35 results match your criteria dominant-negative dn-pkc


Role of protein kinase C-η in cigarette smoke extract-induced apoptosis in MRC-5-cells.

Hum Exp Toxicol 2015 Sep 9;34(9):869-77. Epub 2014 Dec 9.

Department of Pulmonary, Allergy and Critical Care Medicine, Gachon University, Gil Medical Center, Namdong-Gu, Incheon, Republic of Korea

Cigarette smoke (CS) is a major risk factor for emphysema, which causes cell death in structural cells of the lung by mechanisms that are still not completely understood. We demonstrated previously that CS extract (CSE) induces caspase activation in MRC-5 human lung fibroblasts, activated protein kinase C-η (PKC-η), and translocated PKC-η from the cytosol to the membrane. The objective of this study was to investigate the involvement of PKC-η activation in a CSE-induced extrinsic apoptotic pathway. Read More

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September 2015

Taurolithocholate-induced MRP2 retrieval involves MARCKS phosphorylation by protein kinase Cϵ in HUH-NTCP Cells.

Hepatology 2013 Jul 14;58(1):284-92. Epub 2013 May 14.

Departments of Biomedical Sciences, Tufts Cummings School of Veterinary Medicine, North Grafton, MA, USA.

Unlabelled: Taurolithocholate (TLC) acutely inhibits the biliary excretion of multidrug-resistant associated protein 2 (Mrp2) substrates by inducing Mrp2 retrieval from the canalicular membrane, whereas cyclic adenosine monophosphate (cAMP) increases plasma membrane (PM)-MRP2. The effect of TLC may be mediated via protein kinase Cϵ (PKCϵ). Myristoylated alanine-rich C kinase substrate (MARCKS) is a membrane-bound F-actin crosslinking protein and is phosphorylated by PKCs. Read More

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PKC-ε mediates multiple endothelin-1 actions on systolic Ca2+ and contractility in ventricular myocytes.

Biochem Biophys Res Commun 2012 Jul 12;423(3):600-5. Epub 2012 Jun 12.

Molecular and Cellular Pharmacology, University of Wisconsin School of Medicine and Public Health, Madison, WI, USA.

Endothelin-1 (ET-1) induces positive inotropy (enhanced contractility) in cardiac muscle, but establishing underlying cellular mechanisms has been controversial in part because of a growing number of signaling pathways and end effectors targeted by ET-1. Here we present evidence that ET-1 induces positive inotropism in ventricular tissue by increasing both systolic Ca2+ and myofilament Ca2+ sensitivity. To examine the roles of PKC-δ and PKC-ε in these acute responses to ET-1, kinase inactive dominant negative PKC (dn-PKC) constructs were expressed in adult rat ventricular myocytes. Read More

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Rottlerin induces apoptosis of HT29 colon carcinoma cells through NAG-1 upregulation via an ERK and p38 MAPK-dependent and PKC δ-independent mechanism.

Chem Biol Interact 2012 Apr 5;197(1):1-7. Epub 2012 Mar 5.

Department of Immunology, School of Medicine, Keimyung University, Dalseo-Gu, Daegu, Republic of Korea.

Rottlerin, a selective inhibitor of novel isoforms of protein kinase C δ (PKC δ), has been shown to exert multiple effects on cancer cells, including inhibition of cell proliferation and migration. However, the molecular mechanisms responsible for these effects are not fully understood. We found that rottlerin dramatically induced non-steroidal anti-inflammatory drug activated gene-1 (NAG-1) expression in both p53 wild-type and p53-null cancer cell lines, suggesting that NAG-1 upregulation is a common response to rottlerin that occurs independently of p53 in multiple cell lines. Read More

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Rottlerin enhances IL-1β-induced COX-2 expression through sustained p38 MAPK activation in MDA-MB-231 human breast cancer cells.

Exp Mol Med 2011 Dec;43(12):669-75

Department of Immunology Keimyung University School of Medicine Daegu 704-701, Korea.

Cyclooxygenase-2 (COX-2) is an important enzyme in inflammation. In this study, we investigated the underlying molecular mechanism of the synergistic effect of rottlerin on interleukin1β (IL-1β)-induced COX-2 expression in MDA-MB-231 human breast cancer cell line. Treatment with rottlerin enhanced IL-1β-induced COX-2 expression at both the protein and mRNA levels. Read More

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December 2011

PKC-alpha mediates flow-stimulated superoxide production in thick ascending limbs.

Am J Physiol Renal Physiol 2010 Apr 6;298(4):F885-91. Epub 2010 Jan 6.

Department of Internal Medicine, Hypertension and Vascular Research Division, Henry Ford Hospital, 2799 West Grand Blvd., Detroit, MI 48202, USA.

We showed that luminal flow increases net superoxide (O(2)(-)) production via NADPH oxidase in thick ascending limbs. Protein kinase C (PKC) activates NADPH oxidase activity in phagocytes, cardiomyocytes, aortic endothelial cells, vascular smooth muscle cells, and renal mesangial cells. However, the flow-activated pathway that induces NADPH oxidase activity in thick ascending limbs is unclear. Read More

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Involvement of PKC alpha in PMA-induced facilitation of exocytosis and vesicle fusion in PC12 cells.

Biochem Biophys Res Commun 2009 Mar 23;380(2):371-6. Epub 2009 Jan 23.

Division of Bioengineering, Nanyang Technological University, 70 Nanyang Drive, Block N1.3, Singapore 637457, Singapore.

Phorbol-12-myristate-13-acetate, a stable analog of the important signaling membrane lipid diacylglycerol (DAG), is known to potentiate exocytosis and modulate vesicle fusion kinetics in neurons and endocrine cells. The exact mechanisms underlying the actions of PMA, however, is often not clear, largely because of the diversity of the DAG/PMA receptors involved in the exocytotic process, which include, most notably, various isoforms of protein kinase C (PKC). In this study, the roles of PKC alpha in PMA-mediated regulation of exocytosis were investigated by over-expressing wild-type PKC alpha (wt-PKC alpha) or dominant negative PKC alpha (dn-PKC alpha). Read More

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Differential physiological effects of Raf-1 kinase pathways linked to protein kinase C activation depending on the stimulus in v-H-ras-transformed cells.

Authors:
Michael Lee

Cancer Res Treat 2008 Jun 30;40(2):39-44. Epub 2008 Jun 30.

Department of Biology, College of Natural Sciences, University of Incheon, Incheon, Korea.

Purpose: We investigated the molecular mechanism by which the Raf-1 kinase pathways that are linked to protein kinase C induce differential physiological effects, depending on the stimulus, by employing the pharmacological PKC activator PMA.

Materials And Methods: Parental and v-Ha-ras transfected NIH 3T3 cells were chosen as test systems and these cells were transiently transfected with the pMTH vector that encodes dominant-negative (DN) PKC-epsilon with using Lipofectamine 2000. The cell proliferation reagent WST-1 was used for the quantitative determination of cellular proliferation. Read More

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Protein kinase C-epsilon regulates sphingosine 1-phosphate-mediated migration of human lung endothelial cells through activation of phospholipase D2, protein kinase C-zeta, and Rac1.

J Biol Chem 2008 Apr 22;283(17):11794-806. Epub 2008 Feb 22.

Department of Medicine, University of Chicago, Chicago, Illinois 60637, USA.

The signaling pathways by which sphingosine 1-phosphate (S1P) potently stimulates endothelial cell migration and angiogenesis are not yet fully defined. We, therefore, investigated the role of protein kinase C (PKC) isoforms, phospholipase D (PLD), and Rac in S1P-induced migration of human pulmonary artery endothelial cells (HPAECs). S1P-induced migration was sensitive to S1P(1) small interfering RNA (siRNA) and pertussis toxin, demonstrating coupling of S1P(1) to G(i). Read More

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Regulation of mTOR and S6K1 activation by the nPKC isoforms, PKCepsilon and PKCdelta, in adult cardiac muscle cells.

J Mol Cell Cardiol 2007 Dec 4;43(6):754-66. Epub 2007 Oct 4.

Cardiology Division of the Department of Medicine, Gazes Cardiac Research Institute, Medical University of South Carolina, 114 Doughty Street, Charleston, SC 29425, USA.

Activation of both mTOR and its downstream target, S6K1 (p70 S6 kinase) have been implicated to affect cardiac hypertrophy. Our earlier work, in a feline model of 1-48 h pressure overload, demonstrated that mTOR/S6K1 activation occurred primarily through a PKC/c-Raf pathway. To further delineate the role of specific PKC isoforms on mTOR/S6K1 activation, we utilized primary cultures of adult feline cardiomyocytes in vitro and stimulated with endothelin-1 (ET-1), phenylephrine (PE), TPA, or insulin. Read More

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December 2007

Lysophosphatidic acid modulates c-Met redistribution and hepatocyte growth factor/c-Met signaling in human bronchial epithelial cells through PKC delta and E-cadherin.

Cell Signal 2007 Nov 13;19(11):2329-38. Epub 2007 Jul 13.

Department of Medicine, University of Chicago, Chicago, IL 60637, USA.

Previously we demonstrated that ligation of lysophosphatidic acid (LPA) to G protein-coupled LPA receptors induces transactivation of receptor tyrosine kinases (RTKs), such as platelet-derived growth factor receptor beta (PDGF-Rbeta) and epidermal growth factor receptor (EGF-R), in primary cultures of human bronchial epithelial cells (HBEpCs). Here we examined the role of LPA on c-Met redistribution and modulation of hepatocyte growth factor (HGF)/c-Met pathways in HBEpCs. Treatment of HBEpCs with LPA-induced c-Met serine phosphorylation and redistribution to plasma membrane, while treatment with HGF-induced c-Met internalization. Read More

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November 2007

Involvement of protein kinase C-epsilon in activity-dependent potentiation of large dense-core vesicle exocytosis in chromaffin cells.

J Neurosci 2006 Aug;26(35):8999-9005

Department of Life Science, Division of Molecular and Life Sciences, Systems Biodynamics National Core Research Center, Pohang University of Science and Technology, Pohang, 790-784, South Korea.

Neurotransmitter release is modulated in an activity-dependent manner. We showed previously that repetitive stimulation of nicotinic acetylcholine receptor (nAChR) induced activity-dependent potentiation (ADP) of large dense-core vesicle (LDCV) exocytosis in chromaffin cells. Here we report that protein kinase C (PKC)-epsilon is critically involved in ADP. Read More

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Endothelin-1 and PKC induce positive inotropy without affecting pHi in ventricular myocytes.

Exp Biol Med (Maywood) 2006 Jun;231(6):865-70

Department of Physiology, Molecular and Cellular Pharmacology Training Program, University of Wisconsin, 1300 University Avenue, Madison, Wisconsin 53706, USA.

It has been proposed that intracellular alkalinization underlies the enhanced contractility of ventricular myocytes exposed to endothelin (ET)-1. The effects of ET-1 on the contractility and intracellular pH (pH(i)) were examined here in cultured adult rat ventricular myocytes by employing the pH-sensitive fluorescent dye SNARF-1. Variable pH(i) changes were observed on ET-1 stimulation. Read More

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Dominant-negative PKC-epsilon impairs apical actin remodeling in parallel with inhibition of carbachol-stimulated secretion in rabbit lacrimal acini.

Am J Physiol Cell Physiol 2005 Oct 1;289(4):C1052-68. Epub 2005 Jun 1.

Department of Pharmaceutical Sciences, University of Southern California School of Pharmacy, 1985 Zonal Ave., Los Angeles, California 90033, USA.

We investigated the involvement of PKC-epsilon in apical actin remodeling in carbachol-stimulated exocytosis in reconstituted rabbit lacrimal acinar cells. Lacrimal acinar PKC-epsilon cosedimented with actin filaments in an actin filament binding assay. Stimulation of acini with carbachol (100 microM, 2-15 min) significantly (P < or = 0. Read More

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October 2005

Cigarette smoke extract increases C5a receptor expression in human bronchial epithelial cells.

J Pharmacol Exp Ther 2005 Jul 20;314(1):476-82. Epub 2005 Apr 20.

Pulmonary, Critical Care, and Sleep Medicine Section, Department of Internal Medicine, University of Nebraska Medical Center, 985815 Nebraska Medical Center, Omaha, NE 68198-5815, USA.

We have shown that exposing human bronchial epithelial cells (HBECs) to 5% cigarette smoke extract (CSE) up-regulates C5a anaphylatoxin receptor (C5aR) expression as determined by flow cytometric analysis and immunohistochemistry. In this study, we conducted whole-cell saturation studies to quantitate the receptor number. After exposing an HBEC line (BEAS-2B) to CSE, radiolabeled C5a bound saturably with Kd = 2. Read More

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Alpha2(I) collagen gene regulation by protein kinase C signaling in human dermal fibroblasts.

Nucleic Acids Res 2005 1;33(4):1337-51. Epub 2005 Mar 1.

Department of Dermatology, Faculty of Medicine, University of Tokyo 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8655, Japan.

We investigated the mechanisms by which protein kinase C (PKC) regulates the expression of the alpha2(I) collagen gene in normal dermal fibroblasts. Reduction of PKC-alpha activity by treatment with Gö697-6 or by overexpression of a dominant negative (DN) mutant form decreased alpha2(I) collagen gene expression. This decrease required a sequence element in the collagen promoter that contains Sp1/Sp3 binding sites. Read More

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Differential regulation of angiotensin II-induced expression of connective tissue growth factor by protein kinase C isoforms in the myocardium.

J Biol Chem 2005 Apr 7;280(16):15719-26. Epub 2005 Feb 7.

Research Division, Joslin Diabetes Center, Harvard Medical School and Department of Pathology, Brigham and Women's Hospital, Boston, Massachusetts 02215, USA.

Protein kinase C (PKC) and angiotensin II (AngII) can regulate cardiac function in pathological conditions such as in diabetes or ischemic heart disease. We have reported that expression of connective tissue growth factor (CTGF) is increased in the myocardium of diabetic mice. Now we showed that the increase in CTGF expression in cardiac tissues of streptozotocin-induced diabetic rats was reversed by captopril and islet cell transplantation. Read More

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PKC-delta-dependent activation of oxidative stress in adipocytes of obese and insulin-resistant mice: role for NADPH oxidase.

Am J Physiol Endocrinol Metab 2005 Feb 26;288(2):E405-11. Epub 2004 Oct 26.

Dept. of Human Genetics and Molecular Medicine, Sackler School of Medicine, Tel-Aviv University, Tel-Aviv 69978, Israel.

Oxidative stress is thought to be one of the causative factors contributing to insulin resistance and type 2 diabetes. Previously, we showed that reactive oxygen species (ROS) production is significantly increased in adipocytes from high-fat diet-induced obese and insulin-resistant mice (HF). ROS production was also associated with the increased activity of PKC-delta. Read More

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February 2005

Protein phosphatase 2A negatively regulates insulin's metabolic signaling pathway by inhibiting Akt (protein kinase B) activity in 3T3-L1 adipocytes.

Mol Cell Biol 2004 Oct;24(19):8778-89

Division of Endocrinology and Metabolism, Department of Medicine, Shiga University of Medical Science, Otsu, Japan.

Protein phosphatase 2A (PP2A) is a multimeric serine/threonine phosphatase which has multiple functions, including inhibition of the mitogen-activated protein (MAP) kinase pathway. Simian virus 40 small t antigen specifically inhibits PP2A function by binding to the PP2A regulatory subunit, interfering with the ability of PP2A to associate with its cellular substrates. We have reported that the expression of small t antigen inhibits PP2A association with Shc, leading to augmentation of insulin and epidermal growth factor-induced Shc phosphorylation with enhanced activation of the Ras/MAP kinase pathway. Read More

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October 2004

Protein kinase C-alpha-induced hypertrophy of neonatal rat ventricular myocytes.

Am J Physiol Heart Circ Physiol 2004 Dec 22;287(6):H2777-89. Epub 2004 Jul 22.

Cardiovascular Institute, Loyola Univ. Medical Center, Bldg. 110, Rm. 5232, 2160 S. First Ave., Maywood, IL 60153, USA.

Protein kinase C (PKC) isoenzymes play a critical role in cardiomyocyte hypertrophy. At least three different phorbol ester-sensitive PKC isoenzymes are expressed in neonatal rat ventricular myocytes (NRVMs): PKC-alpha, -delta, and -epsilon. Using replication-defective adenoviruses (AdVs) that express wild-type (WT) and dominant-negative (DN) PKC-alpha together with phorbol myristate acetate (PMA), which is a hypertrophic agonist and activator of all three PKC isoenzymes, we studied the role of PKC-alpha in signaling-specific aspects of the hypertrophic phenotype. Read More

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December 2004

Proteomic analysis reveals a role for protein kinase C-alpha in phagosome maturation.

Biochem Biophys Res Commun 2004 Jul;319(3):810-6

INRS-Institut Armand-Frappier, Université du Québec, Laval, Que., Canada H7V 1B7.

Acquisition of microbicidal properties by phagosomes requires the action of molecules which regulate the interactions between phagosomes and endocytic organelles. Members of the protein kinase C (PKC) superfamily of serine/threonine kinases are recruited to phagosomes with various kinetics during phagolysosome biogenesis. To study the role of PKC-alpha in this process, we compared the composition of latex bead-containing phagosomes isolated from control and dominant-negative (DN) PKC-alpha-overexpressing RAW 264. Read More

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IFN-gamma-induced MHC class II expression: transactivation of class II transactivator promoter IV by IFN regulatory factor-1 is regulated by protein kinase C-alpha.

J Immunol 2003 Oct;171(8):4187-94

Institut National de la Recherche Scientifique-Institut Armand-Frappier, Université du Québec, Laval, Québec, Canada.

Previous studies based on pharmacological evidence suggested a requirement for protein kinase C (PKC) activity in the regulation of IFN-gamma-induced MHC class II (MHC-II) expression. In the present study, we investigated the molecular mechanisms by which PKC-alpha modulates IFN-gamma-induced MHC-II expression in the mouse macrophage cell line RAW 264.7. Read More

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October 2003

Escherichia coli K-1 interaction with human brain micro-vascular endothelial cells triggers phospholipase C-gamma1 activation downstream of phosphatidylinositol 3-kinase.

J Biol Chem 2003 Nov 2;278(46):45753-62. Epub 2003 Sep 2.

Division of Infectious Diseases and Congressman Dixon Image Core, Childrens Hospital Los Angeles, California, USA.

Escherichia coli, the most common Gram-negative bacterium that causes meningitis in neonates, invades human brain microvascular endothelial cells (HBMEC) by rearranging host cell actin via the activation of phosphatidylinositol 3-kinase (PI3K) and PKC-alpha. Here, further, we show that phospholipase (PLC)-gamma1 is phosphorylated on tyrosine 783 and condenses at the HBMEC membrane beneath the E. coli entry site. Read More

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November 2003

Role of protein kinase C alpha for uptake of unopsonized prey and phagosomal maturation in macrophages.

Biochem Biophys Res Commun 2003 Mar;302(4):653-8

Division of Medical Microbiology, Department of Molecular and Clinical Medicine, Faculty of Health Sciences, Linköping University, S-581 85 Linköping, Sweden.

Protein kinase C alpha (PKC alpha) participates in F-actin remodeling during phagocytosis and phagosomal maturation in macrophages. Leishmania donovani promastigotes, which inhibit phagosomal maturation, cause accumulation of periphagosomal F-actin instead of the disassembly observed around other prey [Cell. Microbiol. Read More

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Cross-regulation of novel protein kinase C (PKC) isoform function in cardiomyocytes. Role of PKC epsilon in activation loop phosphorylations and PKC delta in hydrophobic motif phosphorylations.

J Biol Chem 2003 Apr 31;278(16):14555-64. Epub 2003 Jan 31.

Department of Pharmacology, College of Physicians and Surgeons, Columbia University, New York, New York 10032, USA.

Recent studies identify conventional protein kinase C (PKC) isoform phosphorylations at conserved residues in the activation loop and C terminus as maturational events that influence enzyme activity and targeting but are not dynamically regulated by second messengers. In contrast, this study identifies phorbol 12-myristoyl 13-acetate (PMA)- and norepinephrine-induced phosphorylations of PKC epsilon (at the C-terminal hydrophobic motif) and PKC delta (at the activation loop) as events that accompany endogenous novel PKC (nPKC) isoform activation in neonatal rat cardiomyocytes. Agonist-induced nPKC phosphorylations are prevented (and the kinetics of PMA-dependent PKC down-regulation are slowed) by pharmacologic inhibitors of nPKC kinase activity. Read More

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Thrombin stimulation of vascular adhesion molecule-1 in endothelial cells is mediated by protein kinase C (PKC)-delta-NF-kappa B and PKC-zeta-GATA signaling pathways.

J Biol Chem 2003 Feb 18;278(9):6976-84. Epub 2002 Dec 18.

Department of Molecular Medicine, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts 02215, USA.

We recently demonstrated that thrombin induces the expression of vascular adhesion molecule-1 (VCAM-1) in endothelial cells by an NF-kappaB- and GATA-dependent mechanism. In the present study, we describe the signaling pathways that mediate this response. Thrombin stimulation of the VCAM-1 gene and promoter in human umbilical vein endothelial cells was inhibited by preincubation with the phosphatidylinositol 3-kinase inhibitor, LY294002, the protein kinase C (PKC)-delta inhibitor, rottlerin, a PKC-zeta peptide inhibitor, or by overexpression of dominant negative (DN)-PKC-zeta. Read More

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February 2003

Modulation of lipopolysaccharide-induced NF-IL6 activation by protein kinase C-alpha in a mouse macrophage cell line.

Eur J Immunol 2002 Oct;32(10):2897-904

INRS-Institut Armand-Frappier, Université du Québec, 531 des Prairies, Laval, Québec, H7V 1B7 Canada.

We have previously shown that overexpression of a dominant-negative (DN) mutant of protein kinase C-alpha (PKC-alpha) in RAW 264.7 macrophages inhibited lipopolysaccharide (LPS)-induced IL-1alpha, inducible nitric oxide synthase and cyclooxygenase-2 expression. This inhibition was not related to defective NF-kappaB nuclear translocation, suggesting that PKC-alpha might be involved in the modulation of other LPS-inducible transcription factors. Read More

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October 2002

Involvement of protein kinase C beta 2 in c-myc induction by high glucose in pancreatic beta-cells.

J Biol Chem 2002 Feb 19;277(5):3680-5. Epub 2001 Nov 19.

Section on Islet Transplantation and Cell Biology and Section on Vascular Cell Biology, Joslin Diabetes Center, Boston, Massachusetts 02215, USA.

The expression of the basic helix-loop-helix transcription factor c-Myc is induced in pancreatic islets of several different diabetic model animals and is possibly involved in suppression of the insulin gene transcription. In this study, we found that activity of protein kinase C is increased by high glucose, preceding the induction of c-myc expression and that PKC beta2 specifically regulates c-myc expression in pancreatic beta-cells. Since PKC alpha, beta2, delta, epsilon, and zeta were expressed in rat pancreatic islets, we prepared each wild type (WT) and dominant negative type (DN) PKC isoform (alpha, beta2, delta, epsilon, and zeta)-expressing adenovirus to examine the effect of each PKC isoform on c-myc expression. Read More

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February 2002

High glucose-enhanced mesangial cell extracellular signal-regulated protein kinase activation and alpha1(IV) collagen expression in response to endothelin-1: role of specific protein kinase C isozymes.

Diabetes 2001 Oct;50(10):2376-83

Institute of Medical Science, the University Health Network. Department of Medicine, University of Toronto, Toronto, Canada.

High glucose (HG) stimulates glomerular mesangial cell (MC) expression of extracellular matrix, a process involving protein kinase C (PKC) isozymes and enhanced signaling by autocrine peptides such as endothelin-1 (ET-1). The purpose of this study was to identify the specific PKC isozymes mediating the effects of HG on MC extracellular signal-regulated protein kinase (ERK1/2) signaling and alpha1(IV) collagen expression in response to ET-1. HG (30 mmol/l for 72 h) enhanced ET-1-stimulated alpha1(IV) collagen mRNA expression from 1. Read More

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October 2001

Proteinase-activated receptor-2-mediated activation of stress-activated protein kinases and inhibitory kappa B kinases in NCTC 2544 keratinocytes.

J Biol Chem 2001 Aug 18;276(34):31657-66. Epub 2001 Jun 18.

Department of Physiology and Pharmacology, Strathclyde Institute for Biomedical Sciences, University of Strathclyde, 27 Taylor Street, Glasgow G4 ONR, United Kingdom.

In this study we examined the regulation of the stress-activated protein (SAP) kinases and inhibitory kappa B kinases (IKKs) through stimulation of the novel G-protein-coupled receptor proteinase-activated receptor-2 in the human keratinocyte cell line NCTC2544. Trypsin and the peptide SLIGKV stimulated a time-dependent increase in both c-Jun N-terminal kinase and p38 mitogen-activated protein kinase activity. Trypsin also stimulated NF kappa B-DNA binding and the activation of the upstream kinases IKK alpha and -beta. Read More

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