Artículos de revistas
Osteopontin, A Chemotactic Protein With Cytokine-like Properties, Is Up-regulated In Muscle Injury Caused By Bothrops Lanceolatus (fer-de-lance) Snake Venom
Registro en:
Toxicon. , v. 58, n. 5, p. 398 - 409, 2011.
410101
10.1016/j.toxicon.2011.07.011
2-s2.0-80052155938
Autor
Barbosa-Souza V.
Contin D.K.
Filho W.B.
de Araujo A.L.
Irazusta S.P.
da Cruz-Hofling M.A.
Institución
Resumen
Osteopontin (OPN) is a chemotactic, adhesive protein whose receptors include some integrins and matrix proteins known to have role in inflammatory and repair processes. We examined the time course of OPN expression at acute and chronic stages after intramuscular injection of Bothrops lanceolatus venom in rats. Additionally, we examined the expression of CD68 (a marker for phagocytic macrophages) and the myogenic factors, myoD and myogenin. There was a biphasic upregulation of OPN (6-48 h and 3-14 days post-venom), i.e., during acute inflammation and myogenic cell proliferation and differentiation phases. OPN was detected in CD68 + macrophages, fibroblasts, normal and damaged myofibers, myoblasts and myotubes. Myogenin was expressed in the cytoplasm (atypical pattern) and nucleus of myoblasts and myotubes from 18 h to 7 days, after which it was expressed only in nuclei. Macrophage numbers, OPN and myogenin expression were still elevated at 7, 14 and 7 days. At 3 days, when OPN achieved the peak, some clusters of myoblasts were within regions of intense collagen deposition. Fibrosis may represent limitation for repairing processes and may explain the small diameter of regenerated fibers at 21 days post-venom. The expression of OPN in the course of venom-induced damage and regeneration suggests stages-specific mediation role along the whole process. © 2011 Elsevier Ltd. 58 5 398 409 Bogarín, G., Romero, M., Rojas, G., Lutsch, C., Casadamont, M., Lang, J., Otero, R., Gutiérrez, J.M., Neutralization by a monospecific Bothrops lanceolatus antivenom of toxic activities induced by homologous and heterologous Bothrops snake venoms (1999) Toxicon, 37, pp. 551-557 Chargé, S.B., Rudnicki, M.A., Cellular and molecular regulation of muscle regeneration (2004) Physiol. Rev., 84, pp. 209-238 Chazaud, B., Brigitte, M., Yacoub-Youssef, H., Arnold, L., Gherardi, R., Sonnet, C., Lafuste, P., Chrétien, F., Dual and beneficial roles of macrophages during skeletal muscle regeneration (2009) Exerc. Sport Sci. Rev., 37, pp. 18-22 Chen, X., Li, Y., Role of MMP in skeletal muscle: migration, differentiation, regeneration and fibrosis (2009) Cell Adh. Migr., 3, pp. 337-341 Dedieu, S., Mazères, G., Cottin, P., Brustis, J.J., Involvement of myogenic regulator factors during fusion in the cell line C2C12 (2002) Int. J. Dev. Biol., 46, pp. 235-241 Ferri, P., Barbieri, E., Burattini, S., Guescini, M., D'Emilio, A., Biagiotti, L., Del Grande, P., Falcieri, E., Expression and subcellular localization of myogenic regulatory factors during the differentiation of skeletal muscle C2C12 myoblasts (2009) J. Cell Biochem., 108, pp. 1302-1317 Fox, J.W., Serrano, S.M., Insights into and speculations about snake venom metalloproteinases (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity (2008) FEBS J., 275, pp. 3016-3030 Fox, J.W., Serrano, S.M., Timeline of key events in snake venom metalloproteinase research (2009) J. Proteomics, 72, pp. 200-208 França, F.O.S., Málaque, C.M.S., Acidente botrópico (2003) Animais Peçonhentos no Brasil: Biologia, Clínica e Terapêutica dos Acidentes, pp. 72-86. , Sarvier, São Paulo, J.L. Cardoso (Ed.) Guimarães, A.Q., Cruz-Höfling, M.A., Araújo, P.M.F., Bon, C., Lôbo de Araújo, A., Pharmacological and histopathological characterization of Bothrops lanceolatus (Fer de lance) venom-induced edema (2004) Inflamm. Res., 53, pp. 284-291 Gutiérrez, J.M., Ownby, C.L., Skeletal muscle degeneration induced by venom phospholipases A2: insights into the mechanisms of local and systemic myotoxicity (2003) Toxicon, 42, pp. 914-931 Gutiérrez, J.M., Rucavado, A., Escalante, T., Díaz, C., Hemorrhage induced by snake venom metalloproteinases: biochemical and biophysical mechanisms involved in microvessel damage (2005) Toxicon, 45, pp. 997-1011 Gutiérrez, J.M., Sanz, L., Escolano, J., Fernández, J., Lomonte, B., Angulo, Y., Rucavado, A., Calvete, J.J., Snake venomics of the lesser Antillean pit vipers Bothrops caribbaeus and Bothrops lanceolatus: correlation with toxicological activities and immunoreactivity of heterologous antivenom (2008) J. Proteome Res., 7, pp. 4396-4408 Gutiérrez, J.M., Clinical toxicology of snake bites in Central América (1995) Handbook of Clinical Toxicology of Animal Venoms and Poisons, pp. 645-665. , CRC Press, Boca Ratón, Meier, White (Eds.) Heino, J., Käpylä, J., Cellular receptors of extracellular matrix molecules (2009) Curr. Pharm. Des., 15, pp. 1309-1317 Hirata, A., Masuda, S., Tamura, T., Kai, K., Ojima, K., Fukase, A., Motoyoshi, K., Takeda, S., Expression profiling of cytokines and related genes in regenerating skeletal muscle after cardiotoxin injection: a role for osteopontin (2003) Am. J. Pathol., 163, pp. 203-215 Holterman, C.E., Rudnicki, M.A., Molecular regulation of satellite cell function (2005) Semin. Cell Dev. Biol., 16, pp. 575-584 Irita, J., Okura, T., Kurata, M., Miyoshi, K., Fukuoka, T., Higaki, J., Osteopontin in rat renal fibroblasts: functional properties and transcriptional regulation by aldosterone (2008) Hypertension, 51, pp. 507-513 Laing, G.D., Clissa, P.B., Theakston, R.D., Moura-da-Silva, A.M., Taylor, M.J., Inflammatory pathogenesis of snake venom metalloproteinase-induced skin necrosis (2003) Eur. J. Immunol., 33, pp. 3458-3463 Lôbo de Araújo, A., Donato, J.L., Bon, C., Purification from Bothrops lanceolatus (fer de lance) venom of a fibrino(geno)lytic enzyme with esterolytic activity (1998) Toxicon, 36, pp. 745-758 Lôbo de Araújo, A., Kamiguti, A., Bon, C., Coagulant and anticoagulant activities of Bothrops lanceolatus (Fer de lance) venom (2001) Toxicon, 39, pp. 371-375 Lôbo de Araújo, A., Radvanyi, F., Bon, C., Purification of an acidic phospholipase A2 from Bothrops lanceolatus (fer de lance) venom: molecular and enzymatic properties (1994) Toxicon, 32, pp. 1069-1081 Lôbo de Araújo, A., Souza, A.O., Cruz-Höfling, M.A., Flores, C.A., Bon, C., Bothrops lanceolatus (Fer de lance) venom induces oedema formation and increases vascular permeability in mouse hind paw (2000) Toxicon, 38, pp. 209-221 Lorena, D., Darby, I.A., Gadeau, A.P., Leen, L.L., Rittling, S., Porto, L.C., Rosenbaum, J., Desmoulière, A., Osteopontin expression in normal and fibrotic liver. Altered liver healing in osteopontin-deficient mice (2006) J. Hepatol., 44, pp. 383-390 Malbranque, S., Piercecchi-Marti, M.D., Thomas, L., Barbey, C., Courcier, D., Bücher, B., Ridarch, A., Warrell, D.A., Fatal diffuse thrombotic microangiopathy after a bite by the "Fer-de-Lance" pit viper (Bothrops lanceolatus) of Martinique (2008) Am. J. Trop. Med. Hyg., 78, pp. 856-861 Mauro, A., Satellite cell of skeletal muscle fibers (1961) J. Biophys. Biochem. Cytol., 9, pp. 493-495 Merly, F., Lescaudron, L., Rouaud, T., Crossin, F., Gardahaut, M.F., Macrophages enhance muscle satellite cells proliferation and delay their differentiation (1999) Muscle Nerve, 22, pp. 724-732 Mylona, E., Jones, K.A., Mills, S.T., Pavlath, G.K., CD44 regulates myoblast migration and differentiation (2006) J. Cell Physiol., 209, pp. 314-321 Pereira, R.O., Carvalho, S.N., Stumbo, A.C., Rodrigues, C.A.B., Porto, L.C., Moura, A.S., Carvalho, L., Osteopontin expression in coculture of differentiating rat fetal skeletal fibroblasts and myoblasts (2006) In Vitro Cell Dev. Biol. Anim., 42, pp. 4-7 Rosenfeld, G., Symptomatology, pathology, and treatment of snake bites in South America (1971) Venomous Animals and their venoms, pp. 345-841. , Academic Press, New York, W. Bücherl, E.E. Buckley, V. Delofeu (Eds.) Rucavado, A., Escalante, T., Teixeira, C.F., Fernándes, C.M., Díaz, C., Gutiérrez, J.M., Increments in cytokines and matrix metalloproteinases in skeletal muscle after injection of tissue-damaging toxins from the venom of the snake Bothrops asper (2002) Mediators Inflamm., 11, pp. 121-128 Rucavado, A., Nuñes, J., Gutiérrez, J.M., Blister formation and skin damage induced by BaP1, a haemorrhagic metalloptotease from the venom of the snake Bothrops asper (1998) Int. J. Exp. Pathol, 79, pp. 245-254 Sanchez, E.F., Schneider, F.S., Yarleque, A., Borges, M.H., Richardson, M., Figueiredo, S.G., Evangelista, K.S., Eble, J., The novel metalloproteinase atroxlysin-I from Peruvian Bothrops atrox (Jergón) snake venom acts both on blood vessel ECM and platelets (2010) Arch. Biochem. Biophys., 496, pp. 9-20 Scatena, M., Liaw, L., Giachelli, C.M., Osteopontin: a multifunctional molecule regulating chronic inflammation and vascular disease (2007) Arterioscler. Thromb. Vasc. Biol., 27, pp. 2302-2309 Singh, M., Foster, C.R., Dalal, S., Singh, K., Osteopontin: role in extracellular matrix deposition and myocardial remodeling post-MI (2010) J. Mol. Cell Cardiol., 48, pp. 538-543 Stocker, K., Christ, W., Leloup, P., Characterization of the venoms of various Bothrops species by immunoelectrophoresis and reaction with fibrinogen agarose (1974) Toxicon, 12, pp. 415-417 Stroka, A., Donato, J.L., Bon, C., Hyslop, S., Lôbo de Araújo, A., Purification and characterization of a hemorrhagic metalloproteinase from Bothrops lanceolatus (Fer-de-lance) snake venom (2005) Toxicon, 45, pp. 411-420 Thomas, L., Tyburn, B., Bucher, B., Pecout, F., Ketterlé, J., Rieux, D., Smadja, D., Plumelle, Y., Prevention of thromboses in human patients with Bothrops lanceolatus envenoming in Martinique: failure of anticoagulants and efficacy of a monospecific antivenom. Research Group on Snake Bites in Martinique (1995) Am. J. Trop. Med. Hyg., 52, pp. 419-426 Tidball, J.G., Inflammatory processes in the muscle injury and repair (2005) Am. J. Physiol. Regul. Integr. Comp. Physiol., 288, pp. R345-R353 Tidball, J.G., Villalta, S.A., Regulatory interactions between muscle and the immune system during muscle regeneration (2010) Am. J. Physiol. Regul. Integr. Comp. Physiol., 298, pp. R1173-R1187 Uaesoontrachoon, K., Yoo, H.J., Tudor, E.M., Pike, R.N., Mackie, E.J., Pagel, C.N., Osteopontin and skeletal muscle myoblast: association with muscle regeneration and regulation of myoblast function in vitro (2008) Int. J. Biochem. Cell Biol., 10, pp. 2303-2314 Vetrone, S.A., Montecino-Rodriguez, E., Kudryashova, E., Kramerova, I., Hoffman, E.P., Liu, S.D., Miceli, M.C., Spencer, M.J., Osteopontin promotes fibrosis in dystrophic mouse muscle by modulating immune cell subsets and intramuscular TGF-β (2009) J. Clin. Invest., 119, pp. 1583-1594 Wang, K.X., Denhardt, D.T., Osteopontin: role in immune regulation and stress responses (2008) Cytokine Growth Factor Rev., 19, pp. 333-345 Yokosaki, Y., Matsuura, N., Sasaki, T., Murakami, I., Schneider, H., Higashiyama, S., Saitoh, Y., Sheppard, D., The integrin α9β1 binds to a novel recognition sequence (SVVYGLR) in the thrombin-cleaved amino-terminal fragment of osteopontin (1999) J. Biol. Chem., 274, pp. 36328-36334 Yokosaki, Y., Tanaka, K., Higashikawa, F., Yamashita, K., Eboshida, A., Distinct structural requirements for binding of the integrins αvβ6, αvβ3, αvβ5, α5β1 and α9β1 to osteopontin (2005) Matrix Biol., 24, pp. 418-427