Commander Squid Berryteuthis Magister Research Articles

First Data on Ecology and Biology of Arctoraja sexoculata (Arhynchobatidae) from the Area off Kuril Islands

First information on the Arctoraja sexoculata frequency of occurrence, ecology, and biology, from the area off the middle Kuril Islands has been provided. It is estimated that the Arctoraja sexoculata is a common bycatch species in trawl fishing for the commander squid Berryteuthis magister in this water area. The locations of catch events for this species were localized off the Ketoy and Simushir Islands and in the Diana Strait at the depths of 250–490 m at a water temperature near the bottom of 1.8–2.5°С. It is supposed that the species belongs to the mesobenthal ichthyocene. In the catches, A. sexoculata represented by individuals of 26–90 cm length and 0.1–5.6 kg body mass. The species probably reaches the age of maturity for the first time at 8–9 years old and over. Its highest life expectancy is 16 years. The individuals of 50–90 cm length become predators consuming predominantly cephalopods and fishes, in the same time isopods and ctenophores among the food items were rarely recorded.

Substrate–inhibitor specificity of cholinesterase and monoamine oxydase from optic ganglia of the pacific squid Todarodes pacificus and commander squid Berryteuthis magister

A comparative analysis of enzymological characteristics of cholinesterase (ChE) and monoamine oxydase (MAO) from the optic ganglia was performed in the Pacific squid Todarodes pacificus and Commander squid Berryteuthis magister caught in their four habitats across the Pacific Northwest. A substrate–inhibitor analysis revealed a homogeneity of T. pacificus and B. magister ChE preparations as well as homogeneity of T. pacificus vs. heterogeneity of B. magister MAO preparations. In case of thiocholine derivatives, the rate of hydrolysis induced by T. pacificus ChE was practically independent of the structure of the acyl group, whereas in case of B. magister ChE it was found to decrease in this substrate series. It is only T. pacificus MAO that was found to be able to deaminate also a diaminooxydase substrate histamine. ChE activity was higher in T. pacificus than in B. magister for the whole substrate series, while for MAO the same activity pattern was observed for tyramine, tryptamine and serotonin. In both squids, the sensitivity of ChE to organophosphorus inhibitors containing the dimethylbutyl group was by several orders of magnitude higher than that in mammals. The sensitivity of ChE to the siloxane reversible inhibitors was lower in T. pacificus ChE and much lower in B. magister than in mammals.

Activities of Tetramethylene-Bis-Onium Reversible Cholinesterase Inhibitors as Influenced by the Nature of the Onium Atom

Inorganic tetramethylene bis-onium compounds were studied as reversible inhibitors of various cholinesterases (ChE), i.e., human erythrocyte acetyl-ChE, horse blood serum butyryl-ChE, grass frog Rana temporaria brain ChE, and Pacific squid Todarodes pacificus and commander squid Berryteuthis magister visual ganglia ChE from various habitats in the northwest Pacific Ocean, in order to study the influence of the nature of the onium atom on their anti-ChE activities. bis-Phosphonium inhibitors turned out to be significantly more potent effectors than bis-ammonium compounds, which may actually have been due to the significant increases of size and hydrophobicity of the onium groups. The bis-ammonium organosilicon compound and its monoammonium analog turned out to be equally active as reversible ChE inhibitors in mammals. The bis-phenyliodonium derivative was studied for the first 7time, was characterized by significantly increased hydrophobicity due to introduction of F atoms into the tetramethylene spacer in the onium chain, and exhibited marked anti-ChE activity with respect to mammalian ChE.

Tetramethonium derivatives as reversible inhibitors of various cholinesterases

To study the effect of the onium atom nature on anticholinesterase efficiency, we tested elementorganic derivatives of tetramethylenbisonium compounds as reversible inhibitors of the following cholinesterases (ChE): acetyl-ChE from human erythrocytes, butyryl-ChE from horse serum, ChE from the brain of the grass frog Rana temporaria, ChEs from visual ganglia of the Pacific squid Todarodes pacificus, and ChE from visual ganglia of the commander squid Berryteuthis magister from different habitats in the Northwestern Pacific Ocean. Bisphosphonium inhibitors were found to be much stronger effectors than bisammonum compounds, although this may be due to a significantly increased size and hydrophobicity of their onium groups. Bisammonium organosilicon compound and its monoammonium analog were equally active as reversible ChE inhibitors in mammals. The first studied bis(phenyliodonium) derivative, which is characterized by a significantly increased hydrophobicity due to the introduction of fluorine atoms to the interonium tetramethylene chain, also exhibited a pronounced anticholinesterase effect on mammalian ChE.

Reversible lupinin inhibitors of cholinesterases of mammalian blood and of optical ganglia of individuals of the Commander squid Berryteuthis magister from different zones of species areal

Arylsulfoesters and carbonic lupinin esters are studied for the first time as reversible inhibitors of mammalian blood cholinesterases. Studied in detail is sensitivity of cholinesterases to mono- and bislupinin inhibitors in Commander squid individuals from different habitation zones.

Comparative-enzymological study of cholinesterases from optic ganglia of the Commander squid Berryteuthis magister individuals inhabiting different zones of the species area

In this review a comparative analysis is performed of enzymological characteristics of cholinesterase (ChE) from optic ganglia of individuals of the Commander squid Berryteuthis magister caught in 8 zones of its habitation areal in the northern-western Pacific aquatorium, of ChE of the Pacific squid Todarodes pacificus as well as of the "standard" acetylcholinesterase from human erythrocytes and butyrylcholinesterase from horse blood serum. By the method of the substrate-inhibitor analysis there was shown heterogeneity of ChE preparations from the B. magister individuals from different habitation zones. Kinetic parameters of the enzymatic hydrolysis of 8 ester substrates are presented as well as the data on study of inhibitory specificity with use of 20 irreversible organophosphorus inhibitors, which show identity of ChE properties in the B. magister individuals from different habitation zones. Study of the process of the ChE reversible inhibition from the Commander squid individuals under action of 57 mono- and bisonium inhibitors has revealed differences in ChE properties of squid individuals from isolates in different zones of the habitation areal, which argues in favor of the existence of intraspecies groups of the Commander squid B. magister.

Predatory role of the commander squid Berryteuthis magister in the eastern Bering Sea: insights from stable isotopes and food habits

Squid are an important component of many marine food webs, and they can impact other species through predation and competition. However, quantifying their influence on other food web components requires knowledge of their trophic position and trophic ontogeny, which are unknown in many ecosystems. The eastern Bering Sea (EBS) is a highly productive region that sup- ports large commercial fisheries, and a modicum of knowledge exists on the ecological role of squid in this region. We combined stomach content and stable isotope analyses of muscle tissue (! 15 N and ! 13 C) to identify the feeding ecology of the commander squid Berryteuthis magister in the EBS conti- nental slope ecosystem. We also use a novel methodology to elucidate potential finer-scale variation in squid trophic ecology by reconstructing feeding chronologies of individual B. magister from con- centric eye lens layers. Our analyses indicate that the position of B. magister in the EBS food web increases by approximately 1 trophic level between juvenile and adult stages. Also, in contrast to many squid species, we found that predation by B. magister is not constrained by prey body size and that B. magister are more likely to share prey resources with commercially valuable fishes, particu- larly walleye pollock Theragra chalcogramma, than to prey upon their juvenile stages. Further, the reconstructed feeding chronologies indicate substantial variability in squid feeding patterns that are not captured on the time scales of the conventional analyses. Together, the findings of this study con- tribute to a better understanding of the ecological role of B. magister and the trophic linkages and energy flow within the EBS food web.

Comparative study of substrate and inhibitory specificity of monoamine oxidase of squid optic ganglia

Comparative study of substrate specificity of monoamine oxidase (MAO) of optic ganglia of the Pacific squid Todarodes pacificus and the Commander squid Berryteuthis magister has been carried out. The enzyme of the Pacific squid, unlike that of the Commander squid, has been established to be able to deaminate not only tyramine, tryptamine, serotonin, benzylamine, and β-phenylethylamine, but also histamine-substrate of diamine oxidase (DAO). In relation to all studied substrates, the MAO activity of optic ganglia of T. pacificus is several times higher as compared with that of B. magister. In the case of deamination of serotonin this difference was the highest and amounted to 5 times. Semicarbazide, the classic DAO inhibitor, at a concentration of 10 mM did not inhibit catalytic activity of both studied enzymes. The substrate-inhibitory analysis with use of deprenyl and clorgyline, specific inhibitors of different MAO forms, indicates homogeneity of the enzyme of the Pacific squid and heterogeneity of the Commander squid enzyme whose composition seems to contain at least two MAO forms. There are obtained quantitative differences in substrate specificity and reaction capability with respect to the inhibitors clorgylin and deprenyl for MAO of optic ganglia of the studied squid species. These differences probably can be explained by significant differences in the evolutionary level of these biological species.

Interaction of cholinesterase from the visual ganglia of the commander squid Berryteuthis magister from different areas of the range with reversible inhibitors

Interaction of cholinesterase from the visual ganglia of the commander squid Berryteuthis magister from different areas of the range with reversible inhibitors

Substrate specificity of cholinesterase of the commander squid Berryteuthis magister

Substrate specificity of cholinesterase of the commander squid Berryteuthis magister

Catalytical properties of liver monoamine oxidases of the Commander squid Berryteuthis magister from various habitation zones

A detailed kinetic analysis is performed of enzymatic reactions of deamination of tyramine, tryptamine, serotonin, benzylamine, beta-phenylethylamine, and histamine under action of liver monoamine oxidase (MAO) of the Commander squid Berryteuthis magister from various habitation zones in the Bering and Japan Seas. There has been revealed a substrate inhibition by high concentrations of all studied substrates, which seems to indicate mutual effect of various MAO forms present in liver of the studied squids. Analysis of kinetic parameters of enzymatic reactions of deamination of six studied substrates and the substrate-inhibitory analysis with use of two derivatives of acridine and deprenyl indicate the enzyme heterogeneity, the presence of at least two MAO forms and the absence of intraspecies differences in MAO of the Commander squids from various habitation zones. The most active was the MAO form responsible for serotonin deamination. There were obtained quantitative difference in substrate specificity and reaction ability with respect to inhibitor of proflavin for the liver MAO of the Commander and Pacific squids.

The sensitivity of the cholinesterase of the commander squid Berryteuthis magister to organophosphorus inhibitors of different structure

The sensitivity of the cholinesterase of the commander squid Berryteuthis magister to organophosphorus inhibitors of different structure

Anabasine derivatives as reversible and irreversible inhibitors of cholinesterases from different animals

A comparative study was carried out of action of 18 specifically synthesized anabasine derivatives and their analogs, including diiodomethylates of anabasine acylates and bis-anabasine derivatives of dicarboxylic glutaric, adipic, azelaic, and sebacic acids, on activity of cholinesterase of brain of frog Rana temporaria and visual ganglia of the Pacific squid Todarodes pacificus and Commander squid Berryteuthis magister from different zones of habitations in the northwest part of the Pacific Ocean as well as of erythrocyte acetylcholinesterase and serum butyrylcholinesterase. These compounds were not submitted to cholinesterase hydrolysis and turned out to be efficient reversible inhibitors that have to certain degree specificity toward the studied enzymes both by their potency and by the type of their inhibitory action. Specificity of effects of the key structural fragments of the anabasine grouping on anticholinesterase efficacy was checked. Also performed was analysis of action of 24 reversible and irreversible organophosphorus inhibitors, anabasine derivatives, toward erythrocyte acetylcholinesterase and serum butyrylcholinesterase. The anticholinesterase effects of anabasine-containing inhibitors differing in structure and action mechanism was compared.

Use of Bis-Alkaloid Derivatives of Dicarboxylic Acids on the Basis of Lupinine, Anabasine and Cytisine as Reversible Inhibitors of Cholinesterases of Different Origin

Comparative study was carried out on action of a group of bis-alkaloid derivatives (on the basis of lupinine, anabasine, and cytosine, and their iodomethylates) of dicarboxylic acids (succinic, glutaric, azelaic, sebacic) on activity of cholinesterase of optical ganglia of the Commander squid Berryteuthis magister from different zones of habitation in the northwest part of the Pacific Ocean as well as human erythrocyte acetylcholinesterase and horse serum butyrylcholinesterase. These compounds turned out to be potent reversible inhibitors with specificity of action with respect both of sensitivity of the studied enzymes to them and of the type of their inhibitory action. The studied inhibitors can be used as tools in biochemical taxonomy to determine populational structure of such a marketing species as the Commander squid Berryteuthis magister.