Osteopontin, a chemotactic protein with cytokine-like properties, is up-regulated in muscle injury caused by Bothrops lanceolatus (fer-de-lance) snake venom

Toxicon

Volumn 58, Issue 5, 2011, Pages 398-409

  Barbosa Souza, Valéria ^a   Contin, Daniel Kiss ^a   Filho, Waldemar Bonventi ^b   de Araújo, Albetiza Lôbo ^a   Irazusta, Silvia Pierre ^a,b,c   da Cruz Höfling, Maria Alice ^a  

^a UNIVERSITY OF CAMPINAS   (Brazil)

^b Faculdade de Tecnologia de Sorocaba   (Brazil)

^c School CEETPS   (Brazil)

Author keywords

Bothropic venom; CD68 macrophage; Muscle regeneration; Myogenin; Myonecrosis; Osteopontin

Indexed keywords

CD68 ANTIGEN; MYOD PROTEIN; MYOGENIN; OSTEOPONTIN; SNAKE VENOM;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CELL COUNT; CELL DIFFERENTIATION; CELL PROLIFERATION; CONTROLLED STUDY; ENVENOMATION; HISTOPATHOLOGY; IMMUNOHISTOCHEMISTRY; MALE; MORPHOMETRICS; MUSCLE INJURY; MUSCLE REGENERATION; MYOFIBROSIS; NONHUMAN; POISONOUS SNAKE; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; RAT;

ANIMALS; ANTIGENS, CD; ANTIGENS, DIFFERENTIATION, MYELOMONOCYTIC; BOTHROPS; CELL PROLIFERATION; CROTALID VENOMS; IMMUNOHISTOCHEMISTRY; MUSCLES; OSTEOPONTIN; RATS; RATS, WISTAR; UP-REGULATION;

BOTHROPS LANCEOLATUS; RATTUS;

EID: 80052155938     PISSN: 00410101     EISSN: 18793150     Source Type: Journal    
DOI: 10.1016/j.toxicon.2011.07.011     Document Type: Article

References (45)

1. 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. Toxicon 1999, 37:551-557.
2. Chargé S.B., Rudnicki M.A. Cellular and molecular regulation of muscle regeneration. Physiol. Rev. 2004, 84:209-238.
3. 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. Exerc. Sport Sci. Rev. 2009, 37:18-22.
4. Chen X., Li Y. Role of MMP in skeletal muscle: migration, differentiation, regeneration and fibrosis. Cell Adh. Migr. 2009, 3:337-341.
5. Dedieu S., Mazères G., Cottin P., Brustis J.J. Involvement of myogenic regulator factors during fusion in the cell line C2C12. Int. J. Dev. Biol. 2002, 46:235-241.
6. Ferri P., Barbieri E., Burattini S., Guescini M., D'Emilio A., Biagiotti L., Del Grande P., De Luca A., Stocchi V., Falcieri E. Expression and subcellular localization of myogenic regulatory factors during the differentiation of skeletal muscle C2C12 myoblasts. J. Cell Biochem. 2009, 108:1302-1317.
7. 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. FEBS J. 2008, 275:3016-3030.
8. Fox J.W., Serrano S.M. Timeline of key events in snake venom metalloproteinase research. J. Proteomics 2009, 72:200-208.
9. França F.O.S., Málaque C.M.S., et al. Acidente botrópico. Animais Peçonhentos no Brasil: Biologia, Clínica e Terapêutica dos Acidentes 2003, 72-86. Sarvier, São Paulo. J.L. Cardoso (Ed.).
10. 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. Inflamm. Res. 2004, 53:284-291.
11. Gutiérrez J.M., Ownby C.L. Skeletal muscle degeneration induced by venom phospholipases A2: insights into the mechanisms of local and systemic myotoxicity. Toxicon 2003, 42:914-931.
12. Gutiérrez J.M., Rucavado A., Escalante T., Díaz C. Hemorrhage induced by snake venom metalloproteinases: biochemical and biophysical mechanisms involved in microvessel damage. Toxicon 2005, 45:997-1011.
13. Gutiérrez J.M., Sanz L., Escolano J., Fernández J., Lomonte B., Angulo Y., Rucavado A., Warrell D.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. J. Proteome Res. 2008, 7:4396-4408.
14. Gutiérrez J.M. Clinical toxicology of snake bites in Central América. Handbook of Clinical Toxicology of Animal Venoms and Poisons 1995, 645-665. CRC Press, Boca Ratón. Meier, White (Eds.).
15. Heino J., Käpylä J. Cellular receptors of extracellular matrix molecules. Curr. Pharm. Des. 2009, 15:1309-1317.
16. Hirata A., Masuda S., Tamura T., Kai K., Ojima K., Fukase A., Motoyoshi K., Kamakura K., Miyagoe-Suzuki Y., Takeda S. Expression profiling of cytokines and related genes in regenerating skeletal muscle after cardiotoxin injection: a role for osteopontin. Am. J. Pathol. 2003, 163:203-215.
17. Holterman C.E., Rudnicki M.A. Molecular regulation of satellite cell function. Semin. Cell Dev. Biol. 2005, 16:575-584.
18. Irita J., Okura T., Kurata M., Miyoshi K., Fukuoka T., Higaki J. Osteopontin in rat renal fibroblasts: functional properties and transcriptional regulation by aldosterone. Hypertension 2008, 51:507-513.
19. 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. Eur. J. Immunol. 2003, 33:3458-3463.
20. 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. Toxicon 1998, 36:745-758.
21. Lôbo de Araújo A., Kamiguti A., Bon C. Coagulant and anticoagulant activities of Bothrops lanceolatus (Fer de lance) venom. Toxicon 2001, 39:371-375.
22. 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. Toxicon 1994, 32:1069-1081.
23. 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. Toxicon 2000, 38:209-221.
24. 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. J. Hepatol. 2006, 44:383-390.
25. Malbranque S., Piercecchi-Marti M.D., Thomas L., Barbey C., Courcier D., Bücher B., Ridarch A., Smadja D., Warrell D.A. Fatal diffuse thrombotic microangiopathy after a bite by the "Fer-de-Lance" pit viper (Bothrops lanceolatus) of Martinique. Am. J. Trop. Med. Hyg. 2008, 78:856-861.
26. Mauro A. Satellite cell of skeletal muscle fibers. J. Biophys. Biochem. Cytol. 1961, 9:493-495.
27. Merly F., Lescaudron L., Rouaud T., Crossin F., Gardahaut M.F. Macrophages enhance muscle satellite cells proliferation and delay their differentiation. Muscle Nerve 1999, 22:724-732.
28. Mylona E., Jones K.A., Mills S.T., Pavlath G.K. CD44 regulates myoblast migration and differentiation. J. Cell Physiol. 2006, 209:314-321.
29. 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. In Vitro Cell Dev. Biol. Anim. 2006, 42:4-7.
30. Rosenfeld G. Symptomatology, pathology, and treatment of snake bites in South America. Venomous Animals and their venoms 1971, 345-841. Academic Press, New York. W. Bücherl, E.E. Buckley, V. Delofeu (Eds.).
31. 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. Mediators Inflamm. 2002, 11:121-128.
32. 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. Int. J. Exp. Pathol 1998, 79:245-254.
33. 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. Arch. Biochem. Biophys. 2010, 496:9-20.
34. Scatena M., Liaw L., Giachelli C.M. Osteopontin: a multifunctional molecule regulating chronic inflammation and vascular disease. Arterioscler. Thromb. Vasc. Biol. 2007, 27:2302-2309.
35. Singh M., Foster C.R., Dalal S., Singh K. Osteopontin: role in extracellular matrix deposition and myocardial remodeling post-MI. J. Mol. Cell Cardiol. 2010, 48:538-543.
36. Stocker K., Christ W., Leloup P. Characterization of the venoms of various Bothrops species by immunoelectrophoresis and reaction with fibrinogen agarose. Toxicon 1974, 12:415-417.
37. 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. Toxicon 2005, 45:411-420.
38. Thomas L., Tyburn B., Bucher B., Pecout F., Ketterlé J., Rieux D., Smadja D., Garnier 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. Am. J. Trop. Med. Hyg. 1995, 52:419-426.
39. Tidball J.G. Inflammatory processes in the muscle injury and repair. Am. J. Physiol. Regul. Integr. Comp. Physiol. 2005, 288:R345-R353.
40. Tidball J.G., Villalta S.A. Regulatory interactions between muscle and the immune system during muscle regeneration. Am. J. Physiol. Regul. Integr. Comp. Physiol. 2010, 298:R1173-R1187.
41. 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. Int. J. Biochem. Cell Biol. 2008, 10:2303-2314.
42. 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. J. Clin. Invest. 2009, 119:1583-1594.
43. Wang K.X., Denhardt D.T. Osteopontin: role in immune regulation and stress responses. Cytokine Growth Factor Rev. 2008, 19:333-345.
44. Yokosaki Y., Matsuura N., Sasaki T., Murakami I., Schneider H., Higashiyama S., Saitoh Y., Yamakido M., Taooka Y., Sheppard D. The integrin α9β1 binds to a novel recognition sequence (SVVYGLR) in the thrombin-cleaved amino-terminal fragment of osteopontin. J. Biol. Chem. 1999, 274:36328-36334.
45. 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. Matrix Biol. 2005, 24:418-427.