In dry savannahs of West-Africa, the malarial mosquitoes of the Anopheles gambiae sensu stricto complex annually survive the harsh desiccating conditions of the dry season. However, the physiological and biochemical mechanisms underlying how these mosquitoes survive such desiccating conditions are still undefined, and controversial. In this context, we provide the first work examining both proteomic and metabolomic changes in the two molecular forms of A. gambiae s.s (M and S forms) experimentally exposed to the rainy and dry season conditions as they experience in the field. Protein abundances of the mosquitoes were measured using a two-dimensional fluorescence difference gel electrophoresis (2D DIGE) coupled with a matrix-assisted laser desorption/ionisation-time of flight (MALDI-TOF) and tandem mass spectrometry (MS) for protein identification. These assays were conducted by Applied Biomics (http://www.appliedbiomics.com, Applied Biomics, Inc. Hayward, CA, USA), and the mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE partner repository with the dataset identifier PXD000294. The metabolomic analysis was conducted using both Acquity UPLC(®) system (for amino acid identification), and a gas-chromatography-mass spectrometry platform (for sugars identification). Metabolomic fingerprintings were assessed in the University of Rennes 1, UMR CNRS 6553 EcoBio (France). A detailed interpretation of the obtained data can be found in Hidalgo et al. (2014) [1] (Journal of Insect Physiology (2014)).
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http://dx.doi.org/10.1016/j.dib.2015.08.031 | DOI Listing |
Cell Surf
June 2025
Department of Biological Sciences, SUNY University at Buffalo, Buffalo, NY 14260, United States.
In vegetative hyphae, chitin, β-1,3-glucan (laminarin), and a mixed β-1,3-/β-1,4-glucan (lichenin) are the major cell wall polysaccharides. GH72 enzymes have been shown to function as β-1,3-glucanases and glucanosyltransferases and can function in crosslinking β-1,3-glucans together. To characterize the enzymatic activities of the enzymes, we expressed GEL-1 with a HIS6 tag in A chimeric maltose binding protein:GEL-2 was produced in .
View Article and Find Full Text PDFInt J Reprod Biomed
November 2024
Department of Genetics, Reproductive Biomedicine Research Center, Royan Institute for Reproductive Biomedicine, ACECR, Tehran, Iran.
Background: Embryo selection for transfer is critical in assisted reproduction. The presence of DNA in the blastocoel cavity of human blastocysts is assumed to be a consequence of common preimplantation chromosomal abnormalities.
Objective: This study examined the relationship between the amount of blastocoel fluid (BF) DNA and the band intensity of amplified BF-DNA in gel electrophoresis, considering the influence of ploidy status.
Pharmaceutics
December 2024
Department of Applied Chemistry, Tokyo Metropolitan University, Tokyo 192-0397, Japan.
: This study aimed to design and evaluate Chol-PEG micelles and Chol-PEG vesicles as drug delivery system (DDS) carriers and inhibitors of amyloid-β (Aβ) aggregation, a key factor in Alzheimer's disease (AD). : The physical properties of Chol-PEG assemblies were characterized using dynamic light scattering (DLS), electrophoretic light scattering (ELS), and transmission electron microscopy (TEM). Inhibitory effects on Aβ aggregation were assessed via thioflavin T (ThT) assay, circular dichroism (CD) spectroscopy, and native polyacrylamide gel electrophoresis (native-PAGE).
View Article and Find Full Text PDFMedicina (Kaunas)
January 2025
Service de Cardiologie Pédiatrique, Hôpital la Rabta Tunis, Tunis 1007, Tunisia.
The pathophysiology of arrhythmogenic cardiomyopathy (ACM), previously known as arrhythmogenic right ventricular cardiomyopathy (ARVC), and its specific biological features remain poorly understood. High-throughput plasma proteomic profiling, a powerful tool for gaining insights into disease pathophysiology at the systems biology level, has not been used to study ACM. This study aimed at characterizing plasmatic protein changes in patients with ACM, which were compared with those of healthy controls, and at exploring the potential role of the identified proteins as biomarkers for diagnosis and monitoring.
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