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Cyanobacteria, also known as blue-green algae, are prokaryotic, phototrophic microorganisms that may form massive blooms in eutrophic water reservoirs. Some cyanobacterial strains are able to produce secondary metabolites – cyanotoxins that may be hazardous to aquatic and terrestial animals. These compunds can be grouped into: hepatotoxins, neurotoxins, cytotoxins dermatotoxins and irritant toxins. Microcystins are well-known cyclic heptapeptides acting as inhibitors of protein phosphatases type 1 and 2A. These cyanotoxins induce various adverse effects in freshwater invertebrates including biochemical, physiological and behavioral changes. Moreover, accumulation of microcystins in different tissues occurs, therefore transfer of these cyanotoxins through the food chain to animals being at higher trophic levels may be possible. The purpose of this paper is to review the knowledge on the effects of microcystins on three main groups of freshwater invertebrates: zooplankton, higher crustaceans, mollusks and to indicate possible ecotoxicological consequences of this impact on aquatic environment and invertebrate aquacultures.
Cyanobacterial blooms, often observed in eutrophic water reservoirs, produce toxic metabolites known as cyanotoxins that affect animal health. There are five groups of cyanotoxins classified on the basis of their toxic action: hepatotoxins, neurotoxins, cytotoxins, dermatotoxins and irritant toxins. Microcystin (MC) is a very common and well described hepatotoxin produced by various genera, such as Microcystis, Anabaena, Planktothrix, Anabenopsis, Hapalosiphon and Nostoc. It acts as an inhibitor of serine/threonine protein phosphatase 1 (PP1) and 2A (PP2A), inducing hyperphosphorylation of cell proteins and a variety of toxic changes in hepatocytes often leading to liver insufficiency and death caused by hypovolemic shock. Since the reports on MC toxicity are on the increase this cyanotoxin should be treated as an important environmental factor affecting human and animal health. A brief overview of existing literature on the intake, mechanism of action, and hepatotoxic effects on mammalian animals is presented in this paper
Some species of soil bacteria and most organisms living in extreme environments such as salt lakes or coal or salt mines have effective protective mechanisms that enable them to function under adverse conditions. A common way to protect against harmful environmental factors is the production and accumulation of substances with an osmoprotective effect. One of such substances is ectoine, or 1,4,5,6-tetrahydro-2-methyl-4-pyrimidine-carboxylic acid of an amphoteric nature. The effect of ectoin, mainly based on the binding of water molecules, has found wide application in the protection of macromolecules and cells. This work is a review of the use of this amino acid in human and veterinary medicine.
Cyanobacteria (Cyanophyta, Cyanoprocaryota, Cyanobacteria) (blue-green algae) are procaryotic phototrophic microorganisms playing an important ecological role in the freshwater and marine environment as primary producers. However, as a consequence of water eutrophication observed in many reservoirs in different parts of the world, these microorganisms form massive scums, known as water blooms, releasing cyanotoxins hazardous to fish and other aquatic organisms. Cyanotoxins are cyanobacterial secondary metabolites of various chemical structures harmful to humans, terrestial and aquatic animals such as fish. The most abundant cyanotoxins are microcystins and hepatotoxins inducing toxic changes in fish liver, kidney, gills, digestive tract and immune system. Very little is known on the effects of alkaloid neurotoxic anatoxin-a on fish and their immunity. The aim of this study was to assess the in vitro influence of anatoxin-a on immune cells isolated from the common carp (Cyprinus carpio L.). The leukocyte intracellular level of ATP was reduced only at the highest concentration of anatoxin-a. Apoptotic and necrotic leukocytes were observed at the lower and the highest concentrations of anatoxin-a, respectively. Elevated activity of caspases 3/7 after 2 hours and a concentration-dependent decrease in the proliferative ability of T and B lymphocytes was also observed. The results suggest that anatoxin-a could be a possible immunotoxic agent in the aquatic environment and may increase the susceptibility of fish to infectious and neoplastic diseases. Therefore, constant monitoring of anatoxin-a and its producers in lakes and fish ponds should be performed.
The aim of this study was to describe the stability of proteins encoded in mtDNA, which are part of the OXPHOS system, in different model organisms and to define why certain proteins are more prone to be unstable than others. The in silico analyses involved 155 reference sequences of all proteins encoded in the mitochondrial DNA in twelve model organisms representing different phylogenetic groups. The amino acid sequences of the proteins were taken from the GenPept database. The bioinformatic analyses were performed in the ProtParam program. Thirty-eight of the 155 analyzed proteins exhibited instability. The greatest numbers of unstable mitochondrial proteins were detected in H. sapiens and A. mexicanum and the lowest levels were found in C. elegans. ND1 and ATP8 were the most unstable mitochondrial proteins. Proteins COX1 and COX3 did not exhibit instability in the examined group of organisms. The highest instability index values were recorded in the case of protein ATP8. Protein ND1 turned out to be stable in the representatives of the class invertebrates. The preliminary results of the pioneer investigations indicate that the type and number of unstable proteins encoded in mtDNA was species specific. Protein instability in lower organisms may be associated with resistance to oxidative stress. In higher organisms, in turn, protein instability may be related to the physiological production of free oxygen radicals, which play multiple roles in metabolic processes. The phenomenon of instability in the respiratory chain proteins may have a strategic function although it appears to be detrimental to the stability of the protein structure per se.
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