Search

Your search keyword '"Sánchez, Elda E."' showing total 372 results
Start Over Author "Sánchez, Elda E."
372 results on '"Sánchez, Elda E."'

6. Lys49 myotoxin from the Brazilian lancehead pit viper elicits pain through regulated ATP release

Author

Zhang, Chuchu, Medzihradszky, Katalin F, Sánchez, Elda E, Basbaum, Allan I, and Julius, David

Subjects
Biomedical and Clinical Sciences, Neurosciences, Clinical Sciences, Pain Research, Chronic Pain, Adenosine Triphosphate, Animals, Bothrops, Brazil, Female, Group II Phospholipases A2, Humans, Male, Mice, Mice, Inbred C57BL, Pain, Rats, Receptors, Purinergic, Reptilian Proteins, Sensory Receptor Cells, Signal Transduction, Snake Bites, Toxins, Biological, Viper Venoms, Lys49 myotoxin, ATP release, pannexin, pain, purinergic receptor
Abstract

Pain-producing animal venoms contain evolutionarily honed toxins that can be exploited to study and manipulate somatosensory and nociceptive signaling pathways. From a functional screen, we have identified a secreted phospholipase A2 (sPLA2)-like protein, BomoTx, from the Brazilian lancehead pit viper (Bothrops moojeni). BomoTx is closely related to a group of Lys49 myotoxins that have been shown to promote ATP release from myotubes through an unknown mechanism. Here we show that BomoTx excites a cohort of sensory neurons via ATP release and consequent activation of P2X2 and/or P2X3 purinergic receptors. We provide pharmacological and electrophysiological evidence to support pannexin hemichannels as downstream mediators of toxin-evoked ATP release. At the behavioral level, BomoTx elicits nonneurogenic inflammatory pain, thermal hyperalgesia, and mechanical allodynia, of which the latter is completely dependent on purinergic signaling. Thus, we reveal a role of regulated endogenous nucleotide release in nociception and provide a detailed mechanism of a pain-inducing Lys49 myotoxin from Bothrops species, which are responsible for the majority of snake-related deaths and injuries in Latin America.

Published
2017

16. Rattling the border wall: Pathophysiological implications of functional and proteomic venom variation between Mexican and US subspecies of the desert rattlesnake Crotalus scutulatus

Author

Dobson, James, Yang, Daryl C., op den Brouw, Bianca, Cochran, Chip, Huynh, Tam, Kurrupu, Sanjaya, Sánchez, Elda E., Massey, Daniel J., Baumann, Kate, Jackson, Timothy N.W., Nouwens, Amanda, Josh, Peter, Neri-Castro, Edgar, Alagón, Alejandro, Hodgson, Wayne C., and Fry, Bryan G.

Published
2018
Full Text
View/download PDF

18. A heteromeric Texas coral snake toxin targets acid-sensing ion channels to produce pain.

Author

Bohlen, Christopher J, Chesler, Alexander T, Sharif-Naeini, Reza, Medzihradszky, Katalin F, Zhou, Sharleen, King, David, Sánchez, Elda E, Burlingame, Alma L, Basbaum, Allan I, and Julius, David

Subjects
Oocytes, Cells, Cultured, Hindlimb, Animals, Mice, Knockout, Xenopus laevis, Humans, Mice, Rats, Elapidae, Pain, Protons, Capsaicin, Sodium Channels, Nerve Tissue Proteins, Elapid Venoms, Ion Channel Gating, Amino Acid Sequence, Protein Structure, Quaternary, Hydrogen-Ion Concentration, Molecular Sequence Data, Male, TRPV Cation Channels, Sensory Receptor Cells, Protein Multimerization, Nociception, Acid Sensing Ion Channels, Sodium Channel Agonists, Pain Research, Chronic Pain, Neurosciences, 5.1 Pharmaceuticals, General Science & Technology
Abstract

Natural products that elicit discomfort or pain represent invaluable tools for probing molecular mechanisms underlying pain sensation. Plant-derived irritants have predominated in this regard, but animal venoms have also evolved to avert predators by targeting neurons and receptors whose activation produces noxious sensations. As such, venoms provide a rich and varied source of small molecule and protein pharmacophores that can be exploited to characterize and manipulate key components of the pain-signalling pathway. With this in mind, here we perform an unbiased in vitro screen to identify snake venoms capable of activating somatosensory neurons. Venom from the Texas coral snake (Micrurus tener tener), whose bite produces intense and unremitting pain, excites a large cohort of sensory neurons. The purified active species (MitTx) consists of a heteromeric complex between Kunitz- and phospholipase-A2-like proteins that together function as a potent, persistent and selective agonist for acid-sensing ion channels (ASICs), showing equal or greater efficacy compared with acidic pH. MitTx is highly selective for the ASIC1 subtype at neutral pH; under more acidic conditions (pH < 6.5), MitTx massively potentiates (>100-fold) proton-evoked activation of ASIC2a channels. These observations raise the possibility that ASIC channels function as coincidence detectors for extracellular protons and other, as yet unidentified, endogenous factors. Purified MitTx elicits robust pain-related behaviour in mice by activation of ASIC1 channels on capsaicin-sensitive nerve fibres. These findings reveal a mechanism whereby snake venoms produce pain, and highlight an unexpected contribution of ASIC1 channels to nociception.

Published
2011

19. Molecular basis of infrared detection by snakes

Author

Gracheva, Elena O, Ingolia, Nicholas T, Kelly, Yvonne M, Cordero-Morales, Julio F, Hollopeter, Gunther, Chesler, Alexander T, Sánchez, Elda E, Perez, John C, Weissman, Jonathan S, and Julius, David

Subjects
Biomedical and Clinical Sciences, Neurosciences, Animals, Boidae, Chickens, Cloning, Molecular, Crotalus, Hot Temperature, Infrared Rays, Light Signal Transduction, Molecular Sequence Data, Predatory Behavior, Rats, Sensory Receptor Cells, Transient Receptor Potential Channels, Trigeminal Ganglion, General Science & Technology
Abstract

Snakes possess a unique sensory system for detecting infrared radiation, enabling them to generate a 'thermal image' of predators or prey. Infrared signals are initially received by the pit organ, a highly specialized facial structure that is innervated by nerve fibres of the somatosensory system. How this organ detects and transduces infrared signals into nerve impulses is not known. Here we use an unbiased transcriptional profiling approach to identify TRPA1 channels as infrared receptors on sensory nerve fibres that innervate the pit organ. TRPA1 orthologues from pit-bearing snakes (vipers, pythons and boas) are the most heat-sensitive vertebrate ion channels thus far identified, consistent with their role as primary transducers of infrared stimuli. Thus, snakes detect infrared signals through a mechanism involving radiant heating of the pit organ, rather than photochemical transduction. These findings illustrate the broad evolutionary tuning of transient receptor potential (TRP) channels as thermosensors in the vertebrate nervous system.

Published
2010

25. Functional characterization of six aspartate (D) recombinant mojastin mutants (r-Moj): A second aspartate amino acid carboxyl to the RGD in r-Moj-D_ peptides is not sufficient to induce apoptosis of SK-Mel-28 cells.

Author

Ramos, Carla J., Gutierrez, Daniel A., Aranda, Ana S., Koshlaychuk, Melissa A., Carrillo, David A., Medrano, Rafael, McBride, Terri D., U, Andrew, Medina, Stephanie M., Lombardo, Melissa C., Lucena, Sara E., Sanchez, Elda E., and Soto, Julio G.

Published
2016
Full Text
View/download PDF

28. Antivenoms and Coagulation

Author

Sánchez, Elda E., Rodríguez-Acosta, Alexis, Cantu, Esteban, Guerrero, Belsy, Kini, R. Manjunatha, editor, Clemetson, Kenneth J, editor, Markland, Francis S., editor, McLane, Mary Ann, editor, and Morita, Takashi, editor

Published
2010
Full Text
View/download PDF

47. The mojastin mutant Moj-DM induces apoptosis of the human melanoma SK-Mel-28, but not the mutant Moj-NN nor the non-mutated recombinant Moj-WN

Author

Seoane, Agustin I., Tran, Victoria L., Sanchez, Elda E., White, Stephanie A., Choi, Jason L., Gaytán, Brandon, Chavez, Natalie, Reyes, Steven R., Ramos, Carla J., Tran, Luan H., Lucena, Sara E., Sugarek, Maria, Perez, John C., Mandal, Stephanie A., Ghorab, Shervin, Rodriguez-Acosta, Alexis, Fung, Branden K., and Soto, Julio G.

Published
2010
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results