scholarly journals Histopathological Evaluation of the Exposure by Cyanobacteria Cultive Containing [d-Leu1]Microcystin-LR on Lithobates catesbeianus Tadpoles

Toxins ◽  
2018 ◽  
Vol 10 (8) ◽  
pp. 318 ◽  
Author(s):  
Osmindo Rodrigues Pires Júnior ◽  
Natiela de Oliveira ◽  
Renan Bosque ◽  
Maria Nice Ferreira ◽  
Veronica Morais Aurélio da Silva ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Microcystis Aeruginosa ◽  
Intestinal Tract ◽  
Mass Spectrometry Analysis ◽  
Clean Water ◽  
Tissue Samples ◽  
Spectrometry Analysis ◽  
Lithobates Catesbeianus ◽  
Histopathological Evaluation ◽  
Unialgal Culture

This study evaluated the effects of [d-Leu1]Microcystin-LR variant by the exposure of Lithobates catesbeianus tadpole to unialgal culture Microcystis aeruginosa NPLJ-4 strain. The Tadpole was placed in aquariums and exposed to Microcystis aeruginosa culture or disrupted cells. For 16 days, 5 individuals were removed every 2 days, and tissue samples of liver, skeletal muscle, and intestinal tract were collected for histopathology and bioaccumulation analyses. After exposure, those surviving tadpoles were placed in clean water for 15 days to evaluate their recovery. A control without algae and toxins was maintained in the same conditions and exhibited normal histology and no tissue damage. In exposed tadpoles, samples were characterized by serious damages that similarly affected the different organs, such as loss of adhesion between cells, nucleus fragmentation, necrosis, and hemorrhage. Samples showed signs of recovery but severe damages were still observed. Neither HPLC-PDA nor mass spectrometry analysis showed any evidence of free Microcystins bioaccumulation.

scholarly journals Effect of Ocular Hypertension on D-β-Aspartic Acid-Containing Proteins in the Retinas of Rats

2019 ◽  
Vol 2019 ◽  
pp. 1-8 ◽  
Author(s):  
Takashi Kanamoto ◽  
Takashi Tachibana ◽  
Yasushi Kitaoka ◽  
Toshio Hisatomi ◽  
Yasuhiro Ikeda ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Ocular Hypertension ◽  
Aspartic Acid ◽  
Atp Synthase ◽  
Wistar Rats ◽  
Protein Band ◽  
Mass Spectrometry Analysis ◽  
Liquid Chromatography Mass Spectrometry ◽  
Spectrometry Analysis ◽  
Sds Page

Purpose. To investigate the effect of ocular hypertension-induced isomerization of aspartic acid in retinal proteins. Methods. Adult Wistar rats with ocular hypertension were used as an experimental model. D-β-aspartic acid-containing proteins were isolated by SDS-PAGE and western blot with an anti-D-β-aspartic acid antibody and identified by liquid chromatography-mass spectrometry analysis. The concentration of ATP was measured by ELISA. Results. D-β-aspartic acid was expressed in a protein band at around 44.5 kDa at much higher quantities in the retinas of rats with ocular hypertension than in those of normotensive rats. The 44.5 kDa protein band was mainly composed of α-enolase, S-arrestin, and ATP synthase subunits α and β, in both the ocular hypertensive and normotensive retinas. Moreover, increasing intraocular pressure was correlated with increasing ATP concentrations in the retinas of rats. Conclusion. Ocular hypertension affected the expression of proteins containing D-β-aspartic acid, including ATP synthase subunits, and up-regulation of ATP in the retinas of rats.

scholarly journals N-Terminomics Strategies for Protease Substrates Profiling

Molecules ◽  
2021 ◽  
Vol 26 (15) ◽  
pp. 4699
Author(s):  
Mubashir Mintoo ◽  
Amritangshu Chakravarty ◽  
Ronak Tilvawala
Keyword(s):  
Mass Spectrometry ◽  
Protease Activity ◽  
Viral Infections ◽  
Mass Spectrometry Analysis ◽  
Post Translational Modification ◽  
Spectrometry Analysis ◽  
Physiological Conditions ◽  
Inflammatory Conditions ◽  
Biological Mixtures

Proteases play a central role in various biochemical pathways catalyzing and regulating key biological events. Proteases catalyze an irreversible post-translational modification called proteolysis by hydrolyzing peptide bonds in proteins. Given the destructive potential of proteolysis, protease activity is tightly regulated. Dysregulation of protease activity has been reported in numerous disease conditions, including cancers, neurodegenerative diseases, inflammatory conditions, cardiovascular diseases, and viral infections. The proteolytic profile of a cell, tissue, or organ is governed by protease activation, activity, and substrate specificity. Thus, identifying protease substrates and proteolytic events under physiological conditions can provide crucial information about how the change in protease regulation can alter the cellular proteolytic landscape. In recent years, mass spectrometry-based techniques called N-terminomics have become instrumental in identifying protease substrates from complex biological mixtures. N-terminomics employs the labeling and enrichment of native and neo-N-termini peptides, generated upon proteolysis followed by mass spectrometry analysis allowing protease substrate profiling directly from biological samples. In this review, we provide a brief overview of N-terminomics techniques, focusing on their strengths, weaknesses, limitations, and providing specific examples where they were successfully employed to identify protease substrates in vivo and under physiological conditions. In addition, we explore the current trends in the protease field and the potential for future developments.

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