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An estrogen inducible 104 kDa chaperone glycoprotein binds ferric iron containing proteins: a possible role in intracellular iron trafficking
Author(s) -
Poola Indra
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01183-6
Subject(s) - chaperone (clinical) , biochemistry , iron binding proteins , glycoprotein , protein subunit , chemistry , intracellular , ferritin , transferrin , ferric , binding protein , membrane protein , ferroportin , plasma protein binding , biology , membrane , gene , medicine , organic chemistry , pathology , iron homeostasis
We have previously described an estrogen inducible, intracellular, homodimeric membrane glycoprotein (subunit M r 104 kDa) which is structurally related to ‘chaperone’ proteins (Poola, I. and Kiang J.G., J. Biol. Chem. 269 (1994) 21762–21769). In this report we describe a novel finding that the 104 kDa chaperone protein exhibits affinity for iron containing proteins such as transferrins from several species, human lactoferrin and microbial ferric binding protein (FBP). A single ferric ion in the above proteins appears to be sufficient for binding. It also binds to immobilized ferritin. However, it does not exhibit any affinity for apotransferrins, apolactoferrin, apoferritin and apoFBP. This is the first report of a chaperone protein that exhibits affinity for iron containing proteins.