Zhao L.,University of Texas at El Paso |
Peng B.,Border Biomedical Research Center |
Hernandez-Viezcas J.A.,University of Texas at El Paso |
Rico C.,University of Texas at El Paso |
And 8 more authors.
ACS Nano | Year: 2012
The rapid development of nanotechnology will inevitably release nanoparticles (NPs) into the environment with unidentified consequences. In addition, the potential toxicity of CeO2 NPs to plants and the possible transfer into the food chain are still unknown. Corn plants (Zea mays) were germinated and grown in soil treated with CeO2 NPs at 400 or 800 mg/kg. Stress-related parameters, such as H2O2, catalase (CAT), and ascorbate peroxidase (APX) activity, heat shock protein 70 (HSP70), lipid peroxidation, cell death, and leaf gas exchange were analyzed at 10, 15, and 20 days post-germination. Confocal laser scanning microscopy was used to image H2O2 distribution in corn leaves. Results showed that the CeO2 NP treatments increased accumulation of H 2O2, up to day 15, in phloem, xylem, bundle sheath cells and epidermal cells of shoots. The CAT and APX activities were also increased in the corn shoot, concomitant with the H2O2 levels. Both 400 and 800 mg/kg CeO2 NPs triggered the up-regulation of the HSP70 in roots, indicating a systemic stress response. None of the CeO2 NPs increased the level of thiobarbituric acid reacting substances, indicating that no lipid peroxidation occurred. CeO2 NPs, at both concentrations, did not induce ion leakage in either roots or shoots, suggesting that membrane integrity was not compromised. Leaf net photosynthetic rate, transpiration, and stomatal conductance were not affected by CeO2 NPs. Our results suggest that the CAT, APX, and HSP70 might help the plants defend against CeO2 NP-induced oxidative injury and survive NP exposure. © 2012 American Chemical Society.
Cruz C.E.,University of Sao Paulo |
Fogaca A.C.,University of Sao Paulo |
Nakayasu E.S.,Border Biomedical Research Center |
Angeli C.B.,University of Sao Paulo |
And 10 more authors.
Parasites and Vectors | Year: 2010
Background: Hemoglobin is a rich source of biologically active peptides, some of which are potent antimicrobials (hemocidins). A few hemocidins have been purified from the midgut contents of ticks. Nonetheless, how antimicrobials are generated in the tick midgut and their role in immunity is still poorly understood. Here we report, for the first time, the contribution of two midgut proteinases to the generation of hemocidins. Results: An aspartic proteinase, designated BmAP, was isolated from the midgut of Rhipicephalus (Boophilus) microplus using three chromatographic steps. Reverse transcription-quantitative polymerase chain reaction revealed that BmAP is restricted to the midgut. The other enzyme is a previously characterized midgut cathepsin L-like cysteine proteinase designated BmCL1. Substrate specificities of native BmAP and recombinant BmCL1 were mapped using a synthetic combinatorial peptide library and bovine hemoglobin. BmCL1 preferred substrates containing non-polar residues at P2 subsite and polar residues at P1, whereas BmAP hydrolysed substrates containing non-polar amino acids at P1 and P1'. Conclusions: BmAP and BmCL1 generate hemocidins from hemoglobin alpha and beta chains in vitro. We postulate that hemocidins may be important for the control of tick pathogens and midgut flora. © 2010 Cruz et al; licensee BioMed Central Ltd.
Cox M.B.,University of Texas at El Paso |
Cox M.B.,Border Biomedical Research Center |
Johnson J.L.,University of Idaho
Methods in Molecular Biology | Year: 2011
Molecular chaperones are a diverse group of highly conserved proteins that transiently interact with partially folded polypeptide chains during normal cellular processes, such as protein translation, translocation, and disassembly of protein complexes (1). Prior to folding or after denaturation, hydrophobic residues that are normally sequestered within a folded protein are exposed to the aqueous environment and are prone to aggregation or misfolding. Multiple classes of molecular chaperones, such as Hsp70s and Hsp40s, recognize and transiently bind polypeptides with exposed hydrophobic stretches in order to prevent misfolding. Other types of chaperones, such as Hsp90, have more specialized functions in that they appear to interact with only a subset of cellular proteins. This chapter focuses on the role of Hsp90 and partner co-chaperones in promoting the folding and activation of a diverse group of proteins with critical roles in cellular signaling and function. © 2011 Springer Science+Business Media, LLC.