The role of transferrin in the mechanism of cellular iron uptake

Abstract

INTRODUCTIONThe role of transferrin and its cell surface receptor in cellular iron metabolism has received considerable interest during the last decade. Hence, over this period several reviews covering various aspects of the topic have been published.In this review we attempt to summarize the new knowledge and controversies encountered during the last 4-5 years. The focus is on iron metabolism by the hepatocyte. We also view the concept of transferrin-cell interactions from angles which previously may not have been given particular attention, and we include some aspects of iron metabolism not normally covered by reviews of this type. Central parts of what may be regarded as well-established knowledge either have been entirely omitted, or are only briefly described or mentioned to the extent considered relevant to the particular topic discussed. Important aspects of iron metabolism such as iron adsorption, haemochromatosis, ferritin iron and iron in infection and neoplasia are not covered in the present paper. Instead, the reader is referred to one or more of the recently published reviews [1-5] and references therein.

Decay of Superoxide catalyzed by ferritin

“…bathophenanthroline disulphonic acid; BPS). The thermodynamic driving force introduced by the non-physiological chelator, may favour the formation of the Fe(II)chelator complex [11,12]. Therefore, one should be careful to interpret the pathophysiological significance of these studies.…”

Transferrin-functionalized nanoparticles lose their targeting capabilities when a biomolecule corona adsorbs on the surface

“…As an illustrative example, cancer cell metabolism of iron may lead to over-expression of transferrin receptor (TfR) 25 , making transferrin (Tf, a glycoprotein of 79 kDa that binds TfR at extracellular pH, K d = 1-100 nM) 26 , a potential targeting molecule. Previous investigations with Tf-targeted nanoparticles have, sometimes, appeared inconsistent, and problems such as linker stability and protein flexibility have been identified [27][28][29][30] .…”

Cloning, characterization, and modeling of a monoclonal anti‐human transferrin antibody that competes with the transferrin receptor

“…Although the mechanism of the Tf endocytic cycle, by which iron is carried into the cells, is well known (Thorstensen & Romslo, 1990), limited information is available concerning the interaction of Tf with its receptor (TR) and some epitopes on TR may play different biological roles besides binding of Tf (Keyna et al, 1991;Franco et al, 1992). Recent data show that the isolated C-terminal domain of human Tf is recognized by TR, even if both the C-and the N-terminal lobes contribute to the binding (Zak et al, 1994).…”