scholarly journals Concentration dependence of in vitro biotransformation rates of hydrophobic organic sunscreen agents in rainbow trout S9 fractions: Implications for bioaccumulation assessment

2019 ◽  
Vol 38 (3) ◽  
pp. 548-560 ◽  
Author(s):  
Leslie J. Saunders ◽  
Simon Fontanay ◽  
John W. Nichols ◽  
Frank A.P.C. Gobas
2014 ◽  
Vol 17 (3) ◽  
pp. 453-458 ◽  
Author(s):  
J. Małaczewska ◽  
A. K. Siwicki ◽  
R. Wójcik ◽  
W. a. Turski ◽  
E. Kaczorek

Abstract Kynurenic acid (KYNA), an endogenous neuroprotectant formed along the kynurenine pathway of tryptophan degradation, is a selective ligand of the GPR35 receptor, which can be found on the surface of various populations of human immune cells. In infections and inflammations, KYNA produces an anti-inflammatory effect through this receptor, by depressing the synthesis of reactive oxygen species and pro-inflammatory cytokines. However, it is still unrecognized whether receptors for kynurenic acid are also localized on immune cells of poikilothermic animals, or whether KYNA is able to affect these cells. The objective of this study has been to determine the effect of different concentrations of kynurenic acid (12.5 μM to 10 mM) on the viability and mitogenic response of lymphocytes and on the activity of phagocytic cells isolated from blood and the spleen of rainbow trout. The results imply low toxicity of kynurenic acid towards fish immune cells, and the proliferative effect observed at the two lowest concentrations of KYNA (12.5 μM and 25 μM) seems indicative of endogenous kynurenic acid being capable of activating fish lymphocytes. Non-toxic, micromole concentrations of KYNA, however, had no influence on the mitogenic response of lymphocytes nor on the activity of phagocytes in rainbow trout under in vitro conditions. There is some likelihood that such an effect could be observed at lower, nanomole concentrations of KYNA.


2006 ◽  
Vol 40 (15) ◽  
pp. 4653-4658 ◽  
Author(s):  
Heather M. Stapleton ◽  
Brian Brazil ◽  
R. David Holbrook ◽  
Carys L. Mitchelmore ◽  
Rae Benedict ◽  
...  

2010 ◽  
Vol 120 (1) ◽  
pp. 42-58 ◽  
Author(s):  
Abby D. Benninghoff ◽  
William H. Bisson ◽  
Daniel C. Koch ◽  
David J. Ehresman ◽  
Siva K. Kolluri ◽  
...  

1987 ◽  
Vol 10 (9) ◽  
pp. 443-448 ◽  
Author(s):  
MITSUSHI HIKIDA ◽  
SHUZO IWATA
Keyword(s):  

2019 ◽  
Vol 207 ◽  
pp. 43-51 ◽  
Author(s):  
Richard C. Kolanczyk ◽  
Jeffrey S. Denny ◽  
Barbara R. Sheedy ◽  
Patricia K. Schmieder ◽  
Mark A. Tapper

1996 ◽  
Vol 109 (3) ◽  
pp. 569-578 ◽  
Author(s):  
H. Herrmann ◽  
M.D. Munick ◽  
M. Brettel ◽  
B. Fouquet ◽  
J. Markl

We have isolated from a rainbow trout (Oncorhynchus mykiss) spleen cDNA library a clone coding for vimentin. The deduced amino acid sequence reveals a high degree of identity with vimentin from carp (81%), frog (71%), chick and human (73% each). Large stretches in the central alpha-helical rod are identical within all four classes of vertebrates, but in 17 residues spread over the entire rod, the two fish differ distinctly from the tetrapod species. In addition, in the more diverged non-helical head domain, a nonapeptide motif previously shown to be important for regular filament formation is conserved. Recombinant trout vimentin assembles into bona fide filaments in vitro, with a temperature optimum between 18 and 24 degrees C. Above 27 degrees C, however, filament assembly is abruptly abolished and short filaments with thickened ends as well as structures without typical intermediate filament appearance are formed. This distinguishes its assembly properties significantly from amphibian, avian and mammalian vimentin. Also in vivo, after cDNA transfection into vimentin-free mammalian epithelial cells, trout vimentin does not form typical intermediate filament arrays at 37 degrees C. At 28 degrees C, and even more pronounced at 22 degrees C, the vimentin-positive material in the transfected cells is reorganized in the perinuclear region with a partial fibrillar appearance, but typical intermediate filament arrays are not formed. Together with immunoblotting and immunolocalization data from trout tissues, where vimentin is predominantly found in glial and white blood cells, we conclude that vimentin is indeed important in its filamentous form in fish and other vertebrates, possibly fulfilling cellular functions not directly evident in gene targeting experiments carried out in mice.


1991 ◽  
Vol 156 (1) ◽  
pp. 233-248 ◽  
Author(s):  
S. THOMAS ◽  
R. KINKEAD ◽  
P. J. WALSH ◽  
C. M. WOOD ◽  
S. F. PERRY

The sensitivity of red blood cell Na+/H+ exchange to exogenous adrenaline was assessed in vitro using blood withdrawn from catheterized rainbow trout (Oncorhynchus mykiss) maintained under normoxic conditions [water PO2, (PwO2)=20.66 kPa] or after exposure to moderate hypoxia (PwO2=6.67-9.33 kPa) for 48 h, which chronically elevated plasma adrenaline, but not noradrenaline, levels. Peak changes in whole-blood extracellular pH over a 30 min period after adding 50–1000 nmoll−1 adrenaline were employed as an index of sensitivity; the blood was pre-equilibrated to simulate arterial blood gas tensions in severely hypoxic fish (PaO2=2.0 kPa, PaCO2=0.31 kPa). Blood pooled from normoxic fish displayed a dose-dependent reduction in whole-blood pH after addition of adrenaline. Blood pooled from three separate groups of hypoxic fish, however, displayed diminished sensitivity to adrenaline, ranging from complete desensitization to a 60%reduction of the response. Subsequent experiments performed on blood from individual (i.e. not pooled) normoxic or hypoxic fish demonstrated an inverse correlation between the intensity of H+ extrusion (induced by exogenous adrenaline addition) and endogenous plasma adrenaline levels at the time of blood withdrawal. However, acute increases in plasma adrenaline levels in vitro did not affect the responsiveness of the red blood cell to subsequent adrenergic stimulation. The intensity of H+ extrusion was inversely related to the PaO2in vivo between 2.67 and 10.66 kPa, and directly related to the logarithm of the endogenous plasma adrenaline level. The results suggest that desensitization of Na+/H+ exchange in chronically hypoxic fish is related to persistent elevation of levels of this catecholamine. This desensitization can be reversed in vitro as a function of time, but only when blood is maintained under sufficiently aerobic conditions.


Author(s):  
Lyudmyla Buyun ◽  
Oleksandr Gyrenko ◽  
Maryna Opryshko ◽  
Lyudmyla Kovalska ◽  
Halyna Tkachenko ◽  
...  

This research aimed to evaluate the in vitro effect of buffer extract obtained from leaves and pseudobulbs (modified shoots) of Dendrobium parishii Rchb. f. on the 2-thiobarbituric acid reactive substances (TBARS) as lipid peroxidation biomarker, aldehydic and ketonic derivatives of oxidatively modified proteins, and total antioxidant capacity (TAC) in the muscle tissue of the rainbow trout (Oncorhynchus mykiss Walbaum). The shoots (pseudobulbs) with leaves of Dendrobium parishii cultivated under glasshouse conditions were sampled at M.M. Gryshko National Botanic Garden (NBG) (Kyiv, Ukraine). Since 1999, the whole collection of tropical and subtropical plants (including orchids) has had the status of a National Heritage Collection of Ukraine and is supported through State funding. Besides, NBG’s collection of tropical orchids was registered at the Administrative Organ of CITES in Ukraine (Ministry of Environment Protection, registration No. 6939/19/1-10 of 23 June 2004). The collected pseudobulbs and leaves were brought into the laboratory for biochemical studies. Freshly collected leaves were washed, weighed, crushed, and homogenized in 0.1M phosphate buffer (pH 7.4) (in proportion 1:19, w/w) at room temperature. The extract was then filtered and investigated for its antioxidant capacity. The extract was stored at -20°C until use. The increase in TBARS level in the muscle tissue exposed to extracts derived from leaves and pseudobulbs of D. parishii was insignificant. The level of ketonic derivatives of oxidatively modified proteins was non-significantly decreased both for leaf and pseudobulb extracts compared to the untreated samples. The extracts obtained from leaves and pseudobulbs of D. parishii significantly increased the TAC level in muscle tissue due to inhibited the Fe2+/ascorbate-induced oxidation of Tween 80. Overall, these findings demonstrate that aqueous extracts of vegetative organs of Dendrobium parishii can enhance the total antioxidant capacity in the muscle tissue of the rainbow trout. Moreover, this antioxidant effect was more intensive for pseudobulb extracts.


Sign in / Sign up

Export Citation Format

Share Document