ABSTRACT
Arthropod venoms are potential sources of bioactive substances, providing tools for the validation of popular use and new drugs design. Ants belonging to the genus Dinoponera are used in the folk medicine to treat inflammatory conditions. It was previously demonstrated that the venom of the giant ant Dinoponera quadriceps (DqV), containing a mixture of polypeptides, elicit antinociceptive effect in mice models of chemical, mechanical and thermal nociception. The aim of this study was to evaluate DqV antiinflammatory and antihypernociceptive effects in a mice model of traumatic cutaneous wound. Colonies of D. quadriceps were collected in the Serra de Maranguape (State of Ceará, northeastern Brazil), a small mountain range located on the coastal zone, and the venom secreted by the ant glands was extracted with capillary tubes, further lyophilized and maintained at -20 ± 1ºC until use. Wounds were performed in the dorsum of Swiss mice. Animals received intravenous (i.v.) injection of DqV (50 µg -1kg day-1) during 3 days for evaluation of inflammatory parameters present in the wounds: hypernociception, leukocyte infiltrate, myeloperoxidase activity, nitrite nitrate-1 content. Data was tested by two-way ANOVA and Bonferronis post-hoc test. DqV reduced (2.7 folds) hypernociception at 48 hours, leukocyte infiltration by 65% at 6 hours and myeloperoxidase activity by 60% at 0.5 hour after wound induction. In conclusion, the venom extracted from D. quadriceps glands attenuates inflammation and hypernociception in mice cutaneous wounds.
Subject(s)
Animals , Mice , Mice/injuries , Wound Healing , Hymenoptera , Arthropod Venoms/analysis , Anti-Inflammatory AgentsABSTRACT
Hyaluronidases are enzymes that mainly degrade hyaluronan, the major glycosaminoglycan of the interstitial matrix. They are involved in several pathological and physiological activities including fertilization, wound healing, embryogenesis, angiogenesis, diffusion of toxins and drugs, metastasis, pneumonia, sepsis, bacteremia, meningitis, inflammation and allergy, among others. Hyaluronidases are widely distributed in nature and the enzymes from mammalian spermatozoa, lysosomes and animal venoms belong to the subclass EC 3.2.1.35. To date, only five three-dimensional structures for arthropod venom hyaluronidases (Apis mellifera and Vespula vulgaris) were determined. Additionally, there are four molecular models for hyaluronidases fromMesobuthus martensii, Polybia paulista and Tityus serrulatus venoms. These enzymes are employed as adjuvants to increase the absorption and dispersion of other drugs and have been used in various off-label clinical conditions to reduce tissue edema. Moreover, a PEGylated form of a recombinant human hyaluronidase is currently under clinical trials for the treatment of metastatic pancreatic cancer. This review focuses on the arthropod venom hyaluronidases and provides an overview of their biochemical properties, role in the envenoming, structure/activity relationship, and potential medical and biotechnological applications.
Subject(s)
Animals , Animals, Poisonous , Hyaluronoglucosaminidase , Arthropod Venoms/analysis , Arthropod Venoms/therapeutic useABSTRACT
A comparison of some components of the venoms of two Costa Rican tarantulas, Aphonopelma seeamanni (Cambridge) and Sphaerobothria hoffmanni (Karsch) by polyacrylamide gel electrophoresis shows patterns similar to those of Dugesiella hentzi (Girard), a North American tarantula. The digestive secretions have proteins that do not enter the 15% gels; thus no bands are obsorved. The method used by the tarantulas to consume their prey involves the action of both the venom and the digestive secretions. The percent protein, pH, proteolytic activity and hemolytic activity of venom and digestive secretions of both species were determined, and a high proteolytic activity for digestive secretions was found.
Subject(s)
Female , Animals , Arthropod Venoms/analysis , Intestinal Secretions/analysis , Spider Venoms/analysis , Electrophoresis, Polyacrylamide Gel , Intestinal Secretions/physiology , Spider Venoms/physiologyABSTRACT
El veneno de arañas adultas Loxósceles laeta fue obtenido mediante electroestimulación y disección glandular. La distribución electroforética de las proteínas del veneno fue obtenida en gel de poliacrilamida a pH 8.6, obteniéndose 19 y 22 bandas proteicas respectivamente. Mediante electroforesis a pH 7.2 en presencia de dodecil sulfato de sodio de sodio se observaron tan solo 18 y 20 respectivamente. Las muestras estudiadas no producen coagulación del fibrinógeno humano, bovino ni plasma humano citratado. El veneno loxoscélico no hidrolizá los substratos BAPna, TAME ni Chromozym TH lo que demuestra la ausencia de Enzima similar a trombina. La presencia de acción procoagulante in vitro del veneno fue demostrada por la aceleración del tiempo de recalcificación del plasma humano. Se discute el rol de esta actividad en el envenenamiento loxoscélico