or fostriecin, consistent with PP1-mediated dephosphorylation. We propose that CPI-17 binds at the PP1 active site where it is dephosphorylated, but association of MYPT1 with PP1C allosterically retards this hydrolysis, resulting in formation of a complex of MYPT1.PP1C.P-CPI-17, leading to an increase in smooth muscle contraction.
2808 related Products with: Phosphoprotein inhibitor CPI-17 specificity depends on allosteric regulation of protein phosphatase-1 by regulatory subunits.to PKA RIIA (Protein Kin Rabbit Anti-G protein alp Rabbit Anti-G protein alp Rabbit Anti-G protein alp MK-1775 Mechanisms: Wee-1 Rabbit Anti-G protein alp Rabbit Anti-G protein alp Rabbit Anti-G protein alp to PKA--RIIA (Protein Ki SGI-1776 Mechanisms: PIM Rabbit Anti-G protein alp Rabbit Anti-G protein alp
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A novel phosphoprotein inhibitor of protein type-1 phosphatase holoenzymes.Control of protein phosphatases is now understood to depend on binding to a variety of regulatory or targeting subunits to form holoenzymes with restricted localization and substrate specificity. In addition, the catalytic subunits of both type-1 and type-2 phosphatases bind specific inhibitor proteins. Here, we report discovery of a new inhibitor protein called PHI-1 that is specific for type-1 protein phosphatase (PP1). Recombinant tagged PHI-1 was phosphorylated by protein kinase C at two sites, one a Ser and one a Thr; phosphorylation enhanced inhibitory potency 50-fold. Mutation of Thr57 to Ala gave a protein phosphorylated only on Ser, without change in inhibitory activity, indicating that phosphorylation of Thr57 was required for full activity. Immunoblotting showed that PHI-1 was expressed in most animal tissues and several cell lines, and a second larger protein called PHI-2 was present in different muscles, especially cardiac muscle. Unlike any other known inhibitor, PHI-1 inhibited the myosin- and glycogen-associated holoenzyme versions of PP1 as well as the monomeric catalytic subunit of PP1. Discovery of PHI-1 and PHI-2 opens new possibilities for regulation of PP1 via phosphorylation-dependent signaling pathways.
2210 related Products with: A novel phosphoprotein inhibitor of protein type-1 phosphatase holoenzymes.Rabbit Anti-G protein alp Rabbit Anti-G protein alp Type II 5-phosphatase ant Rabbit Anti-G protein alp Rabbit Anti-G protein alp Rabbit Anti-G protein alp Rabbit Anti-G protein alp Rabbit Anti-G protein alp Rabbit Anti-G protein alp Anti PCOLE 1 (Procollagen Rabbit Anti-G protein alp Rabbit Anti-G protein alp
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