(H 2 O 2 ), while catalase (CAT) converts it into water (H 2 O) and oxygen (O 2 ) [96]. In
the present study, induction of SOD activity in gill and liver would help to avoid
reactive oxygen species generation caused by oxidative damage [97]. Similarly,
Matozzo et al. [98] observed an increase of SOD activity in gills of clam Ruditapes
philippinarum exposed to triclosan treatments.
LPO activity in liver of Treatments I and II showed a biphasic trend, and the
values range from 7.56 to 2.16 mol of MDA/g protein and 14.74 to 6.96 mol of
MDA/g protein respectively. Significant changes were observed in the LPO activity
of gill, liver, and kidney of triclosan-exposed rohu fingerlings [75]. The elevation of
LPO level may be due to increased production of ROS, due to ASA stress leading to
lipid peroxidation. The significant changes observed in liver LPO level of fish may
be due to the persuaded activity of antioxidants, increasing the scavenging of free
radicals and reducing MDA production [77].
The CAT and GPx are reactive oxidative species (ROS) reducing enzymes. CAT
eliminates hydrogen peroxide, whereas GPx can detoxify hydrogen peroxide and
degrades fatty acid peroxides [38]. The depleted levels of CAT may be due to its
inactivation by (O 2
À ) or due to the poor detoxifying mechanism as a result of the
excess production of hydrogen peroxide. Perhaps Kono and Fridovich [99]
explained the inhibition of CAT activity by (O 2
À ) and the synergetic reaction
between SOD and CAT. Similarly Ku et al. [100], Alak et al. [101] and Rangasamy
et al. [102] observed changes in CAT activity in Pelteobagrus fulvidraco exposed to
triclosan, in rainbow trout exposed to eprinomectin and in Danio rerio exposed to
ketoprofen.
GST is one of the indispensable liver enzymes that defend the cell from the ROS
toxicity by catalysing the reactive intermediates to reduced glutathione through the
process of biotransformation [103, 104]. The fluctuations seen in gill and liver GST
activity might be resulted from the defence mechanism developed by the fish against
oxidative damage caused by the ASA [105, 106]. Comparably Liao et al. [107] and
Zivina et al. (2013) observed an increase in liver GST activity of medaka fish on
ketamine exposure and in developmental stages of zebrafish on ASA exposure,
whereas Ajima et al. [108] reported for the decreased brain GST activity of the
fish exposed to verapamil.
Glutathione (GSH) is one of the important antioxidants capable of preventing
damage to cells caused by reactive oxygen species [109]. In the current study, GSH
levels in the liver and gill were found to be depleted which indicates its utilization to
meet the oxidative stress caused by the drug. Zhang et al. [110] reported that the
decline in GSH level may be due to the lack of adaptive mechanisms and GSH
oxidation to GSSG. Similar decrease was also noted in Carassius auratus after
exposure to decabromodiphenyl ether and ethane or their mixture [111] and in
Channa punctatus after exposure to thermal power plant effluents [112].
Toxicity Assessment of Acetylsalicylic Acid to a Freshwater Fish Cyprinus. . .
209
the present study, induction of SOD activity in gill and liver would help to avoid
reactive oxygen species generation caused by oxidative damage [97]. Similarly,
Matozzo et al. [98] observed an increase of SOD activity in gills of clam Ruditapes
philippinarum exposed to triclosan treatments.
LPO activity in liver of Treatments I and II showed a biphasic trend, and the
values range from 7.56 to 2.16 mol of MDA/g protein and 14.74 to 6.96 mol of
MDA/g protein respectively. Significant changes were observed in the LPO activity
of gill, liver, and kidney of triclosan-exposed rohu fingerlings [75]. The elevation of
LPO level may be due to increased production of ROS, due to ASA stress leading to
lipid peroxidation. The significant changes observed in liver LPO level of fish may
be due to the persuaded activity of antioxidants, increasing the scavenging of free
radicals and reducing MDA production [77].
The CAT and GPx are reactive oxidative species (ROS) reducing enzymes. CAT
eliminates hydrogen peroxide, whereas GPx can detoxify hydrogen peroxide and
degrades fatty acid peroxides [38]. The depleted levels of CAT may be due to its
inactivation by (O 2
À ) or due to the poor detoxifying mechanism as a result of the
excess production of hydrogen peroxide. Perhaps Kono and Fridovich [99]
explained the inhibition of CAT activity by (O 2
À ) and the synergetic reaction
between SOD and CAT. Similarly Ku et al. [100], Alak et al. [101] and Rangasamy
et al. [102] observed changes in CAT activity in Pelteobagrus fulvidraco exposed to
triclosan, in rainbow trout exposed to eprinomectin and in Danio rerio exposed to
ketoprofen.
GST is one of the indispensable liver enzymes that defend the cell from the ROS
toxicity by catalysing the reactive intermediates to reduced glutathione through the
process of biotransformation [103, 104]. The fluctuations seen in gill and liver GST
activity might be resulted from the defence mechanism developed by the fish against
oxidative damage caused by the ASA [105, 106]. Comparably Liao et al. [107] and
Zivina et al. (2013) observed an increase in liver GST activity of medaka fish on
ketamine exposure and in developmental stages of zebrafish on ASA exposure,
whereas Ajima et al. [108] reported for the decreased brain GST activity of the
fish exposed to verapamil.
Glutathione (GSH) is one of the important antioxidants capable of preventing
damage to cells caused by reactive oxygen species [109]. In the current study, GSH
levels in the liver and gill were found to be depleted which indicates its utilization to
meet the oxidative stress caused by the drug. Zhang et al. [110] reported that the
decline in GSH level may be due to the lack of adaptive mechanisms and GSH
oxidation to GSSG. Similar decrease was also noted in Carassius auratus after
exposure to decabromodiphenyl ether and ethane or their mixture [111] and in
Channa punctatus after exposure to thermal power plant effluents [112].
Toxicity Assessment of Acetylsalicylic Acid to a Freshwater Fish Cyprinus. . .
209