Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P30044 (antioxidant enzyme)
 8,037 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Copper trafficking in mammalian cells is highly regulated. CCS is a copper chaperone that donates copper to the antioxidant enzyme copper/zinc superoxide dismutase 1 (SOD 1). Mutations of SOD1 are responsible for approximately 20% of familial amyotrophic lateral sclerosis (FALS). Monospecific antibodies were generated to evaluate the localization and cellular distribution of this copper chaperone in human and mouse brain as well as other organs. CCS is found to be ubiquitously expressed by multiple tissues and is present in particularly high concentrations in kidney and liver. In brain and spinal cord, CCS was found throughout the neuropil, with expression largely confined to neurons and some astrocytes. Like SOD1, CCS immunoreactivity was intense in Purkinje cells, deep cerebellar neurons, and pyramidal cortical neurons, whereas in spinal cord, CCS was highly expressed in motor neurons. In cortical neurons, CCS was present in the soma and proximal dendrites, as well as some axons. Although the distribution of CCS paralleled that of SOD1, there was a 12-30-fold molar excess of SOD1 over CCS. That both SOD1 and CCS are present, together, in cells that degenerate in ALS also emphasizes the potential role of CCS in mutant SOD1-mediated toxicity.
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PMID:The copper chaperone CCS is abundant in neurons and astrocytes in human and rodent brain. 988 96

Ten years ago, the linkage between mutations in the gene coding for the antioxidant enzyme Cu,Zn superoxide dismutase (SOD1) and the neurodegenerative disease known as familial amyotrophic lateral sclerosis (FALS) was established. This finding has prompted a myriad of new studies in experimental models aimed at investigating the toxic function of the mutant enzymes. The cellular functions that are impaired in motoneurons as a consequence of molecular alterations induced by the expression of FALS SOD1 converge on pathways that might be activated in sporadic ALS by other toxic factors. Recent data demonstrate that, although motoneurons are lost in patients, other cell types are also affected and actively contribute to the pathogenesis of the disease.
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PMID:Lessons from models of SOD1-linked familial ALS. 1531 Apr 60

Research increasingly suggests that enantiomer selectivity may be a part of the toxicological effects of chiral contaminants. In this study, we selected Japonica rice variety Xiushui 63 seedlings to evaluate the enantioselectivity of imazethapyr (IM). Significant differences in rice seedling morphology, antioxidant enzyme, oxidant marker and gene transcription were observed between the two IM enantiomers. In the seedling morphological assay, IM enantiomers inhibited elongation of primary roots and shoots, and reduced the number of adventitious roots and the density of root hairs. The inhibitory effects were enhanced with increasing concentrations of IM. The maximal root relative inhibition rate reached 80.4%, 67.0%, and 73.5% for R-(-)-IM, S-(+)-IM and racemate at the concentration of 0.5 mg L(-1), respectively, and the maximal shoot relative inhibition rate reached 77.7%, 26.9%, and 61.7%, respectively. The activities of SOD, POD and CAT and the content of MDA increased at 0.5 mg L(-1) of R-(-)-IM treatment, and were 1.8, 3.3, 1.4, and 2.2 times, respectively, over the activities S-(+)-IM. Real-time PCR showed that R-(-)-IM minimized the transcript abundance of ALS in shoot tissue to 12.2% of the S-(+)-IM, and minimized the transcript abundance of PC in seed to 9.2% of the S-(+)-IM. R-(-)-IM maximized the transcript abundance of beta-amylase in shoots to 8.6-time of the S-(+)-IM. Results from this study imply that R-(-)-IM has stronger toxicity on the growth of rice than S-(+)-IM.
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PMID:Enantioselective phytotoxicity of the herbicide imazethapyr in rice. 1950 84