Molecular cloning and characterization of Mn-superoxide dismutase from disk abalone (Haliotis discus discus)

Ekanayake, Prashani Mudika; Kang, Hyun-Sil; Zyosa, Mahanama De; Jee, Youngheun; Lee, Youn-Ho; Lee, Jehee

doi:10.1016/j.cbpb.2006.08.004

Cited by 37 publications

(16 citation statements)

References 30 publications

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“…Similar results were also observed in Mn-SODs of Litopenaeus vannamei, Haliotis discus discus and H. mylodon (Ekanayake et al 2006;Gómez-Anduro et al, 2006;Cho et al, 2009). Therefore, these findings suggest that…”

Section: Discussionsupporting

confidence: 83%

Purification, molecular cloning, and some properties of a manganese-containing superoxide dismutase from Japanese flounder (Paralichthys olivaceus)

Wang

Osatomi

Nagatomo

et al. 2011

Comparative Biochemistry and Physiology Part B: Biochemistry an

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Manganese-superoxide dismutase (Mn-SOD) from Japanese flounder (Paralichthys olivaceus) hepatopancreas has been purified with high purification (781-fold) and recovery (10.8%). The molecular mass of the purified enzyme was estimated to be 26 kDa by SDS-PAGE under reducing conditions. In activity staining by native-PAGE, the Japanese flounder Mn-SOD gave three active bands and exhibited KCN-insensitive activity. In addition, the electrophoretic mobility of this enzyme was observed to be faster than that of Japanese flounder Cu,Zn-SOD. On the other hand, the N-terminal amino acid sequence of this Mn-SOD was determined to be 16 amino acid residues, and the sequence showed high homology to other Mn-SODs but not Japanese flounder Cu,Zn-SOD. Analysis of nucleotide and deduced amino acid sequences revealed that the Mn-SOD cDNA consisted of a 64 bp 5'-non-coding region, a 675 bp open reading frame encoding 225 amino acids, and a 465 bp 3'-non-coding region. The first 27 amino acids containing a mitochondria-targeting signal were highly conserved among other Mn-SODs.

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Section: Discussionsupporting

confidence: 83%

Purification, molecular cloning, and some properties of a manganese-containing superoxide dismutase from Japanese flounder (Paralichthys olivaceus)

Wang

Osatomi

Nagatomo

et al. 2011

Comparative Biochemistry and Physiology Part B: Biochemistry an

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“…The purified enzyme showed 2,324 U/mg activity. This value was almost similar to the MnSOD activity reported from Haliotis discus discus (Ekanayake et al, 2006), but lower to MnSOD reported from Tatumella ptyseos (Ken et al, 2005).…”

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confidence: 85%

“…levisporus exhibited remarkable thermal stability. The activity of a MnSOD from Haliotis discus discus was destroyed completely at 70°C after 1 h (Ekanayake et al, 2006). The periplasmic Cu/ZnSOD from E. coli suffered a reversible inactivation when heated to 70°C for 29 min (Benov et al, 1997).…”

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confidence: 99%

Cloning, expression, and characterization of thermostable Manganese superoxide dismutase from Thermoascus aurantiacus var. levisporus

et al. 2009

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A superoxide dismutase (SOD) gene of Thermoascus aurantiacus var. levisporus, a thermophilic fungus, was cloned, sequenced, and expressed in Pichia pastoris and its gene product was characterized. The coding sequence predicted a 231 residues protein with a unique 35 amino acids extension at the N-terminus indicating a mitochondrial-targeting sequence. The content of Mn was 2.46 microg/mg of protein and Fe was not detected in the purified enzyme. The enzyme was found to be inhibited by NaN(3), but not by KCN or H(2)O(2). These results suggested that the SOD in Thermoascus aurantiacus var. levisporus was the manganese superoxide dismutase type. In comparison with other MnSODs, all manganese-binding sites were also conserved in the sequence (H88, H136, D222, H226). The molecular mass of a single band of the enzyme was estimated to be 21.7 kDa. The protein was expressed in tetramer form with molecular weight of 68.0 kDa. The activity of purified protein was 2,324 U/mg. The optimum temperature of the enzyme was 55 degrees C and it exhibited maximal activity at pH 7.5. The enzyme was thermostable at 50 and 60 degrees C and the half-life at 80 degrees C was approximately 40 min.

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“…The heat inactivation was obtained as previously described and confirmed by spectrophotometer analysis. Non-heated exogenous enzymes were normally active [14,58].…”

Section: Experimental Protocols (Fig 2)mentioning

confidence: 99%

Post-ischemic early acidosis in cardiac postconditioning modifies the activity of antioxidant enzymes, reduces nitration, and favors protein S-nitrosylation

Penna

Perrelli

Tullio

et al. 2011

Pflugers Arch - Eur J Physiol

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Postconditioning (PostC) modifies early post-ischemic pH, redox-environment and activity of enzymes. We hypothesized that early acidosis in PostC may affect superoxide-dismutase (SOD) and catalase(CAT) activities, may reduce 3-nitrotyrosine(3-NT)-and may increase S-nitrosylated (SNO)-protein levels, thus deploying its protective effects. To verify this hypothesis, we studied early (7 th min) and late (120 th min) phases of reperfusion a) endogenous-SOD and -CAT activities, and b) 3-NT-and SNO-protein levels. Isolated rat hearts underwent 30-min ischemia/120-min reperfusion(I/R) or PostC (5 cycles of 10-s I/R at the beginning of 120-min reperfusion) either with or without exogenous-CAT or -SOD infused during the initial 3-min of reperfusion. The effects of early reperfusion with acidic-buffer(AB, pH 6.8) on endogenous antioxidant-enzymes were also tested. Pressure, infarct-size and lactate-dehydrogenase release were also measured. At the 7 th min, PostC induced a significant decrease in SOD-activity with no major change in both Mn-and Cu/Zn-SOD levels, and in CAT-activity and level. PostC also reduced 3-NT and increased SNO levels. Exogenous-SOD, but not -CAT abolished PostCcardioprotection. In late reperfusion(120-min), I/R increased SOD-activity, but decreased CATactivity and Cu/Zn-SOD levels; these effects were reversed by PostC; 3-NT was not affected, but SNO was increased by PostC. AB reproduced PostC effects on antioxidant-enzymes.Conclusions: PostC downregulates endogenous-SOD and preserves -CAT activity, thus increasing SNO and reducing 3-NT levels. These effects are triggered by early post-ischemic acidosis. Yet acidosis-induced SOD-downregulation may limit denitrosylation; thus contributing to PostC-triggering. Hence, exogenous-SOD, but not -CAT, interferes with PostC-triggering.Persistent SOD-downregulation and SNO-increase may contribute to PostC and AB beneficial effects.

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Molecular cloning and characterization of Mn-superoxide dismutase from disk abalone (Haliotis discus discus)

Cited by 37 publications

References 30 publications

Purification, molecular cloning, and some properties of a manganese-containing superoxide dismutase from Japanese flounder (Paralichthys olivaceus)

Purification, molecular cloning, and some properties of a manganese-containing superoxide dismutase from Japanese flounder (Paralichthys olivaceus)

Cloning, expression, and characterization of thermostable Manganese superoxide dismutase from Thermoascus aurantiacus var. levisporus

Post-ischemic early acidosis in cardiac postconditioning modifies the activity of antioxidant enzymes, reduces nitration, and favors protein S-nitrosylation

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