PUBLICATION
Profenofos induced biochemical alterations and in silico modelling of hatching enzyme, ZHE1 in zebrafish (Danio rerio) embryos
- Authors
- Pamanji, R., Yashwanth, B., Venkateswara Rao, J.
- ID
- ZDB-PUB-160614-1
- Date
- 2016
- Source
- Environmental Toxicology and Pharmacology 45: 123-131 (Journal)
- Registered Authors
- Keywords
- Antioxidant enzymes, Hsp70, In silico, Profenofos, ZHE1, Zebrafish
- MeSH Terms
-
- Animals
- Binding Sites
- Catalase/metabolism
- Computer Simulation
- DNA Damage
- Female
- Glutathione/metabolism
- Glutathione Reductase/metabolism
- Glutathione Transferase/metabolism
- HSP70 Heat-Shock Proteins
- Insecticides/toxicity*
- Male
- Metalloproteases/metabolism*
- Models, Molecular*
- Organothiophosphates/toxicity*
- Oxidative Stress/drug effects
- Superoxide Dismutase/metabolism
- Water Pollutants, Chemical/toxicity*
- Zebrafish/metabolism
- Zebrafish/physiology
- Zebrafish Proteins/metabolism*
- PubMed
- 27295611 Full text @ Environ. Toxicol. Pharmacol.
Citation
Pamanji, R., Yashwanth, B., Venkateswara Rao, J. (2016) Profenofos induced biochemical alterations and in silico modelling of hatching enzyme, ZHE1 in zebrafish (Danio rerio) embryos. Environmental Toxicology and Pharmacology. 45:123-131.
Abstract
The current study was aimed to investigate the oxidative stress response in zebrafish embryos exposed to sub-lethal (LC10) and lethal (LC50) concentrations of profenofos for 96-h and in silico modelling of zebrafish hatching enzyme, ZHE1 to explain the delayed hatching. Embryos exposed to profenofos under semi-static conditions significantly diminished glutathione (GSH), superoxide dismutase (SOD) and glutathione reductase (GR) levels, but increased the activities of catalase (CAT) and glutathione S-transferase (GST) concomitantly with marked elevation in malondialdehyde (MDA) content in whole-body homogenate of the treated groups compared with control. In addition, stress protein Hsp70 expression and DNA damage were significantly increased in a concentration- dependent manner compared with controls. From the computational docking studies of ZHE1 with profenofos revealed that profenofos is binding to three amino acids, histidine 99, histidine 109 and arginine 182 at the active site of the enzyme through hydrogen bonding which may lead to inhibition of hatching.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping