New drugs are being developed each year for cancer, heart attacks, and strokes and some have been derived from snake venoms. Snake venoms are complex mixtures of molecules that can have therapeutic value in the treatment of clot-induced ischemia, cancer, and other human disorders. Snake venoms are rich, stable sources of disintegrins, metalloproteases, and fibrinolytic enzymes. The literature contains many references on how venom and/or venom components are being used in medicine. There are 44 subspecies of poisonous snakes within the U.S.. Despite the vast species diversity, 90% of the papers published have been with venom from a limited number of the more common species (Crotalus (C.) atrox, C. adamanteus, C. viridis viridis, Agkistrodon (A.) contortrix contortrix, A. contortrix laticinctus, and A. piscivorus piscivorus). Many of the snake venoms are not available for research. Therefore, venom composition and potential usefulness in medicine has not been explored. There is a need to develop a Center capable of providing quality venoms, venom fractions, tissues, organs, skins, and monoclonal and polyclonal antibodies for biomedical research. For over 28 years, TAMUK has maintained a strong venom research program and has developed a serpentarium that presently houses over 350 snakes composed of 14 species and 24 subspecies. Two years ago, the Texas A&M University System Board of Regents approved the development of a Natural Toxins Research Center (NTRC) at TAMUK. The mission of the NTRC is to provide global research, training, and resources that will lead to the discovery of medically important toxins found in venoms. The objectives of this proposal are to: 1) provide reliable sources of venoms and other snake products that are not available from other vendors; 2) breed poisonous snakes in captivity that are endangered or difficult to acquire; 3) characterize medically important venoms by electrophoretic titration (ET), high performance liquid chromatography (HPLC), enzyme activities, and cell-based assays; 4) develop a research program that provides insights into structure/function relationships of venom proteins, and 5) develop a database that will be useful to other investigators. The database will allow the user to view the snakes, their geographical distribution and venom characteristics.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Animal (Mammalian and Nonmammalian) Model, and Animal and Biological Material Resource Grants (P40)
Project #
5P40RR018300-04
Application #
7051428
Study Section
National Center for Research Resources Initial Review Group (RIRG)
Program Officer
Chang, Michael
Project Start
2003-04-15
Project End
2008-03-31
Budget Start
2006-04-01
Budget End
2007-03-31
Support Year
4
Fiscal Year
2006
Total Cost
$464,020
Indirect Cost
Name
Texas A&M University-Kingsville
Department
Biology
Type
Schools of Arts and Sciences
DUNS #
868154089
City
Kingsville
State
TX
Country
United States
Zip Code
78363
Gutierrez, Daniel A; Aranda, Ana S; Carrillo, David A R et al. (2016) Functional analysis of four single (RGDWL, RGDWM, RGDWP, RGDMN) and two double (RGDNM, RGDMP) mutants: The importance of methionine (M) in the functional potency of recombinant mojastin (r-Moj). Toxicon 124:1-7
Ramos, Carla J; Gutierrez, Daniel A; Aranda, Ana S et al. (2016) 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. Toxicon 118:36-42
Giron, Maria E; Rodriguez-Acosta, Alexis; Salazar, Ana Maria et al. (2013) Isolation and characterization of two new non-hemorrhagic metalloproteinases with fibrinogenolytic activity from the mapanare (Bothrops colombiensis) venom. Arch Toxicol 87:197-208
Carey, Clayton M; Bueno, Raymund; Gutierrez, Daniel A et al. (2012) Recombinant rubistatin (r-Rub), an MVD disintegrin, inhibits cell migration and proliferation, and is a strong apoptotic inducer of the human melanoma cell line SK-Mel-28. Toxicon 59:241-8
Calvete, Juan J; Pérez, Alicia; Lomonte, Bruno et al. (2012) Snake venomics of Crotalus tigris: the minimalist toxin arsenal of the deadliest Nearctic rattlesnake venom. Evolutionary Clues for generating a pan-specific antivenom against crotalid type II venoms [corrected]. J Proteome Res 11:1382-90
Lucena, Sara E; Jia, Ying; Soto, Julio G et al. (2012) Anti-invasive and anti-adhesive activities of a recombinant disintegrin, r-viridistatin 2, derived from the Prairie rattlesnake (Crotalus viridis viridis). Toxicon 60:31-9
Yin, Chunhui; Jia, Ying; Garcia, Carlos A (2012) A novel method for the purification of low soluble recombinant C-type lectin proteins. Biochem Biophys Res Commun 425:636-41
Massey, Daniel J; Calvete, Juan J; Sánchez, Elda E et al. (2012) Venom variability and envenoming severity outcomes of the Crotalus scutulatus scutulatus (Mojave rattlesnake) from Southern Arizona. J Proteomics 75:2576-87
Suntravat, Montamas; Yusuksawad, Mariem; Sereemaspun, Amornpun et al. (2011) Effect of purified Russell's viper venom-factor X activator (RVV-X) on renal hemodynamics, renal functions, and coagulopathy in rats. Toxicon 58:230-8
Giron, Maria E; Estrella, Amalid; Sanchez, Elda E et al. (2011) Purification and characterization of a metalloproteinase, Porthidin-1, from the venom of Lansberg's hog-nosed pitvipers (Porthidium lansbergii hutmanni). Toxicon 57:608-18

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