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from page 1)
ROLE OF SELENIUM
Oxidative damage caused
by free radicals results in many detrimental conditions including chronic
diseases. Selenium, an essential trace mineral that is part of antioxidant
enzymes, protects cells against the effects of free radicals. (1)
Adequate selenium status can protect molecules against oxidative and peroxidative
damage common in PLWHIV. (2) Selenium is also essential for normal
functioning of the body's immune system and thyroid gland.
Physiologically, selenium
(Se) functions in the form of selenoproteins, incorporating selenium as
selenocysteine. Numerous selenoproteins have been identified (Table
1). The total number in humans and higher animals may be as high as
30-50 units. (3, 4) Selenium's role in the enzyme glutathione peroxidase
was discovered in 1973. (5) Unlike zinc, selenium homeostasis is
not regulated by absorption. (4) Proteins containing selenomethionine
are digested in the human body and absorbed with the selenomethionine intact.
Selenomethionine is metabolized analogously to selenocysteine or can be
incorporated into selenoproteins that serve as unregulated storage forms
of selenium. (5)
SELENIUM AND THE IMMUNE
SYSTEM
Selenium is vital to cell-mediated
immunity and B-cell function. (5) The
body also needs adequate levels of selenium for T-cells, to function properly.
Various researchers who studied the relationship of trace elements and
the immune system associated abnormal copper, selenium or zinc levels with
immune dysfunction. (6-10) Along with zinc, HIV uses selenium in
viral proteins, creating a complex set of interactions between nutrient
levels, host requirements and viral utilization. (11) Taylor disclosed
that the use of zinc and selenium by the HIV virus might at least lead
to a localized intracellular depletion of these minerals. Although a deficiency
of selenium appears to be associated with HIV disease progression, selenium
supplementation inhibits the virus and may slow progression. (2)
| TABLE 1. SELECTED
SELENOPROTEINS IN MAMMALIAN TISSUES |
| Cellular or classical glutathione peroxidase
(GPX1) |
Iodothyronine 5-deiodinase-1 (DI1) |
|
|
| Gastrointestinal glutathione peroxidase (GPX2) |
Iodothyronine 5-deiodinase-2 (DI2) |
|
|
| Plasma (or extracellular) glutathione peroxidase
(GPX3) |
Iodothyronine 5-deiodination-3 (DI3) |
|
|
| Phospholipid hydroperoxide glutathione peroxidase
(GPX4) |
Muscle selenoprotein W (SELW) |
|
|
| Plasma selenoprotein P (SELP) |
Thioredoxin reductase-1 (TRR1) |
|
|
| 15-kDa selenoprotein (15kDa) |
Thioredoxin reductase-2 (TRR2) |
|
|
| Selenophosphate synthetase-2 (SPS2) |
Thioredoxin reductase-3 (TRR3) |
| Table adapted from: Sunde RA. Selenium. In:
Bowman BA, Russell RM, Editors. Present Knowledge in Nutrition, Eighth
edition. Washington, D.C: International Life Sciences Institute Press;
2001:352-365. |
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