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2003 | 50 | 3 | 837-847
Article title

Metabolism of cyclic GMP in peritoneal macrophages of rat and guinea pig.

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Abstracts
EN
The aim of our studies was to establish which enzymes constitute the "cGMP pathway" in rat and guinea pig peritoneal macrophages (PM). We found that in guinea pig PM synthesis of the nucleotide was significantly enhanced in response to activators of soluble guanylyl cyclase (sGC) and it was only slightly stimulated by specific activators of particulate guanylyl cyclases (pGC). In contrast, rat PM responded strongly to atrial natriuretic peptide (ANP), the activator of pGC type A. The rat cells synthesized about three-fold more cGMP than an equal number of the guinea pig cells. The activity of phosphodiesterases (PDE) hydrolyzing cGMP was apparently regulated by cGMP itself in PM of both species and again it was higher in the rat cells than in those isolated from guinea pig. However, guinea pig PM revealed an activity of Ca2+/calmodulin-dependent PDE1, which was absent in the rat cells. Using Western blotting analysis we were unable to detect the presence of cGMP-dependent protein kinase 1 (PKG1) in PM isolated from either species. In summary, our findings indicate that particulate GC-A is the main active form of GC in the rat PM, while in guinea pig macrophages the sGC activity dominates. Since the profiles of the PDE activities in rat and guinea pig PM are also different, we conclude that the mechanisms regulating cGMP metabolism in PM are species-specific. Moreover, our results suggest that targets for cGMP other than PKG1 should be present in PM of both species.
Publisher

Year
Volume
50
Issue
3
Pages
837-847
Physical description
Dates
published
2003
received
2003-06-26
revised
2003-08-07
accepted
2003-08-12
Contributors
  • Laboratory of Signaling Proteins, L. Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wrocław, Poland
  • Laboratory of Signaling Proteins, L. Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wrocław, Poland
  • Laboratory of Signaling Proteins, L. Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wrocław, Poland
  • Laboratory of Signaling Proteins, L. Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wrocław, Poland
References
  • Bellamy TC, Garthwaite J. (2002) The receptor-like properties of nitric oxide-activated soluble guanylyl cyclase in intact cells. Mol Cell Biochem.; 230: 165-76.
  • Bilzer M, Jaeschke H, Vollmar AM, Paumgartner G, Gerbes AL. (1999) Prevention of Kupffer cell-induced oxidant injury in rat liver by atrial natriuretic peptide. Am J Physiol.; 276: G1137-44.
  • Connelly L, Jacobs AT, Palacios-Callender M, Moncada S, Hobbs AJ. (2003) Macrophage endothelial nitric-oxide synthase auto-regulates cellular activation and pro-inflammatory protein expression. J Biol Chem.; 278: 26480-7.
  • Dejda A, Matczak I, Gorczyca WA. (2002) P19 detected in the rat retina and pineal gland is a guanylyl cyclase-activating protein (GCAP). Acta Biochim Polon.; 49: 899-905.
  • Fisher TA, Palmetshofer A, Gambaryan S, Butt E, Jassoy C, Walter U, Sopper S, Lohmann SM. (2001) Activation of cGMP-dependent protein kinase Iβ inhibits interleukin 2 release and proliferation of T cell receptor-stimulated human peripheral T cells. J Biol Chem.; 276: 5967-74.
  • Francis SH, Turko IV, Corbin JD. (2001) Cyclic nucleotide phosphodiesterases: relating structure and function. Prog Nucleic Acid Res Mol Biol.; 65: 1-52.
  • Galea E, Feinstein DI. (1999) Regulation of the expression of the inflammatory nitric oxide synthase (NOS2) by cyclic AMP. FASEB J.; 13: 2125-37.
  • Gantner F, Kupferschmidt R, Schudt C, Wendel A, Hatzelmann A. (1997) In vitro differentiation of human monocytes to macrophages: change of PDE profile and its relationship to suppression of tumour necrosis factor-α release by PDE inhibitors. Br J Pharmacol.; 121: 221-31.
  • Germain N, Bertin B, Legendre A, Martin B, Lagente V, Payne A, Bichot E. (1998) Selective phosphodiesterase inhibitors modulate the activity of alveolar macrophages from sensitized guinea-pigs. Eur Respir J.; 12: 1334-9.
  • Gorczyca WA, Kobiałka M, Kuropatwa M, Kurowska E. (2003). Ca2+ differently affects hydrophobic properties of guanylyl cyclase-activating proteins (GCAPs) and recoverin. Acta Biochim Polon.; 50: 367-76.
  • Gorczyca W, Wieczorek Z, Lisowski J. (1989) Cell surface sialic acid affects immunoglobulin binding to macrophages. FEBS Lett.; 259: 99-102.
  • Hahn PY, Yoo P, Ba ZF, Chaudry IH, Wan P. (1998) Upregulation of Kupffer cell β-adrenoceptors and cAMP levels during the late stage of sepsis. Biochim Biophys Acta.; 1404: 377-84.
  • Heinloth A, Brune B, Fisher B, Galle J. (2002) Nitric oxide prevents oxidized LDL-induced p53 accumulation, cytochrome c translocation, and apoptosis in macrophages via guanylate cyclase stimulation. Atherosclerosis.; 162: 93-101.
  • Hill JR, Corbett JA, Kwon G, Marshall CA, McDaniel ML. (1996) Nitric oxide regulates interleukin 1 bioactivity released from murine macrophages. J Biol Chem.; 271: 22672-8.
  • Hortelano S, Genaro AM, Bosca L. (1993) Phorbol esters induce nitric oxide synthase and increase arginine influx in cultured peritoneal macrophages. FEBS Lett.; 320: 135-9.
  • Horton JK, Baxendale PM. (1995) Mass measurements of cyclic AMP formation by radioimmunoassay, enzyme immunoassay, and scintillation proximity assay. Methods Mol Biol.; 41: 91-105.
  • Houdijk AP, Adolfs MJ, Bonta IL, De Jone HR. (1990) Atriopeptins and nitroprusside provoke opposite changes in cGMP and cAMP levels in human macrophages. Eur J Pharmacol.; 179: 413-7.
  • Ivanova K, Das PK, Van Den Wijngaard R, Lenz W, Klockenbring T, Malcharzyk V, Drummer C, Gerzer R. (2001) Differential expression of functional guanylyl cyclase in melanocytes: absence of nitric-oxide-sensitive isoform in metastatic cells. J Invest Dermatol.; 116: 409-16.
  • Jaramillo M, Olivier M. (2002) Hydrogen peroxide induces murine macrophage chemokine gene transcription via extracellular signal-regulated kinase- and cyclic adenosine 5'-monophosphate (cAMP)-dependent pathways: involvement of NF-κB, activator protein 1, and cAMP response element binding protein. J Immunol.; 169: 7026-38.
  • Kamisato S, Uemura Y, Takami N, Okamoto K. (1997) Involvement of intracellular cyclic GMP and cyclic GMP-dependent protein kinase in alpha-elastin-induced macrophage chemotaxis. J Biochem.; 121: 862-7.
  • Ke XC, Terashima M, Nariai Y, Nakashima Y, Nabika T, Tanigawa Y. (2001) Nitric oxide regulates actin reorganization through cGMP and Ca2+/calmodulin in RAW 264.7 cells. Biochim Biophys Acta.; 1539: 101-13.
  • Kelly JJ, Barnes PJ, Giembycz MA. (1998) Characterization of phosphodiesterase 4 in guinea-pig macrophages: multiple activities, association states and sensitivity to selective inhibitors. Br J Pharmacol.; 124: 129-40.
  • Kiemer AK, Baron A, Gerbes AL, Bilzer M, Vollmar AM. (2002) The atrial natriuretic peptide as a regulator of Kupffer cell functions. Shock.; 17: 365-71
  • Kiemer AK, Hartung T, Vollmar AM. (2000) cGMP-mediated inhibition of TNF-alpha production by the atrial natriuretic peptide in murine macrophages. J Immunol.; 165: 175-81.
  • Kiemer AK, Vollmar AM. (1998) Autocrine regulation of inducible nitric-oxide synthase in macrophages by atrial natriuretic peptide. J Biol Chem.; 273: 13444-51.
  • Kobiałka M, Gorczyca WA. (2000) Particulate guanylyl cyclases: multiple mechanisms of activation. Acta Biochim Polon.; 47: 517-28.
  • Kobiałka M, Kochanowska IE, Gorczyca WA. (2002) Determination of intracellular cAMP and cGMP using ELISA method. Diagn Lab.; 38: 165-74.
  • Koesling D. (1998) Modulators of soluble guanylyl cyclase. Naunyn-Schmiedeberg's Arch Pharmacol.; 358: 123-6.
  • Kurowska E, Kobiałka M, Zioło E, Strządała L, Gorczyca WA. (2002) The cGMP synthesis and PKG1 expression in murine lymphoid organs. Arch Immunol Ther Exp (Warsz).; 50: 289-94.
  • Lohmann SM, Vaandrager AB, Smolenski A, Walter U, De Jonge HR. (1997) Distinct and specific functions of cGMP-dependent protein kinases. Trends Biochem Sci.; 22: 307-12.
  • Lucas KA, Pitari GM, Kazerounian S, Ruiz-Stewart I, Park J, Schulz S, Chepenik KP, Waldman SA. (2000) Guanylyl cyclases and signaling by cyclic GMP. Pharmacol Rev.; 52: 375-413.
  • Mattana J, Singhal PC. (1993) Effects of atrial natriuretic peptide and cGMP on uptake of IgG complexes by macrophages. Am J Physiol.; 265: C92-8.
  • Morita R, Ukyo N, Furuya M, Uchiyama T, Hori T. (2003) Atrial natriuretic peptide polarizes human dendritic cells toward a Th2-promoting phenotype through its receptor guanylyl cyclase-coupled receptor A. J Immunol.; 170: 5869-75
  • O'Dorisio MS, Fertel R, Finkler E, Brooks R, Vassalo L. (1984) Characterization of cyclic nucleotide metabolism during human monocyte differentiation. J Leukoc Biol.; 35: 617-30.
  • Paolucci C, Rovere P, De Nadai C, Manfredi AA, Clementi E. (2000) Nitric oxide inhibits the tumor necrosis factor alpha-regulated endocytosis of human dendritic cells in a cyclic GMP-dependent way. J Biol Chem.; 275: 19638-44.
  • Prpic V, Uhing RJ, Gettys TW. (1993) Separation and assay of phosphodiesterase isoforms in murine macrophages using membrane matrix DEAE chromatography and [32P]cAMP. Anal Biochem.; 208: 155-60.
  • Pryzwansky KB, Kidao S, Wyatt TA, Reed W, Lincoln TM. (1995) Localization of cyclic GMP-dependent protein kinase in human mononuclear phagocytes. J Leukoc Biol.; 57: 670-8.
  • Soderling SH, Beavo JA. (2000) Regulation of cAMP and cGMP signaling: new phosphodiesterase and new functions. Curr Opin Cell Biol.; 12: 174-9.
  • Syrovets T, Tippler B, Rieks M, Simmet T. (1997) Plasmin is a potent and specific chemoattractant for human peripherial monocytes acting via a cyclic guanosine monophosphate-dependent pathway. Blood.; 89: 4574-83.
  • Tamion F, Richard V, Lyuomi S, Hiron M, Bonmarchand G, Leroy J, Daveau M, Thuillez C, Lebreton J-P. (1999) Induction of haem oxygenase contributes to the synthesis of pro-inflammatory cytokines in re-oxygenated macrophages: role of cGMP. Cytokine.; 11: 326-33.
  • Tenor H, Hatzelmann A, Kupferschmidt R, Stanciu L, Djukanovic R, Schudt C, Wendel A, Church MK, Shute JK. (1995) Cyclic nucleotide phosphodiesterase izoenzyme activities in human alveolar macrophages. Clin Exp Allergy.; 25: 625-33.
  • Throsby M, Yang Z, Lee D, Huang W, Copolov DL, Lim AT. (1993) In vitro evidence for atrial natriuretic factor-(5-28) production by macrophages of adult rat thymi. Endocrinology.; 132: 2184-90.
  • Turner NC, Wood LJ, Burns FM, Gueremy T, Souness JE. (1993) The effect of cyclic AMP and cyclic GMP phosphodiesterase inhibitors on the superoxide burst of guinea-pig peritoneal macrophages. Br J Pharmacol.; 108: 876-83.
  • Vaandrager AB. (2002) Structure and function of the heat-stable enerotoxin receptor/guanylyl cyclase C. Mol Cell Biochem.; 230: 73-83.
  • Witwicka H, Kobiałka M, Gorczyca WA. (2002) Hydrolysis of cyclic GMP in rat peritoneal macrophages. Acta Biochim Polon.; 49: 891-7.
  • Yoshioka Y, Yamamuro A, Maeda S. (2003) Nitric oxide at a low concentration protects murine macrophage RAW264 cells against nitric oxide-induced death via cGMP signaling pathway. Br J Pharmacol.; 139: 28-34.
  • Zolle O, Lawrie AM, Simpson AW. (2000) Activation of the particulate and not the soluble guanylate cyclase leads to the inhibition of Ca2+ extrusion through localized elevation of cGMP. J Biol Chem.; 275: 25892-9.
Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv50i3p837kz
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