Regional localization of the human transferrin receptor gene to 3q26.2----qter

Lukas Kühn
1985
Journal paper

Transport of iron across the cell membrane is mediated by the iron-binding serum protein, transferrin, and its cell-surface receptor. Transferrin receptor is required for cell proliferation and may play a functional role in the pathogenesis of iron-storage disorders and some neoplasias. To better understand the possible involvement of transferrin receptor in such disorders, we have determined the chromosomal locus of the receptor gene by in situ hybridization. The human transferrin receptor gene was thus mapped to 3q26.2----qter, a region of chromosome 3 that appears to be involved in metal transport and that is subject to nonrandom structural rearrangements associated with neoplasia.

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Lukas Kühn
1985
Journal paper

Abstract

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https://infoscience.epfl.ch/record/117542?ln=en

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Post-transcriptional regulation of the transferrin receptor and 4F2 antigen heavy chain mRNA during growth activation of spleen cells

Lukas Kühn

The expression of several cell surface proteins including the transferrin receptor and 4F2 antigen is induced when quiescent cells are activated and proliferate. We have studied this induction in mouse spleen cells after stimulation with 4 beta-phorbol 12-myristate 13-acetate (PMA), the Ca(2+)-ionophore, ionomycin and recombinant interleukin-2 (IL-2). The 4F2 antigen heavy chain and transferrin receptor mRNA were barely detectable in resting cells, but increased 60-fold within 4 h of growth stimulation. The corresponding proteins became measurable at the cell surface after 6 h, prior to the S phase. In run-on transcription assays the transferrin receptor gene was transcribed to almost the same extent in resting and growth-stimulated cell populations and the 4F2 antigen heavy chain gene was induced fivefold. This suggests that post-transcriptional control mechanisms are mainly responsible for the accumulation of the respective mRNA at the onset of cell proliferation. In the case of the transferrin receptor, the induction correlated with an activation of the mRNA-binding iron-regulatory factor which is known to increase the stability of the cytoplasmic transferrin receptor mRNA.

1991

Noncoding 3' sequences of the transferrin receptor gene are required for mRNA regulation by iron

Lukas Kühn

The cell-surface receptor for transferrin mediates cellular uptake of iron from serum. Transferrin receptor protein and mRNA levels are increased in cells treated with iron chelating agents, and are decreased by treatment with iron salts or hemin. Here we report that expression of human transferrin receptor cDNA constructions in stably transfected mouse fibroblasts is regulated both by the iron chelator, desferrioxamine, and by hemin. We found that sequences within the 3' noncoding region are required for the iron-dependent feed-back regulation of receptor expression, whereas the presence of the transferrin receptor promoter region is not necessary. Regulation by iron is observed when transcription is initiated at either the SV-40 early promoter or the transferrin receptor promoter, but deletion of a 2.3 kb fragment within the 2.6 kb 3' noncoding region of the cDNA abolishes regulation and increases the constitutive level of receptor expression. Furthermore, the 3' deletion does not affect the decrease in receptors which is observed in response to growth arrest, indicating that transferrin receptor expression is controlled by at least two distinct mechanisms.

1987

Post-transcriptional regulation of transferrin receptor mRNA by IFN gamma

Lukas Kühn

IFN gamma inhibits the rise in transferrin receptor mRNA level which is normally observed when stationary WISH cells are stimulated to proliferate. This effect is not attributable to a change in the transcription rate of the transferrin receptor gene or in the cytoplasmic stability of the mRNA. The IFN gamma-induced reduction of the transferrin receptor mRNA content is already present at the nuclear level to an extent comparable to that observed in whole cells. Thus, IFN gamma does not impair the passage of this mRNA from the nuclear to the cytoplasmic compartment but probably interferes with a nuclear post-transcriptional event during the processing of the immature transferrin receptor mRNA. Two different levels of regulation of transferrin receptor mRNA have been previously reported. Iron modulates the cytoplasmic stability of this mRNA through the binding of a specific cytoplasmic factor, whereas cell growth variation influences the transcription of this gene. Our results suggest the existence of another mechanism of regulation for transferrin receptor gene expression not so far considered. Furthermore, the distinction between the mechanism of regulation exerted by IFN gamma and that exerted by cell proliferation on transferrin receptor gene expression suggests that, in WISH cells, the IFN-induced transferrin receptor decay is not a consequence of cell growth arrest but rather one of the causes of the antiproliferative effect of IFN through iron deprivation.

1992

Iron

Iron is a chemical element with the symbol Fe () and atomic number 26. It is a metal that belongs to the first transition series and group 8 of the periodic table. It is, by mass, the most common elem

Transferrin

Transferrins are glycoproteins found in vertebrates which bind and consequently mediate the transport of iron (Fe) through blood plasma. They are produced in the liver and contain binding sites for tw

Cell membrane

The cell membrane (also known as the plasma membrane or cytoplasmic membrane, and historically referred to as the plasmalemma) is a biological membrane that separates and protects the interior of a