Selenoproteins contain selenium in stoichiometric amounts. Most are synthes
ized by a process that decodes UGA codons as selenocysteine. Twelve animal
selenoproteins have been characterized, and biochemical functions have been
described for all but three. Two of these "orphan" selenoproteins are disc
ussed in this paper. Selenoprotein P is an extracellular glycoprotein that
contains multiple selenocysteines. It binds heparin and associates with end
othelial cells. Two isoforms have been identified. Plasma concentration of
selenoprotein P correlates with protection against diquat liver injury, sug
gesting that the protein protects against oxidant injury. Selenoprotein W i
s a small intracellular protein that contains one selenocysteine. It binds
glutathione and has been suggested to function in oxidant defense, The post
ulated oxidant defense properties of these selenoproteins are consistent wi
th the facile thiol-redox properties of selenocysteine. It can be predicted
that more proteins will be discovered that take advantage of the chemical
properties of selenium. BioEssays 21:231-237, 1999. (C) 1999 John Wiley & S
ons, Inc.