Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UNIPROT:P04040 (
Catalase
)
3,577
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Intracameral hydrogen peroxide (H2O2) is cleared at a faster rate in young (t1/2, 93 seconds) than in adult (t1/2, 109 seconds) rabbits. Extrapolated zero time concentrations of H2O2 were 3.3 mM in adults and 3.2 mM in young. The more rapid disappearance of H2O2 correlated with greater catalase levels in iris (35%) and corneal endothelium (50%) in young as compared to adult animals.
Catalase
levels have been found to be reduced in ocular tissues with 3-amino-
1H-1,2,4-triazole
(3AT) in a dose-related manner up to 6 ml/kg of an intravenous 3M solution. Iris and ciliary processes showed a linear reduction with dose, while corneal endothelium, liver and lung reached near maximal decreases in catalase activity at 2, 4, and 6 ml/kg, respectively. 3AT caused a significant dose-dependent extension of the rate of clearance of H2O2 from the anterior chamber, that was directly related to catalase loss. The t1/2 for H2O2 disappearance in adult animals increased from 109 seconds with no 3AT, to 147 seconds after 2 ml/kg 3M 3AT, to 161 seconds after 4 ml/kg 3M 3AT and 184 seconds after 6 ml/kg 3M 3AT. Corneal endothelial oxidized glutathione levels were transiently increased after intracameral hydrogen peroxide. Considering the sum total of all tissues of the anterior segment, specific incremental decreases of catalase generated by intravenous 3AT caused the t1/2 of H2O2 clearance from the anterior chamber to become longer, while the reducing power of anterior segment tissues excluding lens epithelium is related clearly to the systemic dose of 3AT.(ABSTRACT TRUNCATED AT 250 WORDS)
...
PMID:Hydrogen peroxide in the rabbit anterior chamber: effects on glutathione, and catalase effects on peroxide kinetics. 342 89
Recently, CeNPs have emerged as an effective therapeutic agent due to their redox-active nature encompassing the ability to switch between +4 or +3 oxidation states of surface "Ce" atoms. CeNPs with predominantly high Ce +4 oxidation state have been shown to exhibit biological catalase enzyme-like activity.
Catalase
enzyme is naturally present in mammalian cells and facilitates the protection from reactive oxygen species (ROS), generated due to decomposition of hydrogen peroxide (H
2
O
2
). Inactivation of cellular catalase enzyme is known to cause several diseases such as acatalasemia, type 2 diabetes mellitus, and vitiligo. In this study, we have artificially inhibited the activity of cellular catalase enzyme from human liver cells (WRL-68) using 3-Amino-
1,2,4-Triazole
(3-AT). Further, CeNPs was used for imparting protective effect against the deleterious effects of elevated cellular H
2
O
2
concentration. Our results suggest that CeNPs (+4) can protect hepatic cells from cytotoxicity and genetic damage from the high concentrations of H
2
O
2
in the absence of functional catalase enzyme. CeNPs were efficiently internalized in WRL-68 cells and effectively scavenge the free radicals generated due to elevated H
2
O
2
inside the cells. Additionally, CeNPs were also shown to protect cells from undergoing early apoptosis and DNA damage induced due to the 3-AT exposure. Moreover, CeNPs did not elicit the natural antioxidant defense system of the cells even in the absence of functional catalase enzyme, suggesting that the observed protection was due to the H
2
O
2
degradation activity of CeNPs (+4). Our finding substantiates the reinforcement of CeNPs as pharmacological agents for the treatment of diseases related to nonfunctional biological catalase enzyme in the mammalian cells.
...
PMID:Redox-dependent catalase mimetic cerium oxide-based nanozyme protect human hepatic cells from 3-AT induced acatalasemia. 3058 18
