Isolation and characterization of the transferrin receptor from human placenta.

Seligman, Paul A.; Schleicher, Roland; Allen, Robert H.

doi:10.1016/s0021-9258(19)86649-8

Cited by 201 publications

(25 citation statements)

References 14 publications

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“…The curve has a maximum at 185.9 kDa, with a standard error of 4.2 kDa (n = 121). This molecular mass corresponds perfectly with the published mass range for the human TfR dimer of 180-190 kDa [11,[26][27][28]. This experimentally derived number was used to interpret the broad peak displayed in Figure 2a.…”

Section: Stem Analysis Of Proteoparticlessupporting

confidence: 72%

“…(b) The left peak of (a) at a higher-resolution. The average molecular mass of the particles was determined to be 185.9 ± 4.2 kDa and corresponds perfectly to the published mass of the human TfR dimer [11,[26][27][28]. As a result of the membrane insertion, all receptor heads are locked at the same distance from the membrane but are free to rotate about their stalk.…”

Section: Molecular Dimensions Of the Human Tfr Dimersupporting

confidence: 66%

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Structural model of phospholipid-reconstituted human transferrin receptor derived by electron microscopy

et al. 1998

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Proteoparticles resemble TfR exosomes that are expelled by sheep reticulocytes upon maturation. The structure of proteoparticles in vitro is thus interpreted as being the result of the TfR's strong self-association potential, which might facilitate the endosomal sequestration of the TfR away from other membrane proteins and its subsequent return to the cell surface within tubular structures. The stalk is assumed to facilitate the tight packing of receptor molecules in coated pits and recycling tubuli.

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Section: Stem Analysis Of Proteoparticlessupporting

confidence: 72%

Section: Molecular Dimensions Of the Human Tfr Dimersupporting

confidence: 66%

Structural model of phospholipid-reconstituted human transferrin receptor derived by electron microscopy

et al. 1998

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“…It is one of many surface glycoprotein receptors that participate in the uptake of ligands from serum. TfR is a ubiquitous cell surface asialoglycoprotein (Mr -180,000) composed of two identical disulfide-linked subunits (Mr -90,000) (39,47,50). Its function is the uptake of iron from transferrin, the serum iron transport protein.…”

mentioning

confidence: 99%

Intracellular movement of cell surface receptors after endocytosis: resialylation of asialo-transferrin receptor in human erythroleukemia cells.

Snider¹,

Rogers²

1985

The Journal of Cell Biology

223

121

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The intracellular movement of cell surface transferrin receptor (TfR) after internalization was studied in K562 cultured human erythroleukemia cells. The sialic acid residues of the TfR glycoprotein were used to monitor transport to the Golgi complex, the site of sialyltransferases. Surface-labeled cells were treated with neuraminidase, and readdition of sialic acid residues, monitored by isoelectric focusing of immunoprecipitated TfR, was used to assess the movement of receptor to sialyltransferase-containing compartments. Asialo-TfR was resialylated by the cells with a half-time of 2-3 h. Resialylation occurred in an intracellular organelle, since it was inhibited by treatments that allow internalization of surface components but block transfer out of the endosomal compartment. Moreover, roughly half of the resialylated molecules were cleaved when cells were retreated with neuraminidase after culturing, indicating that this fraction of the molecules had returned to the cell surface. These results suggest that TfR is transported from the cell surface to the Golgi complex, the intracellular site of sialyltransferases, and then returns to the cell surface. This pathway, which has not been previously described for a cell surface receptor, may be different from the route followed by TfR in iron uptake, since reported rates of transferrin uptake and release are significantly more rapid than the resialylation of asialo-TfR.In recent years, it has become clear that plasma membrane proteins move into and out of cells. Membrane proteins are exchanged between the cell surface and intracellular organelles during the uptake of membrane by pinocytosis and phagocytosis and during the addition of membrane by the fusion of intracellular vesicles with the plasma membrane (for reviews, see references 7, 17, and 49). These processes have been studied extensively by microscopic and cell fractionation techniques. The movement of surface proteins into coated vesicles and endosomes during pinocytosis and into phagosomes and secondary lysosomes during phagocytosis have been described in studies that have used specific antibodies and ligands as probes. However, these noncovalently bound probes may not report accurately on the intracellular transport of surface proteins, since they may dissociate from their original binding sites after endocytosis. In addition, these techniques yield information about only the distribution of the probe at the moment the cells are examined.To overcome some of these problems, we are studying intracellular protein transport using covalent modifications of cell surface proteins as probes. This approach was inspired by the many studies that have followed the movement of newly made proteins through organelles of the secretory apparatus by analyzing the posttranslational modifications that occur in those organdies (24, 48). Our strategy involves making covalent alterations to cell surface components so that they become substrates for enzymes of known intracellular location. Movement of proteins to the...

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“…M. P. Galbraith et al, 1980b;Hamilton et al, 1979;Faulk et al, 1980) has been described. The apparent subunit molecular weight of Tf receptors isolated from human, rat and rabbit reticulocytes and human placental tissue has been reported to be 90000-95 000 (Leibman & Aisen, 1977;Sullivan & Weintraub, 1978;Hu & Aisen, 1978;Wada et al, 1979;Enns et al, 1981;Seligman et al, 1979), but Abbreviations used: Tf, transferrin; Tf(Fe)2, diferric transferrin; MEM, Eagle's minimal essential medium.…”

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confidence: 99%

Transferrin receptors of human fibroblasts. Analysis of receptor properties and regulation

Ward¹,

Kushner²,

Kaplan³

1982

Biochemical Journal

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Normal human skin fibroblasts cultured in vitro exhibit specific binding sites for 125I-labelled transferrin. Kinetic studies revealed a rate constant for association (Kon) at 37 degrees C of 1.03 X 10(7) M-1 X min-1. The rate constant for dissociation (Koff) at 37 degrees C was 7.9 X 10(-2) X min-1. The dissociation constant (KD) was 5.1 X 10(-9) M as determined by Scatchard analysis of binding and analysis of rate constants. Fibroblasts were capable of binding 3.9 X 10(5) molecules of transferrin per cell. Binding of 125I-labelled diferric transferrin to cells was inhibited equally by either apo-transferrin or diferric transferrin, but no inhibition was evident with apo-lactoferrin, iron-saturated lactoferrin, or albumin. Preincubation of cells with saturating levels of diferric transferrin or apo-transferrin produced no significant change in receptor number or affinity. Preincubation of cells with ferric ammonium citrate caused a time- and dose-dependent decrease in transferrin binding. After preincubation with ferric ammonium citrate for 72 h, diferric transferrin binding was 37.7% of control, but no change in receptor affinity was apparent by Scatchard analysis. These results suggest that fibroblast transferrin receptor number is modulated by intracellular iron content and not by ligand-receptor binding.

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Isolation and characterization of the transferrin receptor from human placenta.

Cited by 201 publications

References 14 publications

Structural model of phospholipid-reconstituted human transferrin receptor derived by electron microscopy

Structural model of phospholipid-reconstituted human transferrin receptor derived by electron microscopy

Intracellular movement of cell surface receptors after endocytosis: resialylation of asialo-transferrin receptor in human erythroleukemia cells.

Transferrin receptors of human fibroblasts. Analysis of receptor properties and regulation

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