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. 2013 Mar;21(2):89–96. doi: 10.4062/biomolther.2013.015

Table 3.

GPx isoenzymes in mammalian cells

Type Structure Distribution Function

GPx1 (cytosolic GPx;cGPx) Homotetramer; contains a single selenocysteine residue in each of four identical subunits Abundant in cytosol of erythrocytes, kidney, liver or lung Selenium-dependent, Ubiquitously distributed (Chu et al., 2004)
GPx2 (gastrointestinal GPx; GI-GPx) Homotetramer; selenocysteine at active site 40 of the protein sequence Abundant in the epithelium of the whole gastrointestinal tract Selenium-dependent (Yan and Chen, 2006)
GPx3 (plasma/extracellualar GPx;pGPx) A glycosylated homotetramer of 23 kDa subunits The only extracellular isoform of GPxs; a secretrd protein into blood plasma; also expressed in the kidney, lung, heart, placenta Selenium-dependent, Extracellular peroxidase (Olson et al., 2010)
GPx4 (phospholipid hydro- peroxide GPx;PHGPx) Monomer; selenocysteine at active site 73) In most tissue both in cytosol and associated with membranes Selenium-dependent, protect phospholipid, inactive struc- tural capsule of epididymal spermatozoa (Imai and Nakagawa, 2003)
GPx5 (epididymal androgerelated protein or secretory GPx) 221 amino acids In epididymis; secreted protein. Selenium-independent (Vernet et al., 1999)