19 research outputs found
Characterization Of The Crotalus Durissus Terrificus Venom By Atomic Force Microscopy
A preliminary analysis of the morphology of crude CDT venom was performed using atomic force microscopy (AFM). As a result, a direct measurement of the forces between the surface of the venom crystals and a sharp probe tip was achieved.20413171321Azevedo Marques, M.M., Cupo, P., Coimbra, T.M., Hering, S.E., Rossi, M.A., Laure, C.J., (1985) Toxicon, 23, p. 631Sanchez, E.E., Soliz, L.A., Susana Ramirez, M., Perez, J.C., (2001) Toxicon, 39, p. 523Soares, A.M., Mancin, A.C., Cecchini, A.L., Arantes, E.C., Franca, S.C., Gutierrez, J.M., Giglio, J.R., (2001) Int. J. Biochem. Cell Biol., 33, p. 877Choumet, V., Lafaye, P., Demangel, C., Bon, C., Mazie, J.C., (1999) Biol. Chem., 380, p. 561Sanchez, S.A., Chen, Y., Muller, J.D., Gratton, E., Hazlett, T.L., (2001) Biochemistry, 40, p. 6903Sharma, S., Jabeen, T., Singh, J.K., Bredhorst, R., Vogel, C.W., Betzel, C., Singh, T.P., (2001) Acta Crystallogr., Sect. D: Biol. Crystallogr., 57, p. 596Nonato, M.C., Garrat, R.C., Mascarenhas, Y.P., Jesus, W.D.P., Assakura, M.T., Serrano, S.M.T., Oliva, G., (2001) Biol. Crystallogr., D, 57, p. 599Arni, R.K., Ward, R.J., (1996) Toxicon, 34, p. 827Souza, D.H.F., Selistre-deAraujo, H.S., Garratt, R.C., (2000) Toxicon, 38, p. 1307Binning, G., Coate, C.F., Gerber, G., (1986) Phys. Rev. Lett., 56, p. 930Baranauskas, V., Vidal, B.C., Parizotto, N.A., (1998) Appl. Biochem. Biotechnol., 69, p. 91Baranauskas, V., Garavello-Freitas, I., Jingguo, Z., Cruz-Hofling, M.A., (2001) J. Vac. Sci. Technol. A, 19, p. 104
Expression Of Vegf And Flk-1 And Flt-1 Receptors During Blood-brain Barrier (bbb) Impairment Following Phoneutria Nigriventer Spider Venom Exposure
Apart from its angiogenic and vascular permeation activity, the vascular endothelial growth factor (VEGF) has been also reported as a potent neuronal protector. Newborn rats with low VEGF levels develop neuron degeneration, while high levels induce protective mechanisms in several neuropathological conditions. Phoneutria nigriventer spider venom (PNV) disrupts the blood-brain barrier (BBB) and causes neuroinflammation in central neurons along with excitotoxic signals in rats and humans. All these changes are transient. Herein, we examined the expression of VEGF and its receptors, Flt-1 and Flk-1 in the hippocampal neurons following envenomation by PNV. Adult and neonatal rats were evaluated at time limits of 2, 5 and 24 h. Additionally, BBB integrity was assessed by measuring the expression of occludin, β-catenin and laminin and neuron viability was evaluated by NeuN expression. VEGF, Flt-1 and Flk-1 levels increased in PNV-administered rats, concurrently with respective mRNAs. Flt-1 and Flk-1 immunolabeling was nuclear in neurons of hippocampal regions, instead of the VEGF membrane-bound typical location. These changes occurred simultaneously with the transient decreases in BBB-associated proteins and NeuN positivity. Adult rats showed more prominent expressional increases of the VEGF/Flt-1/Flk-1 system and earlier recovery of BBB-related proteins than neonates. We conclude that the reactive expressional changes seen here suggest that VEGF and receptors could have a role in the excitotoxic mechanism of PNV and that such role would be less efficient in neonate rats. © 2013 by the authors; licensee MDPI, Basel, Switzerland.51225722588Vassilevsky, A.A., Koslov, S.A., Egorov, T.A., Grishin, E.V., Purification and characterization of biologically active peptides from spider venoms (2010) Methods Mol. Biol., 615, pp. 87-100Reis, H.J., Prado, M.A., Kalapothakis, E., Cordeiro, M.N., Diniz, C.R., de Marco, L.A., Gomez, M.V., Romano-Silva, M.A., Inhibition of glutamate uptake by a polypeptide toxin (phoneutriatoxin 3-4) from the spider Phoneutria nigriventer (1999) Biochem. J., 343, pp. 413-418Gomez, M.V., Kalapothakis, E., Guatimosim, C., Prado, M.A., Phoneutria nigriventer venom: A cocktail of toxins that affect ion channels (2002) Cell. Mol. Neurobiol., 22, pp. 579-588Bucaretchi, F., Deus Reinaldo, C.R., Hyslop, S., Madureira, P.R., de Capitani, E.M., Vieira, R.J., A clinico-epidemiological study of bites by spiders of the genus Phoneutria (2000) Rev. Inst. Med. Trop. São Paulo, 42, pp. 17-21Le Sueur, L., Kalapothakis, E., Cruz-Höfling, M.A., Breakdown of the blood-brain barrier and neuropathological changes induced by Phoneutria nigriventer spider venom (2003) Acta Neuropathol., 105, pp. 125-134Le Sueur, L., Collares-Buzato, C.B., Cruz-Höfling, M.A., Mechanisms involved in the blood-brain barrier increased permeability induced by Phoneutria nigriventer spider venom in rats (2004) Brain Res., 1027, pp. 38-47Rapôso, C., Odorissi, P.A.M., Oliveira, A.L.R., Aoyama, H., Ferreira, C.V., Verinaud, L., Fontana, K., da Cruz-Höfling, M.A., Effect of Phoneutria nigriventer venom on the expression of junctional protein and P-gp efflux pump function in the blood-brain barrier (2012) Neurochem. Res., 37, pp. 1967-1981Nag, S., Kapadia, A., Stewart, D.J., Review: Molecular pathogenesis of blood-brain barrier breakdown in acute brain injury (2011) Neuropathol. Appl. Neurobiol., 37, pp. 3-23Olsson, A.K., Dimberg, A., Kreuger, J., Claesson-Welsh, L., VEGF receptor signaling in control of vascular function (2006) Nat. Rev. Mol. Cell Biol., 7, pp. 359-371Sköld, M.K., Risling, M., Holmin, S., Inhibition of vascular endothelial growth factor receptor 2 activity in experimental brain contusions aggravates injury outcome and leads to early increased neuronal and glial degeneration (2006) Eur. J. Neurosci., 23, pp. 21-34Ruiz de Almodovar, C., Lambrechts, D., Mazzone, M., Carmeliet, P., Role and therapeutic potential of VEGF in the nervous system (2009) Physiol. Rev., 89, pp. 607-648Morin-Brureau, M., Rigau, V., Lerner-Natoli, M., Why and how to target angiogenesis in focal epilepsies (2012) Epilepsia, 53, pp. 64-68Rapôso, C., Zago, G.M., Silva, G.H., Cruz-Höfling, M.A., Acute blood brain barrier permeabilization in rats after systemic Phoneutria nigriventer venom (2007) Brain Res., 1149, pp. 18-29Mendonça, M.C., Soares, E.S., Stávale, L.M., Irazusta, S.P., Cruz-Höfling, M.A., Upregulation of the vascular endothelial growth factor, Flt-1, in rat hippocampal neurons after envenoming by Phoneutria nigriventerage-related modulation (2012) Toxicon, 60, pp. 656-664Cruz-Höfling, M.A., Zago, G.M., Melo, L.L., Rapôso, C., C-FOS and n-NOS reactive neurons in response to circulating Phoneutria nigriventer spider venom (2007) Brain Res. 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Histoenzymological And Ultrastructural Changes In Lateral Muscle Fibers Of Oreochromis Niloticus (teleostei: Cichlidae) After Local Injection Of Veratrine
The effects of veratrine have been investigated in mammalian, amphibian, and crustacean muscle, but not in fish. In this work, the action of veratrine was studied in the lateral muscle of the freshwater teleost Oreochromis niloticus after intramuscular injection. Histoenzymological typing and electron microscopy of muscle fibers before and 15, 30, and 60 min after veratrine injection (10 ng/kg fish) were used to indirectly assess the morphological changes and the oxidative and m-ATPase activities. In some cases, muscles were pretreated with tetrodotoxin to determine whether the ultrastructural changes were the result of Na+ channel activation by veratrine. Veratrine altered the metabolism of fibers mainly after 30 min. Oxidative fibers showed decreased NADH-TR activity, whereas that of glycolytic and oxidative-glycolytic type fibers increased. There was no change in the m-ATPase activity of the three fiber types, except at 60 min postveratrine, when a novel fiber type, which showed no reversal after acidic and alkaline preincubations, appeared. Ultrastructural damage involved sarcomeres, myofibrils, and mitochondria, but the T-tubules remained intact. Pretreatment with tetrodotoxin (1 ng/ml) prevented the ultrastructural changes caused by veratrine. These results show that in fish skeletal muscle veratrine produces some effects that are not seen in mammalian muscle.1166525534Battersby, B.J., Moyes, C.D., Influence of acclimation temperature on mitochondrial DNA, RNA, and enzymes in skeletal muscle (1998) Am J Physiol, 275, pp. R905-R912Benforado, J.M., The veratrum alkaloids (1967) Physiological pharmacology, pp. 331-398. , Root WS, Hofmann, FG (eds). Academic Press, New YorkBrooke, M.H., Kaiser, K.K., Muscle fiber types: How many and what kind? 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Mouse Extensor Digitorum Longus And Soleus Show Distinctive Ultrastructural Changes Induced By Veratrine
We investigated whether veratrine (5 μl, 10 ng/kg) injected into the mouse extensor digitorum longus (EDL) (fast-twitch) and soleus (SOL) (slow-twitch) muscles provokes distinctive ultrastructural disturbances 15, 30 and 60 min later. The mitochondria in SOL were affected earlier (within 15 min) than in EDL. Swelling of the sarcoplasmic reticulum terminal cisternae was more marked in EDL than in SOL and caused distortion of sarcomeres so that fragmentation of myofilaments was more pronounced in EDL. Hypercontracted sarcomeres were seen mainly in SOL and veratrine caused infoldings of the sarcolemma only in this muscle. In both muscles, the T-tubules remained unaffected and by 60 min after veratrine most of the above alterations had reverted to normal. Pretreatment with tetrodotoxin prevented the alterations induced by veratrine. This suggests that most of the alterations resulted from the enhanced influx of Na+ into muscle fibers. 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Ther., 48, pp. 223-236Milton, R.L., Behforouz, M.A., Na+ channel density in extra junctional sarcolemma of fast and slow twitch mouse skeletal muscle fibers: Functional implications and plasticity after fast motoneuron transplantation to a slow muscle (1995) J. Muscle Res. Cell Motil., 16, pp. 430-439Nagaoka, R., Yamashita, S., Misuno, M., Akaike, N., Intracellular Na+ and K+ shifts induced by contractile activities of rat skeletal muscles (1994) Comp. Biochem. Physiol., 109 A, pp. 957-965Nemeth, P.M., Petter, D., Vrbová, G., Comparison of enzyme activities among single muscle fibres within defined motor units (1981) J. Physiol., 311, pp. 489-495Ogata, T., Morphological and cytochemical features of fiber types in vertebrate skeletal muscle (1988) CRC Crit. Rev. Anat. Cell Biol., 1, pp. 229-275Ownby, C.L., Cameron, D., Tu, A.T., Isolation of a myotoxic component from rattlesnake (Crotalus viridis viridis) venom (1976) Am. J. 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Electrophysiological And Ultrastructural Analysis Of The Neuromuscular Blockade And Miotoxicity Induced By The Micrurus Nigrocinctus Snake Venom.
Micrurus nigrocinctus is the most abundant coral snake in Central America. The venom of this specie induced a concentration-dependent (10-20 micrograms/ml) depolarization in the isolated mouse phrenic nerve-diaphragm preparations incubated at 37 degrees C. d-Tubocurarine (10 micrograms/ml) and (alpha beta ungarotoxin (3-5 micrograms/ml) were able to partially protect against the depolarization induced by the venom (10 micrograms/ml), suggesting the involvement of subsynaptic cholinergic receptors. This venom (10 micrograms/ml) also increased the frequency and amplitude of miniature end-plate potentials (mepps) during the first 10-20 min of incubation. Subsequently, the mepps progressively decreased and disappeared after 60 min. These responses were accompanied by ultrastructural changes involving the nerve terminals, the subsynaptic junctional folds and the muscle mitochondria. The synaptic gutter was shallow and, very often, "shrunken" terminals with omega-shaped axolemmal indentations and a decreased number of synaptic vesicles were present. A common finding was the presence of numerous finger-like, membrane-bounded bodies interposed between the terminal and the Schwann cells or postsynaptic sarcolemma. The preincubation of the venom with specific antivenom or the incubation of the preparations at room temperature (24-26 degrees C) reduced the number and intensity of the ultrastructural alterations. The last finding suggests the involvement of a enzymatic process, probably a phospholipase A2, present in the venom. There was a good correlation between the electrophysiological and ultrastructural effects induced by the venom which allow us to conclude that M. nigrocinctus venom has a presynaptic action in the initial stages of intoxication followed by sub- and postsynaptic effects, the last being the most important cause of neuromuscular blockade. A direct action of the venom on muscle fibers may also contributes to the irreversible blockade.49429029
Low-level Laser Therapy Promotes Vascular Endothelial Growth Factor Receptor-1 Expression In Endothelial And Nonendothelial Cells Of Mice Gastrocnemius Exposed To Snake Venom
Crotalinae snake venoms cause severe local myonecrosis and microvasculature failure at the bite site. We evaluated whether low-level laser therapy (LLLT) could accelerate angiogenesis and myoregeneration in male Swiss mice injected with Bothrops moojeni venom through immunohistochemistry of the vascular endothelial growth factor receptor-1 (VEGFR-1). Envenomed gastrocnemius was either unirradiated (V) or irradiated with HeNe (VHN, 632.8 nm) or GaAs (VGA, 904 nm, 10000 Hz). Animals sacrificed at 3 and 12 h were irradiated once (4 J cm-2), at 24 h (twice) and at 3, 7, 21 days (4, 8, 22 times, respectively). At 3 days, LLLT increased angiogenesis (80%:HeNe vs 40%:GaAs), decreased neutrophils and increased proliferation of regenerating cells. However, after 21 days, myoregeneration observed in the VHN group appeared delayed compared with the V group. As LLLT improved revascularization, the suggestive delay in myoregeneration could be a dose-response inhibitory effect caused by multiple irradiations in myogenesis. The immunodetection of VEGFR-1 in neutrophils, macrophages, satellite cells, fibroblasts, Schwann cells and skeletal and smooth muscle fibers (not seen in saline-controls) at only the acute stages of envenoming suggests a mediator role for VEGFR-1 in local alterations. This is the first time that VEGFR-1 expression, and its modulation by photostimulation, has been demonstrated in endothelial and nonendothelial cells of snake envenomed skeletal muscle. © 2010 The American Society of Photobiology.872418426Da Silva, C.J., Jorge, M.T., Ribeiro, L.A., Epidemiology of snakebite in a central region of Brazil (2003) Toxicon, 41 (2), pp. 251-255. , DOI 10.1016/S0041-0101(02)00287-8, PII S0041010102002878Bieber, A.L., Metal and non-protein constituents in snake venoms (1979) Handbook of Experimental Pharmacology, pp. 295-306. , In (Edited by C. Y. Lee), pp. Springer-Verlag, New YorkLeite, L.C.C., Furtado, M.F.D., Correa, T.C., Raw, I., Characterization of the snake venoms from seven Brazilian species of Bothrops by FPLC anion-exchange chromatography (1992) Comp. Biochem. Physiol., 102, pp. 515-520Ownby, C.L., Locally acting agents: Myotoxins, hemorrhagic toxins and dermonecrotic factors (1990) Handbook of Toxinology, pp. 602-654. , In (Edited by W. T. Shier and D. Mebs), pp. Marcel Dekker, New YorkGutiérrez, J.M., Lomonte, B., Local tissue damage induced by Bothops snake venoms. A review (1989) Mem. Inst. Butantan, 51, pp. 211-223Gutierrez, J.M., Ownby, C.L., Skeletal muscle degeneration induced by venom phospholipases A 2: Insights into the mechanisms of local and systemic myotoxicity (2003) Toxicon, 42 (8), pp. 915-931. , DOI 10.1016/j.toxicon.2003.11.005Harris, J.B., Myotoxic phospholipases A2 and the regeneration of skeletal muscles (2003) Toxicon, 42 (8), pp. 933-945. , DOI 10.1016/j.toxicon.2003.11.011Queiroz, L.S., Santo Neto, H., Rodrigues-Simioni, L., Prado-Franceschi, J., Muscle necrosis and regeneration after envenomation by Bothrops Jararacussu snake venom (1984) Toxicon, 22 (3), pp. 339-346Oshima-Franco, Y., Leite, G.B., Dal Belo, C.A., Hyslop, S., Prado-Franceschi, J., Cintra, A.C.O., Giglio, J.R., Rodrigues-Simioni, L., The presynaptic activity of bothropstoxin-I, a myotoxin from Bothrops jararacussu snake venom (2004) Basic and Clinical Pharmacology and Toxicology, 95 (4), pp. 175-182Bjarnason, J.B., Fox, J.W., Hemorrhagic metalloproteinases from snake venoms (1994) Pharmacology and Therapeutics, 62 (3), pp. 325-372. , DOI 10.1016/0163-7258(94)90049-3Moreira, L., Borkow, G., Ovadia, M., Gutierrez, J., Pathological changes induced by BaH1, a hemorrhagic proteinase isolated from Bothrops asper (terciopelo) snake venom, on mouse capillary blood vessels (1994) Toxicon, 32 (8), pp. 977-987. , DOI 10.1016/0041-0101(94)90376-XKamiguti, A.S., Zuzel, M., Theakston, R.D.G., Snake venom metalloproteinases and disintegrins: Interactions with cells (1998) Brazilian Journal of Medical and Biological Research, 31 (7), pp. 853-862Hati, R., Mitra, P., Sarker, S., Bhattacharyya, K.K., Snake venom hemorrhagins (1999) Critical Reviews in Toxicology, 29 (1), pp. 1-19Rucavado, A., Escalante, T., Teixeira, C.F.P., Fernandes, C.M., Diaz, C., Gutierrez, 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 of Inflammation, 11 (2), pp. 121-128. , DOI 10.1080/09629350220131980Escalante, T., Franceschi, A., Rucavado, A., Gutierrez, J.M., Effectiveness of batimastat, a synthetic inhibitor of matrix metalloproteinases, in neutralizing local tissue damage induced by BaP1, a hemorrhagic metalloproteinase from the venom of the snake Bothrops asper (2000) Biochemical Pharmacology, 60 (2), pp. 269-274. , DOI 10.1016/S0006-2952(00)00302-6, PII S0006295200003026Queiroz, S.L., Marques, M.J., Santo Neto, H., Acute local nerve lesions induced by Bothrops jararacussu snake venom (2002) Toxicon., 40, pp. 1483-1489Jorge, M.T., Ribeiro, L.A., O'Connell, J.L., Prognostic factors for amputation in the case of envenoming by snakes of the Bothrops genus (Viperidae) (1999) Annals of Tropical Medicine and Parasitology, 93 (4), pp. 401-408. , DOI 10.1080/00034989958393Schindl, A., Schindl, M., Schindl, L., Jurecka, W., Honigsmann, H., Breier, F., Increased dermal angiogenesis after low-intensity laser therapy for a chronic radiation ulcer determined by a video measuring system (1999) Journal of the American Academy of Dermatology, 40 (3), pp. 481-484Enwemeka, C.S., Ultrastructural morphometry of membrane-bound intracytoplasmic collagen fibrils in tendon fibroblasts exposed to He-Ne laser beam (1992) Tissue Cell, 42, pp. 511-523Reddy, G.K., Stehno-Bittel, L., Enwemeka, C.S., Laser photostimulation of collagen production in healing rabbit Achilles tendons (1998) Lasers in Surgery and Medicine, 22 (5), pp. 281-287. , DOI 10.1002/(SICI)1096-9101(1998)22:5<281::AID-LSM4>3.0.CO;2-LWeiss, N., Oron, U., Enhancement of muscle regeneration in the rat gastrocnemius muscle by low energy laser irradiation (1992) Anat. Embryol., 186, pp. 467-503Bibikova, A., Oron, U., Regeneration in denervated toad (Bufo viridis) gastrocnemius muscle and the promotion of the process by low energy laser irradiation (1995) Anat. Rec., 241, pp. 123-128Nakano, J., Kataoka, H., Sakamoto, J., Origuchi, T., Okita, M., Yoshimura, T., Low-level laser irradiation promotes the recovery of atrophied gastrocnemius skeletal muscle in rats (2009) Exp. Physiol., 94, pp. 1005-1015Rochkind, S., Nissan, M., Alon, M., Shamir, M., Salame, K., Effects of laser irradiation on the spinal cord for the regeneration of crushed peripheral nerve in rats (2001) Lasers in Surgery and Medicine, 28 (3), pp. 216-219. , DOI 10.1002/lsm.1041Gao, X., Xing, D., Molecular mechanisms of cell proliferation induced by low power laser irradiation (2009) J. Biomed. Sci., 16, p. 4. , DOI:Shefer, G., Partridge, T.A., Heslop, L., Gross, J.G., Oron, U., Halevy, O., Low-energy laser irradiation promotes the survival and cell cycle entry of skeletal muscle satellite cells (2002) Journal of Cell Science, 115 (7), pp. 1461-1469Shefer, G., Ben-Dov, N., Halevy, O., Oron, U., Primary myogenic cells see the light: Improved survival of transplanted myogenic cells following low energy laser irradiation (2008) Lasers in Surgery and Medicine, 40 (1), pp. 38-45. , DOI 10.1002/lsm.20588Dourado, D.M., Favero, S., Baranauskas, V., Da Cruz-Hofling, M.A., Effects of the Ga-As Laser Irradiation on Myonecrosis Caused by Bothrops Moojeni Snake Venom (2003) Lasers in Surgery and Medicine, 33 (5), pp. 352-357. , DOI 10.1002/lsm.10237Barbosa, A.M., Villaverde, A.B., Sousa, L.G., Munin, E., Fernandes, C.M., Cogo, J.C., Zamuner, S.R., Effect of low-level laser therapy in the myonecrosis induced by Bothrops jararacussu snake venom (2009) Photomed. 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Saunders Company, LondonDe Roodt, A.R., Litwin, S., Vidal, J.C., Hemorrhagic activity of Bothrops venoms determined by two different methods and relationship with proteolytic activity on gelatin and lethality (2003) Toxicon, 41 (8), pp. 949-958. , DOI 10.1016/S0041-0101(02)00392-6Calgarotto, A.K., Damico, D.C., Ponce-Soto, L.A., Baldasso, P.A., Da Silva, S.L., Souza, G.H., Eberlin, M.N., Marangoni, S., Biological and biochemical characterization of new basic phospholipase A(2) BmTX-I isolated from Bothrops moojeni snake venom (2008) Toxicon., 51, pp. 1509-1519Charge, S.B.P., Rudnicki, M.A., Cellular and Molecular Regulation of Muscle Regeneration (2004) Physiological Reviews, 84 (1), pp. 209-238. , DOI 10.1152/physrev.00019.2003Tidball, J.G., Inflammatory processes in muscle injury and repair (2005) American Journal of Physiology - Regulatory Integrative and Comparative Physiology, 288 (2), pp. R345-R353. , DOI 10.1152/ajpregu.00454.2004Cheng, M., Nguyen, M.H., Fantuzzi, G., Koh, T.J., Endogenous interferon gamma is required for efficient skeletal muscle regeneration (2008) Am. 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Venom Apparatus Of The Brazilian Tarantula Vitalius Dubius Mello-leitão 1923 (theraphosidae).
Tarantula venoms are a cocktail of proteins and peptides that have been increasingly studied in recent years. In contrast, less attention has been given to analyzing the structure of the paired cephalic glands that produce the venom. We have used light, electron, and confocal microscopy to study the organization and structure of the venom gland of the Brazilian tarantula Vitalius dubius. The chelicerae are hairy chitinous structures, each with a single curved hollow fang that opens via an orifice on the anterior surface. Internally, each chelicera contains striated muscle fiber bundles that control fang extension and retraction, and a cylindrical conical venom gland surrounded by a thick well-developed layer of obliquely arranged muscle fibers. Light microscopy of longitudinal and transverse sections showed that the gland secretory epithelium consists of a sponge-like network of slender epithelial cell processes with numerous bridges and interconnections that form lacunae containing secretion. This secretory epithelium is supported by a basement membrane containing elastic fibers. The entire epithelial structure of the venom-secreting cells is reinforced by a dense network of F-actin intermediate filaments, as shown by staining with phalloidin. Neural elements (axons and acetylcholinesterase activity) are also associated with the venom gland. Transmission electron microscopy of the epithelium revealed an ultrastructure typical of secretory cells, including abundant rough and smooth endoplasmic reticulum, an extensive Golgi apparatus, and numerous mitochondria.335361762
Sildenafil (viagra) Protective Effects On Neuroinflammation: The Role Of Inos/no System In An Inflammatory Demyelination Model
We recently demonstrated that sildenafil reduces the expression of cytokines, COX-2, and GFAP in a demyelinating model induced in wild-type (WT) mice. Herein, the understandings of the neuroprotective effect of sildenafil and the mediation of iNOS/NO system on inflammatory demyelination induced by cuprizone were investigated. The cerebella of iNOS-/- mice were examined after four weeks of treatment with cuprizone alone or combined with sildenafil. Cuprizone increased GFAP, Iba-1, TNF-α, COX-2, IL-1β, and IFN-γ expression, decreased expression of glutathione S-transferase pi (GSTpi), and damaged myelin in iNOS-/- mice. Sildenafil reduced Iba-1, IFN-γ, and IL-1β levels but had no effect on the expression of GFAP, TNF-α, and COX-2 compared to the cuprizone group. Sildenafil elevated GSTpi levels and improved the myelin structure/ultrastructure. iNOS-/- mice suffered from severe inflammation following treatment with cuprizone, while WT mice had milder inflammation, as found in the previous study. It is possible that inflammatory regulation through iNOS-feedback is absent in iNOS-/- mice, making them more susceptible to inflammation. Sildenafil has at least a partial anti-inflammatory effect through iNOS inhibition, as its effect on iNOS-/- mice was limited. 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Pharmacological Study Of Edema And Myonecrosis In Mice Induced By Venom Of The Bushmaster Snake (lachesis Muta Muta) And Its Basic Asp49 Phospholipase A2 (lmtx-i)
Previous in vitro studies show that Lachesis muta venom and its purified Asp49 phospholipase A2, named as LmTX-I, display potent neurotoxic and myotoxic activities. Here, an in vivo study was conducted to investigate some pharmacological effects of the venom or its LmTX-I toxin, after intra-muscular injection in tibialis anterior (TA) and following subplantar injection in hind paws of mice. Findings showed that LmTX-I increased plasma creatine kinase activity and produced strong myonecrosis and inflammatory reactions in TA muscle. In addition to these effects, the venom also induced intense local hemorrhage. Pre-treatment of the venom with EDTA (5 mM) significantly inhibited the edema and hemorrhage. Histological examination showed that L. muta venom caused inner dermal layer thickening in the pad hind paw. In addition, there was marked inflammatory cell infiltration, particularly of neutrophils, and hemorrhage. LmTX-I also demonstrated edema-forming activity, which was inhibited by pretreatment with indomethacin. © 2008 Springer Science+Business Media, LLC.276384391Barros, S.F., Friedlanskaia, I., Petricevich, B.L., Kipnis, T., (1998) Mediators Inflamm, 7, pp. 339-346Calhoun, W., Yu, J., Sung, A., Chau, T.T., Marshall, L.A., Weichman, B.M., Carlson, R.P., (1989) Agents Actions, 27, pp. 418-421Chaves, F., León, G., Alvarado, V.H., Gutiérrez, J.M., (1998) Toxicon, 36, pp. 1861-1869Chaves, F., Teixeira, C.F., Gutiérrez, J.M., (2005) Toxicon, 45, pp. 171-178Chioato, L., De Oliveira, A.H., Ruller, R., Sa, J.M., Ward, R.J., (2002) Biochem J, 366, pp. 971-976Campbell, J.A., Lamar, W.W., Greene, H., (2003) The Venomous Reptiles of the Western Hemisphere, , Cornell University New YorkCirino, G., Peers, S.H., Wallace, J.L., Flower, R.J., (1989) Eur J Pharmacol, 166, pp. 505-510Damico, D.C.S., Bueno, L.G.F., Rodrigues-Simioni, L., Marangoni, S., Cruz-Höfling, M.A., Novello, J.C., (2005) Toxicon, 46, pp. 222-229Damico, D.C.S., Lilla, S., De Nucci, G., Ponce-Soto, L.A., Winck, F.V., Novello, J.C., Marangoni, S., (2005) Biochim Biophys Acta, 1726, pp. 75-86Damico, D.C.S., Bueno, L.G.F., Rodrigues-Simioni, L., Marangoni, S., Cruz-Höfling, M.A., Novello, J.C., (2006) Toxicon, 47, pp. 759-765Dennis, E.A., (1994) J Biol Chem, 269, pp. 13057-13060Farsky, S.H.P., Walber, J., Costa-Cruz, M., Cury, Y., Teixeira, C.F.P., (1997) Toxicon, 35, pp. 185-193Francis, B., Gutiérrez, J.M., Lomonte, B., Kaiser, I.I., (1991) Biophysics, 284, pp. 1587-1594Fuly, A.L., De Miranda, A.L.P., Zingali, R.B., Guimarães, J.A., (2002) Biochem Pharmacol, 63, pp. 1589-1597Gutiérrez, J.M., Lomonte, B., (1995) Toxicon, 33, pp. 1405-1424Gutiérrez, J.M., Ownby, C.L., (2003) Toxicon, 42, pp. 915-931Gutiérrez, J.M., Rojas, G., Lomonte, B., Gené, J.A., Cerdas, L., (1986) Comp Biochem Physiol, 85, pp. 171-175Gutiérrez, J.M., Rucavado, A., (2000) Biochimie, 82, pp. 841-845Harris, J.B., Cullen, M.J., (1990) Electron Microsc Rev, 3, pp. 183-211Kaiser, I.I., Gutiérrez, J.M., Plummer, D., Aird, S.D., Odell, G.V., (1990) Arch Biochem Biophys, 278, pp. 319-325Kini, R.M., (2003) Toxicon, 42, pp. 827-840Lomonte, B., Moreno, E., Tarkowski, A., Hanson, L.A., MacCarana, M., (1994) J Biol Chem, 269, pp. 29867-29873Maraganore, J.M., Heinrikson, R.L., (1986) J Biol Chem, 261, pp. 4797-4804Murakami, M., Kambe, T., Shimbara, S., Yamamoto, S., Kuwata, H., Kudo, I., (1999) J Biol Chem, 274, pp. 29927-29936Neto, H.S., Marques, M.J., (2005) Toxicon, 46, pp. 814-819Nuñez, C.E., Angulo, Y., Lomote, B., (2001) Toxicon, 39, pp. 1587-1594Queiroz, L.S., Marques, M.J., Neto, H.S., (2002) Toxicon, 40, pp. 1483-1486Ran, Y., Zheng, S., Tu, A.T., (1988) Chem Res Toxicol, 1, pp. 337-342Rojas, G., Gutiérrez, J.M., Gené, J.A., Gómez, M., Cerdas, L., (1987) Rev Biol Trop, 35, pp. 59-67Rosenthal, R., Meier, J., Koelz, A., Muller, C., Wegmann, W., Vogelbach, P., (2002) Toxicon, 40, pp. 217-220Sánchez, E.F., Magalhães, A., Diniz, C.R., (1987) Toxicon, 25, pp. 611-619Sánchez, E.F., Magalhães, A., Mandelbaum, F.R., Diniz, C.R., (1991) Biochim Biophys Acta, 1074, pp. 347-356Sánchez, E.F., Costa, M.I.E., Chavez-Olórtegui, C., Assakura, M.T., Mandelbaum, F.R., Diniz, C.R., (1995) Toxicon, 33, pp. 1653-1667Sánchez, E.F., Cordeiro, M.N., De Oliveira, E.B., Juliano, L., Prado, E.S., Diniz, C.R., (1995) Toxicon, 33, pp. 1061-1069Araújo De Selistre, H.S., White, S.P., Ownby, C.L., (1996) Arch Biochem Biophys, 326, pp. 21-30Teixeira, C.F.P., Landucci, E.C.T., Antunes, E., Chacur, M., Cury, Y., (2003) Toxicon, 42, pp. 947-962Vishwanath, B.S., Kini, R.M., Gowda, T.V., (1987) Toxicon, 25, pp. 501-515Vishwanath, B.S., Fawzy, A.A., Franson, R.C., (1988) Inflammation, 12, pp. 549-561Wang, J.P., Teng, C.M., (1990) Eur J Pharmacol, 190, pp. 347-35
Osteopontin, A Chemotactic Protein With Cytokine-like Properties, Is Up-regulated In Muscle Injury Caused By Bothrops Lanceolatus (fer-de-lance) Snake Venom
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.585398409BogarÃn, 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. 551-557Chargé, S.B., Rudnicki, M.A., Cellular and molecular regulation of muscle regeneration (2004) Physiol. 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