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EC SOD (Extracellular superoxide Dismutase)

Antibody for Immunohistochemistry and Western Blot Analysis (H-075-16)

H-075-16   H-075-16-control

H-075-16-1  H-075-16-control01

H-075-16   H-75-16-control

Protocol for Immunohistochemistry

Tissue Sample

Rat Kidney and Heart Tissue

Fixative

10% formalin

Embedding

Paraffin

Negative Control

No primary antibody (pre-immuno serum)

Pretreatment

Intact

Blocking

2% Normal Goat Serum

Primary Antibody

Rabbit Anti-EC SOD (33-54) (Mouse) Serum (Catalog No.:H-075-16)

Optimal Dilution

 1:100~200 (1hour at RT)

Secondary Antibody

Goat Anti-Rabbit IgG, Biotinylated (1:400), 30 min

Amplification

ABC (Vector), 1:400, 30 min

Detection System

HRP

Substrate

DAB (Sigma), 3 min

Counterstained

Hematoxylin, 30 sec

H-075-16-western blot

Discordant Extracellular Superoxide Dismutase Expression and Activity in Neonatal Hyperoxic Lungs

Antioxidant defenses in the neonatal lung are required to adapt to the oxygen (O2)-rich post-natal environment, and oxidant/antioxidant imbalance predisposes to lung injury when high inspired O2 concentrations are used in neonatal lung diseases. The lung's main extracellular enzymatic defense against superoxide, extracellular superoxide dismutase (EC-SOD), is closely regulated during development. In testing the hypothesis that developmental change in EC-SOD expression and activity in the immature lung would be disrupted by hyperoxia we found doubling of lung EC-SOD protein in newborn rats exposed to 95% O2 for 1 week. Furthermore, EC-SOD protein secretion increased but EC-SOD enzyme activity did not change with O2 exposure. EC-SOD mRNA did not change at multiple points between 6 hours and 8 days. Lung EC-SOD recovered by immunoprecipitation after 1 week of O2 showed strong increases in protein nitrotyrosine and variable, non-significant differences in protein carbonyl content. These data provide the first direct evidence that EC-SOD is itself a target of nitration in hyperoxia, and offer a plausible explanation for low EC-SOD activity despite its increased secretion by O2-exposed neonatal lung.

Mamo et al. Am J Respir Crit Care Med. 2004 Aug 1;170(3):313-8.

Overexpression of Cu/Zn-superoxide dismutase and/or catalase in mice inhibits aorta smooth muscle cell proliferation

BACKGROUND: Increasing evidence demonstrates that reactive oxygen species, for example, superoxide (O(2)(-.)) and hydrogen peroxide (H(2)O(2)), promote vascular smooth muscle cell (VSMC) proliferation, and that superoxide dismutase (SOD) and catalase work in concert to scavenge O(2)(-.) and H(2)O(2). This report examined the effect of overexpressing Cu/Zn-SOD or catalase on epidermal growth factor (EGF)-induced proliferation and mitogen-activated protein kinase (MAPK) phosphorylation in VSMCs.
METHODS: The VSMCs were obtained from the aorta of wild-type mice and transgenic mice overexpressing Cu/Zn-SOD and catalase in combination or overexpressing Cu/Zn-SOD or catalase alone. The VSMC proliferation was measured by cell counting and bromodeoxyuridine incorporation assay. The MAPK phosphorylation was determined with Western blotting.
RESULTS: Treatment of wild-type VSMCs with EGF significantly increased proliferation and phosphorylation of extracellular signal-regulated kinases (ERK1/2) and p38 MAPK. Overexpression of Cu/Zn-SOD or catalase attenuated EGF-induced phosphorylation of ERK1/2 and p38 MAPK and suppressed EGF-induced proliferation in VSMCs. For example, the EGF-induced phosphorylation of ERK1/2 and p38 MAPK and EGF-induced proliferation in VSMCs overexpressing Cu/Zn-SOD or catalase were significantly less than in wild-type VSMCs. Moreover, VSMCs overexpressing Cu/Zn-SOD and catalase in combination showed significantly less proliferation and less phosphorylation of the MAPKs than those overexpressing Cu/Zn-SOD or catalase alone.
CONCLUSIONS: Overexpression of Cu/Zn-SOD and catalase in combination is more efficient in inhibiting VSMC proliferation and MAPK phosphorylation than overexpression of Cu/Zn-SOD or catalase alone.

Shi et al. Am J Hypertens. 2004 May;17(5 Pt 1):450-6.

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