Transferrin receptor: Its biological significance

May, Win; Cuatrecasas, Pedro

doi:10.1007/bf01871086

Cited by 163 publications

(68 citation statements)

References 153 publications

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“…Anti-TfR mAb at 300 µg was no more effective than 100 µg on days 0 and 1 (Table 2) [27]. Because TfR is found on a variety of cell types and tissues [2,16], administration of high doses of anti-TfR mAb had the potential to be toxic. No significant changes in body weight or hematocrits were detected after high doses of anti-TfR mAb (data not shown).…”

Section: Allograft Prolongation After Tfr Blockadementioning

confidence: 99%

“…Transferrin receptor (TfR), a 180-kDa disulfide-linked transmembrane glycoprotein, is a widely distributed cell surface receptor present on most proliferating and differentiated quiescent cells [1,2]. TfR expression is increased on rapidly proliferating cells, while expression is decreased or absent on non-dividing cells [2].…”

Section: Introductionmentioning

confidence: 99%

“…TfR expression is increased on rapidly proliferating cells, while expression is decreased or absent on non-dividing cells [2]. TfR binds the major serum iron transporter protein, transferrin, and controls iron uptake by receptormediated endocytosis [1][2][3]. TfR is not only an iron transporter but is also involved in T cell activation [3,4].…”

Section: Introductionmentioning

confidence: 99%

“…Only when the primary and costimulatory signals are received does this process lead to T cell proliferation, IL-2 production, and other effector functions [8,15]. After T cell activation, IL-2 receptor (IL-2R) [5,7] and TfR are upregulated [2,3]. The expression of IL-2 receptor is necessary for IL-2 to bind and assist in T cell activation [13].…”

Section: Introductionmentioning

confidence: 99%

“…The expression of IL-2 receptor is necessary for IL-2 to bind and assist in T cell activation [13]. The increased expression of TfR, which only appears after IL-2 receptor expression, is essential for the initiation of proliferation in quiescent T cells [2,16,17].…”

Section: Introductionmentioning

confidence: 99%

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Transferrin receptor in T cell activation and transplantation

Bayer

Baliga

Woodward

1998

Journal of Leukocyte Biology

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Transferrin receptor (TfR) expression is up-regulated during T cell activation after the interaction of the T cell receptor with the antigenmajor histocompatibility complex and the expression of interleukin-2 (IL-2) receptor. We hypothesize that anti-TfR monoclonal antibody (mAb) will prolong allograft survival by altering T cell responses. In a murine heterotopic nonvascularized cardiac allograft model, CBA/J (H-2 k ) recipients were transplanted with neonatal C57BL/6 (H-2 b ) donor hearts. Anti-TfR or isotype-matched control mAbs (100 g) were administered at the time of transplantation and on the following day. Splenocytes from naive CBA/J mice were stimulated in vitro with C57BL/6 alloantigen. Anti-TfR mAb was administered at 5 g/mL during the initiation of culture. Cytotoxic T lymphocyte (CTL) and mixed lymphocyte responses (MLR) were performed to assess T cell function. After 24 h in culture, cells were harvested, RNA isolated, and semi-quantitative reverse transcriptase-polymerase chain reaction performed. Anti-TfR mAb prolonged allograft survival to 25.7 ؎ 0.9 days compared to the isotype control (10.7 ؎ 0.4 days, P F 0.01, Wilcoxon rank sum). Anti-TfR mAb completely abrogated the CTL response and suppressed the MLR by 70-86% compared to the isotype controls. Anti-TfR mAb suppressed IL-2, interferon-␥ (IFN-␥), IL-10, and IL-12 p40 mRNA expression, but had no effect on IL-4, IL-12 p35, and IL-15 mRNA expression. In conclusion, anti-TfR mAb prolongs allograft survival, suppresses T cell function, and alters IL-2, IL-10, IL-12 p40, and IFN-␥ mRNA expression. These data suggest that the downregulation in IL-12 mRNA by anti-TfR mAb may prevent the development of T helper cells, thereby promoting graft survival and altering cell-mediated immune responses. The partial effect by anti-TfR mAb on cytokine mRNA expression may be due to other contributing factors such as costimulation.

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Section: Allograft Prolongation After Tfr Blockadementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Transferrin receptor in T cell activation and transplantation

Bayer

Baliga

Woodward

1998

Journal of Leukocyte Biology

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Distribution of transferrin binding protein immunoreactivity in the chicken central and peripheral nervous systems

et al. 1997

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Transferrin binding protein (TfBP) is a glycoprotein originally purified from chicken oviduct that exhibits transferrin binding activity. Recent work has shown that TfBP is a post-translationally modified form of the heat shock protein (HSP108), the avian homologue of a glucose regulated protein, GRP94. The function of this protein, however, has not yet been clearly defined. Antiserum to TfBP was found to selectively stain oligodendrocytes of the avian brain. In this study, we further describe these oligodendrocytes and other cell types positive to anti-TfBP in the chick nervous system. In accordance with previous studies, the most prominent cell type that labels with antiserum to TfBP is the oligodendrocyte. At the electron microscopic level, the immunoreactive product is confined to the perinuclear cytoplasm and fine processes of the oligodendrocytes, whereas myelin and axoplasm are devoid of staining. The immunoreactive product is found both in the cytoplasmic matrix and bound to the endoplasmic reticulum and plasma membrane, suggesting that TfBP may have properties of both a soluble and an integral membrane protein. There is great variability in the number of TfBP-oligodendrocytes in different areas of the central nervous system (CNS); large numbers of cells are associated with the white matter regions and are found in the myelinated tracts, whereas few cells are present in the gray matter regions. In the retina, TfBP is localized specifically in the cells, that are morphologically oligodendrocytic and is present in the optic nerve fiber layer and the ganglion cell layer. Obvious staining is also seen in the Bergmann glial cells of the cerebellum and in the Schwann cells of the sciatic nerve. Furthermore, the choroid plexus cells similarly exhibit a strong reaction. The association of TfBP in these specific cell types responsible for myelination and sequestering iron and transferrin implies that TfBP may be involved in myelination and iron metabolism of the chick nervous system, perhaps through a role in transferrin concentration in these cells. A putative role of TfBP, as HSP108, is considered.

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BiomimeticFe(II) Chemistry and Synthetic Studies on Antimalarial and Antitumour Endoperoxides

Chadwick

Rawe

2009

Patai's Chemistry of Functional Groups

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Introduction Endoperoxide‐Containing Antimalarials The Role of Iron The Biological Targets of Antimalarial Endoperoxides Semi‐Synthetic Artemisinin Derivatives Synthetic Endoperoxides Antimalarial Activities of Synthetic Endoperoxide Antimalarials Endoperoxide Containing Compounds with Antitumour Activity

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Transferrin receptor: Its biological significance

Cited by 163 publications

References 153 publications

Transferrin receptor in T cell activation and transplantation

Transferrin receptor in T cell activation and transplantation

Distribution of transferrin binding protein immunoreactivity in the chicken central and peripheral nervous systems

BiomimeticFe(II) Chemistry and Synthetic Studies on Antimalarial and Antitumour Endoperoxides

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