Search for peptidic molecular markers in hemolymph of crowd-(gregarious) and isolated-reared (solitary) desert locusts, Schistocerca gregaria
Autor: | Mazibur M. Rahman, Liliane Schoofs, A. De Loof, Michael Breuer, B Hoste, Elke Clynen, L. Van Den Bosch, Karen Meylaers, Geert Baggerman, Tom Vercammen, Korneel Hens |
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Jazyk: | angličtina |
Rok vydání: | 2016 |
Předmět: |
animal structures
Physiology Molecular Sequence Data Peptide Grasshoppers Biochemistry Mass Spectrometry Cellular and Molecular Neuroscience Endocrinology Hemolymph Bioassay Animals Amino Acid Sequence Nymph Chromatography High Pressure Liquid chemistry.chemical_classification Serine protease Chromatography biology Molecular mass Edman degradation biology.organism_classification chemistry biology.protein Schistocerca Peptides Biomarkers |
Popis: | An HPLC analysis of hemolymph extracts was undertaken to uncover differences between desert locusts, Schistocerca gregaria , reared under either crowded or isolated conditions. Some differences in the chromatographic pattern could be detected. One of the major peaks in the hemolymph of crowd-reared adults was found to be a minor one in isolated-reared individuals, whereas other peaks increased after solitarization. The differences became even more pronounced after several generations of isolated rearing. The dominant chromatographic peak in hemolymph extracts of the crowd-reared animals was identified as a novel peptide with a molecular mass of 6080 Da. Edman degradation in combination with enzymatic fragmentation and quadrupole-time of flight (Q-Tof) mass spectrometry revealed the full sequence: DNADEDTICVAADNKFYLYANSLKLYTCYNQLPKVYVVKPKSQCRSSLSDCPTS. This 54 aa-peptide is very abundant in hemolymph of crowd-reared adults. Its concentration in hemolymph amounts to 0.1 mM. To uncover the function, its effects were investigated in several bioassays, so far without positive results. One of the other peaks differentially expressed in the individuals of the two phases was identified as SGPI-2 (MW=3794 Da), which is a serine protease inhibitor in locusts. |
Databáze: | OpenAIRE |
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