Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P04179 (MnSOD)
 2,777 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Reactive oxygen species are highly toxic agents that appear to have an important role in male infertility. In order to understand the potential for the testis to be protected from reactive oxygen, the mRNA levels of the natural reactive oxygen scavenger, copper-zinc superoxide dismutase (SOD), were determined in testes and other organs in rats using northern analysis and in situ hybridization. Northern analysis of total RNA from organs of 60-day-old rats demonstrated an SOD mRNA with a transcript length of 0.77 kb; its concentration was highest in the kidney, liver, testis, and epididymis. In testis, northern analysis of total RNA demonstrated two mRNA transcripts of 0.77 kb and 0.94 kb. The concentrations of the 0.77-kb transcript varied only slightly between 10 and 100 days of age. In contrast, the 0.94-kb transcript became detectable by northern analysis between 30 and 40 days of age, then its concentration rose progressively to peak at 60 days. In situ hybridization studies demonstrated a uniform distribution of SOD mRNA within seminiferous tubules of prepubertal rats at 10 days of age and a heterogeneous, stage-specific pattern in older animals. In mature rats, the highest level of SOD mRNA was detected in tubules just prior to spermiation (stages VI-VIII). In conclusion, two SOD mRNA transcripts were identified in the rat testes that followed significantly different patterns of expression during development. In situ hybridization studies revealed that accumulation of the SOD mRNA in the seminiferous tubule was stage specific. These data suggest that SOD may play an important role during testicular development and spermatogenesis in rats.
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PMID:Identification and localization of copper-zinc superoxide dismutase gene expression in rat testicular development. 829 28

Spermatozoa are highly sensitive to oxidative stress. The epididymis, a natural sperm reservoir, has maturational and storage functions. The epididymis may also protect spermatozoa from oxidative injury by elaborating scavengers of reactive oxygen species (ROS). Therefore, we have evaluated the mRNA expression of antioxidant enzymes in the normal rat epididymis and the effects of efferent duct ligation no the expression of these enzymes. Adult rat epididymides were harvested, divided into caput, corpus and cauda and processed for RNA extraction. Additional adult rats were subjected to unilateral efferent duct ligation and the epididymides harvested at 1, 4, 8, 16 or 28 days after the procedure. Antioxidant enzyme mRNA expression was assessed by Northern blot analysis using 32P-labelled DNA probes derived from known cDNA sequences for classical cellular glutathione peroxidase (GSHPx), phospholipid hydroperoxide glutathione peroxidase (PHGPX), secretory epididymal glutathione peroxidase (E-GPX), copper-zinc superoxide dismutase (SOD), secretory epididymal superoxide dismutase (E-SOD) and catalase. Specific mRNA levels were measured, with gene expression evaluated relative to total RNA, not per organ. Variations in lane loading were controlled by measuring the levels of 28S ribosomal RNA. GSHPx, PHGPX, SOD and catalase mRNA were detected in the caput, corpus and cauda epididymis. E-GPX mRNA was only detected in the caput, whereas E-SOD mRNA was primarily detected in the corpus. At 28 days after efferent duct ligation, epididymal weight decreased by 34% relative to controls (p < 0.05). With the exception of PHGPX, the relative mRNA levels of the antioxidant enzymes studied did not change after efferent duct ligation. This study demonstrates that mRNAs for multiple antioxidant enzymes are expressed in the epididymis and that the relative expression of these enzymes remains largely unchanged in response to efferent duct ligation. Taken together, these results suggest that antioxidant enzymes may play an important, region-specific role in epididymal function. Expression of the secretory antioxidant enzymes E-SOD and E-GPX is region-specific, indicating that the need for antioxidant enzymes may vary along the length of the epididymis.
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PMID:Identification and characterization of antioxidant enzyme mRNAs in the rat epididymis. 929 18

We studied the immunoexpression of Cu/Zn superoxide dismutase (Cu/ZnSOD) and mRNAs expression of extracellular superoxide dismutase (E-SOD), and epididymal specific glutathione peroxidase 5 (GPX5), in epithelial cells of caput and cauda epididymis of rats treated with finasteride, a steroid-based inhibitor of 5alpha-reductase. The 5alpha-reductase is known to exist in two isoforms. Both 5alpha-red1 and 5alpha-red2 catalyse the irreversible conversion of T into DHT. Formation of DHT in the epididymis is mostly due to the action of 5alpha-red2 and finasteride is more potent inhibitor of this isoform. Rats were treated with finasteride for 56 days covering the duration of one spermatogenesis (four cycles of the seminiferous epithelium). Although E-SOD mRNA is normally expressed in cells of cauda but not of caput epididymis, treatment with finasteride produced the E-SOD transcript in cells of caput epididymis too. The GPX5 transcript was detected in cells of caput epididymis of control and experimental rats, but the level of expression measured densitometrically was significantly lower in finasteride-treated rats. The immunoexpression of Cu/ZnSOD was also changed in epididymis of finasteride-treated rats. Finasteride appears to change the pattern of expression of antioxidant enzymes and may alter the protective function of the epididymis in relation to spermatozoa.
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PMID:Expression of E-SOD, GPX5 mRNAs and immunoexpression of Cu/ZnSOD in epididymal epithelial cells of finasteride-treated rats. 1881 21