Reductive Mobilization of Iron from Intact Ferritin: Mechanisms and Physiological Implication.

ABSTRACT: Ferritins are highly conserved supramolecular protein nanostructures composed of two different subunit types, H (heavy) and L (light). The two subunits co-assemble into a 24-subunit heteropolymer, with tissue specific distributions, to form shell-like protein structures within which thousands of iron atoms are stored as a soluble inorganic ferric iron core. In-vitro (or in cell free systems), the mechanisms of iron(II) oxidation and formation of the mineral core have been extensively investigated, although it is still unclear how iron is loaded into the protein in-vivo. In contrast, there is a wide spread belief that the major pathway of iron mobilization from ferritin involves a lysosomal proteolytic degradation of ferritin, and the dissolution of the iron mineral core. However, it is sti

SUBMITTER: Bou-Abdallah F 

PROVIDER: S-EPMC6315955 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature