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Selenoprotein P. A selenium-rich extracellular glycoprotein
1Department of Medicine, Vanderbilt University School of Medicine, Nashville, TN 37232.
The Journal of Nutrition
|October 1, 1994
Summary
Selenoprotein P, a key selenium-carrying glycoprotein, is rapidly turned over in plasma and its levels decrease in selenium deficiency. This protein is proposed to function in extracellular oxidant defense, protecting against lipid peroxidation.
Area of Science:
- Biochemistry
- Molecular Biology
- Nutritional Science
Background:
- Selenoprotein P is a major selenium-binding glycoprotein found in plasma.
- Its concentration significantly decreases in selenium-deficient states.
- It contains multiple selenocysteine residues, crucial for its function.
Purpose of the Study:
- To characterize Selenoprotein P in rats and humans.
- To investigate its expression and regulation under selenium deficiency.
- To explore its potential role in extracellular oxidant defense.
Main Methods:
- Purification of Selenoprotein P from plasma.
- Biochemical analysis of selenium content.
- cDNA cloning and sequencing.
- Northern blot analysis of mRNA expression.
- Assessment of protection against diquat-induced toxicity.
Main Results:
- Selenoprotein P constitutes a large fraction of plasma selenium in replete rats.
- Its plasma concentration and half-life indicate rapid turnover.
- cDNA sequencing predicts 10 selenocysteine residues, though the protein appears modified.
- Selenoprotein P mRNA levels decrease in selenium deficiency, but less than glutathione peroxidase mRNA.
- Selenoprotein P presence correlates with protection against lipid peroxidation in deficient rats.
Conclusions:
- Selenoprotein P plays a significant role in selenium transport and metabolism.
- Its regulation is linked to selenium status, with distinct patterns compared to other selenoproteins.
- Evidence suggests Selenoprotein P functions as an extracellular antioxidant, protecting against oxidative damage.