Relevant bibliographies by topics / Transferrin – Receptors

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Academic literature on the topic 'Transferrin – Receptors'

Author: Grafiati
Published: 4 June 2021
Last updated: 24 January 2023

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Journal articles on the topic "Transferrin – Receptors"

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Kawabata, Hiroshi. "Transferrin and transferrin receptors update." Free Radical Biology and Medicine 133 (March 2019): 46–54. http://dx.doi.org/10.1016/j.freeradbiomed.2018.06.037.

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Richard, Cyrielle, and Frédérique Verdier. "Transferrin Receptors in Erythropoiesis." International Journal of Molecular Sciences 21, no. 24 (December 19, 2020): 9713. http://dx.doi.org/10.3390/ijms21249713.

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Erythropoiesis is a highly dynamic process giving rise to red blood cells from hematopoietic stem cells present in the bone marrow. Red blood cells transport oxygen to tissues thanks to the hemoglobin comprised of α- and β-globin chains and of iron-containing hemes. Erythropoiesis is the most iron-consuming process to support hemoglobin production. Iron delivery is mediated via transferrin internalization by the endocytosis of transferrin receptor type 1 (TFR1), one of the most abundant membrane proteins of erythroblasts. A second transferrin receptor—TFR2—associates with the erythropoietin receptor and has been implicated in the regulation of erythropoiesis. In erythroblasts, both transferrin receptors adopt peculiarities such as an erythroid-specific regulation of TFR1 and a trafficking pathway reliant on TFR2 for iron. This review reports both trafficking and signaling functions of these receptors and reassesses the debated role of TFR2 in erythropoiesis in the light of recent findings. Potential therapeutic uses targeting the transferrin-TFR1 axis or TFR2 in hematological disorders are also discussed.
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Huebers, H. A., and C. A. Finch. "The physiology of transferrin and transferrin receptors." Physiological Reviews 67, no. 2 (April 1987): 520–82. http://dx.doi.org/10.1152/physrev.1987.67.2.520.

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FAST, Beate, Katrin KREMP, Michael BOSHART, and Dietmar STEVERDING. "Iron-dependent regulation of transferrin receptor expression in Trypanosoma brucei." Biochemical Journal 342, no. 3 (September 5, 1999): 691–96. http://dx.doi.org/10.1042/bj3420691.

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Transferrin is an essential growth factor for African trypanosomes. Here we show that expression of the trypanosomal transferrin receptor, which bears no structural similarity with mammalian transferrin receptors, is regulated by iron availability. Iron depletion of bloodstream forms of Trypanosoma brucei with the iron chelator deferoxamine resulted in a 3-fold up-regulation of the transferrin receptor and a 3-fold increase of the transferrin uptake rate. The abundance of expression site associated gene product 6 (ESAG6) mRNA, which encodes one of the two subunits of the trypanosome transferrin receptor, is regulated 5-fold by a post-transcriptional mechanism. In mammalian cells the stability of transferrin receptor mRNA is controlled by iron regulatory proteins (IRPs) binding to iron-responsive elements (IREs) in the 3′-untranslated region (UTR). Therefore, the role of a T. brucei cytoplasmic aconitase (TbACO) that is highly related to mammalian IRP-1 was investigated. Iron regulation of the transferrin receptor was found to be unaffected in δaco::NEO/δaco::HYG null mutants generated by targeted disruption of the TbACO gene. Thus, the mechanism of post-transcriptional transferrin receptor regulation in trypanosomes appears to be distinct from the IRE/IRP paradigm. The transferrin uptake rate was also increased when trypanosomes were transferred from medium supplemented with foetal bovine serum to medium supplemented with sera from other vertebrates. Due to varying binding affinities of the trypanosomal transferrin receptor for transferrins of different species, serum change can result in iron starvation. Thus, regulation of transferrin receptor expression may be a fast compensatory mechanism upon transmission of the parasite to a new host species.
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Moura, Ivan C., Olivier Hermine, Catherine Lacombe, and Patrick Mayeux. "Erythropoiesis and transferrin receptors." Current Opinion in Hematology 22, no. 3 (May 2015): 193–98. http://dx.doi.org/10.1097/moh.0000000000000133.

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Anderson, Gregory J., June W. Halliday, and Lawrie W. Powell. "Transferrin receptors in hemochromatosis." Hepatology 7, no. 5 (September 1987): 967–69. http://dx.doi.org/10.1002/hep.1840070529.

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Kuiper-Kramer, Ellen P. A., Jules L. L. M. Coenen, Carla M. S. Huisman, André Abbes, Jan van Raan, and Henk G. van Elsacker. "Relationship between Soluble Transferrin Receptors in Serum and Membrane-Bound Transferrin Receptors." Acta Haematologica 99, no. 1 (January 29, 1998): 8–11. http://dx.doi.org/10.1159/000040707.

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Hirata, T., P. B. Bitterman, J. F. Mornex, and R. G. Crystal. "Expression of the transferrin receptor gene during the process of mononuclear phagocyte maturation." Journal of Immunology 136, no. 4 (February 15, 1986): 1339–45. http://dx.doi.org/10.4049/jimmunol.136.4.1339.

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Abstract The expression of transferrin receptors by blood monocytes, human alveolar macrophages, and in vitro matured macrophages was evaluated by immunofluorescence, radioligand binding, and Northern analysis, using the monoclonal anti-human transferrin receptor antibody OKT9, [125I]-labeled human transferrin and a [32P]-labeled human transferrin receptor cDNA probe, respectively. By immunofluorescence, the majority of alveolar macrophages expressed transferrin receptors (86 +/- 3%). The radioligand binding assay demonstrated the affinity constant (Ka) of the alveolar macrophage transferrin receptor was 4.4 +/- 0.7 X 10(8) M-1, and the number of receptors per cell was 4.4 +/- 1.2 X 10(4). In marked contrast, transferrin receptors were not present on the surface or in the cytoplasm of blood monocytes, the precursors of the alveolar macrophages. However, when monocytes were cultured in vitro and allowed to mature, greater than 80% expressed transferrin receptors by day 6, and the receptors could be detected by day 3. Consistent with these observations, a transferrin receptor mRNA with a molecular size of 4.9 kb was demonstrated in alveolar macrophages and in vitro matured macrophages but not in blood monocytes. Thus, although blood monocytes do not express the transferrin receptor gene, it is expressed by mature macrophages, an event that probably occurs relatively early in the process of monocyte differentiation to macrophages.
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Cerneus, DP, GJ Strous, and A. van der Ende. "Bidirectional transcytosis determines the steady state distribution of the transferrin receptor at opposite plasma membrane domains of BeWo cells." Journal of Cell Biology 122, no. 6 (September 15, 1993): 1223–30. http://dx.doi.org/10.1083/jcb.122.6.1223.

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Trophoblast-like BeWo cells form well-polarized epithelial monolayers, when cultured on permeable supports. Contrary to other polarized cell systems, in which the transferrin receptor is found predominantly on the basolateral cell surface, BeWo cells express the transferrin receptor at both apical and basolateral cell surfaces (Cerneus, D.P., and A. van der Ende. 1991. J. Cell Biol. 114: 1149-1158). In the present study we have addressed the question whether BeWo cells use a different sorting mechanism to target transferrin receptors to the cell surface, by examining the biosynthetic and transcytotic pathways of the transferrin receptor in BeWo cells. Using trypsin and antibodies to detect transferrin receptors at the cell surface of filter-grown BeWo cells, we show that at least 80% of newly synthesized transferrin receptor follows a direct pathway to the basolateral surface, demonstrating that the transferrin receptor is efficiently intracellularly sorted. After surface arrival, pulse-labeled transferrin receptor equilibrates between apical and basolateral cell surfaces, due to ongoing transcytotic transport in both directions. The subsequent redistribution takes over 120 min and results in a steady state distribution with 1.5-2.0 times more transferrin receptors at the basolateral surface than at the apical surface. By monitoring the fate of surface-bound 125I-transferrin, internalized either from the apical or basolateral surface transcytosis of the transferrin receptor was studied. About 15% of 125I-transferrin is transcytosed in the basolateral to apical direction, whereas 25% is transcytosed in the opposite direction, indicated that the fraction of receptors involved in transcytosis is roughly twofold higher for the apical receptor pool, as compared to the basolateral pool. Upon internalization, both apical and basolateral receptor pools become redistributed on both surfaces, resulting in a twofold higher number of transferrin receptors at the basolateral surface. Our results indicate that in BeWo cells bidirectional transcytosis is the main factor in surface distribution of transferrin receptors on apical and basolateral surfaces, which may represent a cell type-specific, post-endocytic, sorting mechanism.
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Steinle, Alexander. "Transferrin‘ activation: Bonding with transferrin receptors tunes KLRG1 function." European Journal of Immunology 44, no. 6 (May 7, 2014): 1600–1603. http://dx.doi.org/10.1002/eji.201444670.

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Dissertations / Theses on the topic "Transferrin – Receptors"

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Lazarus, Alan H. "Involvement of transferrin receptors in human natural killer cell specificity." Thesis, McGill University, 1988. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=75860.

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Natural Killer (NK) cells are able to recognize and lyse tumor cells without prior immunization or sensitization. The initial events leading to target cell lysis by NK cells involves a poorly defined recognition and binding phase. It has been hypothesized however that human NK cells may recognize transferrin receptors as target structures on tumor cells.
To determine the possible involvement of transferrin receptors in human NK cell specificity, a correlation study between transferrin receptor expression and competitive activity for NK cell mediated lysis was undertaken. We have determined that the level of transferrin receptors expressed by different populations of K562 cells correlated well with their level of competitive activity for NK cell mediated lysis.
To investigate if these transferrin receptors could be recognized and bound by NK cells, a solid phase receptor binding assay was developed. As a model system, it was demonstrated that nitrocellulose immobilized transferrin retained its specific functional receptor binding capacity. This technique was quantitative and proved to be sufficiently sensitive to specifically detect nanogram quantities of transferrin receptor protein. Binding was assessed using an ELISA based system.
Human PBL were fractionated by discontinuous Percoll density centrifugation, bound to nitrocellulose, and evaluated for transferrin receptor binding capacity. A sample aliquot of cells from each Percoll fraction was retained to assess NK cell activity. It was observed that there was no positive relationship between NK cell activity and transferrin receptor binding capacity in these Percoll fractionated cells.
These findings indicate that while transferrin receptors may be involved in human NK cell specificity, they do not support a role for transferrin receptors in a high affinity mechanism between NK cells and tumor target cells.
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Cardoso, Aline Monticelli 1988. "Estudos sobre a internalização celular da STC1 humana." [s.n.], 2015. http://repositorio.unicamp.br/jspui/handle/REPOSIP/314360.

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Orientador: Jörg Kobarg
Dissertação (mestrado) - Universidade Estadual de Campinas, Instituto de Biologia
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Resumo: A Stanniocalcina-1 (STC1) humana é uma glicoproteína homóloga a Stanniocalcina (STC) originalmente identificada como um hormônio regulador da homeostase de cálcio em peixes. A STC1 humana secretada atua em diferentes processos fisiológicos incluindo a angiogênese, a hipóxia e, principalmente, a carcinogênese, demonstrando assim uma atividade abrangente. Atualmente não se conhece o receptor da STC1 e pouco se sabe sobre o mecanismo de ação e de entrada nas células dessa proteína. Assim, o objetivo desse trabalho foi investigar um candidato a receptor de membrana dessa proteína, o receptor de transferrina (TfR1), uma proteína transmembrana responsável pela absorção de ferro nas células. Esse receptor é provavelmente expresso por todas as células em diferentes níveis, em destaque em células do sistema hematopoiético, em células em divisão celular e células neoplásicas. Assim, avaliou-se por citometria de fluxo o efeito do tratamento com STC1 em células não transfectadas e células transfectadas superexpressando o receptor de transferrina. Células tratadas com STC1 demonstraram um efeito semelhante ao tratamento com transferrina, um conhecido ligante desse receptor, no qual ambos diminuíram o número de células positivas para a marcação da superfície com transferrina conjugada com fluorocromo (transferrina-Alexa Fluor® 488 - Life Technologies). Em outro conjunto de experimentos de Western Blot foi demonstrado que a STC1 adicionada no sobrenadante das culturas de células é internalizada nas células e detectável no lisado celular, principalmente as células transfectadas para a superexpressão do receptor de transferrina. Complementarmente, em experimentos de localização subcelular por imunofluorescência a STC1 foi detectada em uma forma pontual e espalhada no citoplasma. Em conjunto, todos esses experimentos sugerem que STC1 e transferrina interferem na localização do receptor de transferrina na superfície celular e que possivelmente esse receptor está envolvido em mecanismos de internalização da própria STC1
Abstract: Human Stanniocalcin 1 (STC1) is the mammalian homologue of STC, which was originally identified as a calcium-regulating hormone in bony fishes. The human secreted Stanniocalcin acts on different physiological processes, including angiogenesis, hypoxia and especially carcinogenesis, facts that demonstrate their activity is wide. Currently there are few data on the mechanism of action of this protein or how it enters the cell. Thus, the aim of this study was to investigate transferrin receptor (TfR1) as a candidate to membrane receptor protein of STC1. This receptor is a membrane protein responsible for the iron uptake in cells. This receptor is probably expressed by all cells especially by cells in division and cancer cells, but its expression level may vary. We evaluated by flow cytometry the effect of STC1 treatment in non-transfected cells and cell with TfR1 overexpression. The treatment with STC demonstrated a similar effect to treatment with transferrin, a known ligand for receptor, which decreased the number of positive cells for staining with fluorochrome (transferrin conjugated to Alexa Fluor® 488 - Life Technologies). We also demonstrated by Western Blot that STC1 added to the supernatant of cultures of cells, especially cells that overexpress transferrin receptor, is internalized into the cells and detectable in the cell lysate. Additionally, in subcellular localization experiments by immunofluorescence STC1 was detected in a timely manner and scattered in the cytoplasm. Together all this information suggests that STC1 and transferrin interferes with the localization of the transferrin receptor in the cellular surface and perhaps this receptor is involved in the mechanism of internalization of STC1
Mestrado
Bioquimica
Mestra em Biologia Funcional e Molecular
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Kim, Jonghan. "Pharmacokinetics and pharmacodynamics of protein turnover and production in vivo." Connect to this title online, 2004. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1100554543.

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Thesis (Ph. D.)--Ohio State University, 2004.
Title from first page of PDF file. Document formatted into pages; contains xxi, 203 p.; also includes graphics. Includes bibliographical references (p. 191-203).
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Hälldin, Jonas. "Oxidative stress and alterations in the mammalian iron metabolism : a study on iron, inflammation, oxidative stress and neurodegeneration in cellular model systems /." Stockholm : Department of Neurochemistry, Stockholm University, 2007. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-7037.

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Lazaron, Victor. "A Potential Role for the 70 kD Heat Shock Cognate Protein in Receptor Endocytosis." eScholarship@UMMS, 1996. http://escholarship.umassmed.edu/gsbs_diss/234.

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Nutrient and growth factor receptors internalize through dathrin coated pits. The signal sequences which mediate the association between receptors and the coated pit reside in receptor cytoplasmic tail domains. These signal sequences have been extensively investigated in nutrient receptors, and a minimal functional sequence has been identified consisting of a tyrosine residue in an exposed b turn. Protein-protein contacts between internalization signal sequences and components of the coated pit machinery have been proposed to mediate rapid internalization. In vitro evidence suggests the AP-2 adaptor may be that protein component. The signal sequences of growth factor receptors are less well understood. However, a growth factor- and temperature- dependent binding between the epideimal growth factor receptor and the AP-2 adaptor has been observed. We identified Hsc70 as a cytosolic ligand for the cytoplasmic tail of the transferrin receptor. The binding was mapped to the internalization signal sequence of the receptor tail. Mutations within the signal sequence which inhibit internalization result in alteration of signal sequence secondary structure and reduction in stimulation of the Hsc70 ATPase. Co-immunoprecipitation analysis showed a population of transferrin receptors which are bound to Hsc70, suggesting an association in vivo. We also showed binding of Hsc70 to the epidermal growth factor receptor by co-immunoprecipitation analysis. This binding was increased by treatment with EGF. The binding was transient, and occured prior to the binding of the receptor to AP-2 adaptors. Other agents which induce EGF receptor clustering and internalization also stimulate the transient increase in Hsc70 binding and the later AP-2 binding, suggesting a role in early endocytosis. These data support the hypothesis that Hsc70 is associated with the receptors for transferrin and epidermal growth factor in vitro and in vivo. We propose a role for the 70 kD heat shock protein in the assembly/disassembly of protein complexes involved in receptor signalling and/or internalization.
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Carvalho, Beatriz Assis. "Estado nutricional de ferro de lactentes atendidos em unidades básicas de saúde." Universidade Federal de Goiás, 2015. http://repositorio.bc.ufg.br/tede/handle/tede/4498.

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Conselho Nacional de Pesquisa e Desenvolvimento Científico e Tecnológico - CNPq
To evaluate the nutritional status of iron and its related factors in children 12 to 15 months assisted in Health Units in Goiânia, Goiás. METHODS: This is a cross-sectional study nested in research "Effectiveness of home fortification with vitamins and minerals in the prevention of iron deficiency and anemia in children under one year of age: a multicenter study in Brazilian cities ". The study was conducted with 230 children, aged between 12 and 15 months, assisted in Health Units in Goiânia, from June 2012 to February 2013. The prevalence of iron deficiency, iron deficiency anemia and anemia were assessed by the plasma means concentration of ferritin and transferrin receptor, hemoglobin and C-reactive protein. Multiple linear regression was used to estimate the effect of independent variables on the log plasma concentrations of ferritin. These variables were socioeconomic, demographic, maternal, pregnancy, anthropometric, breastfeeding, use of supplement, and biochemical parameters. RESULTS: Regarding the iron status, iron deficiency and iron deficiency anemia prevalence was 14.1% and 1.5%, respectively. Also, anemia prevalence was 5.6% of the infants studied. The predictors of ferritin were folate, vitamin B12 and the use of iron supplement at the time of collection, which each unit raised the log plasma concentration of ferritin in 0.009 mg/L, 0.001 mg/L and 0.315 mg/L, respectively. CONCLUSION: The results of this study showed low prevalence of iron deficiency and anemia in children studied. The use of iron supplements and serum concentrations of vitamin B12 and folate correlated ferritin concentrations and consequently the iron status in this population. Keywords: Iron Deficiency; Ferritins; Receptors, transferrin; Folic Acid; Vitamin B 12; Infant.
Avaliar o estado nutricional de ferro e os seus fatores relacionados em crianças de 12 a 15 meses atendidas em Unidades Básicas de Saúde de Goiânia, Goiás. MÉTODOS: Trata-se de um estudo transversal aninhado a pesquisa “Efetividade da fortificação caseira com vitaminas e minerais na prevenção da deficiência de ferro e anemia em crianças menores de um ano: estudo multicêntrico em cidades brasileiras”. O trabalho foi realizado com 230 crianças, de 12 e 15 meses, atendidas em Unidades Básicas de Saúde de Goiânia, no período de junho de 2012 a fevereiro de 2013. As prevalências de deficiência de ferro, anemia por deficiência de ferro e anemia foram avaliadas por meio da concentração plasmática de ferritina e receptor de transferrina, hemoglobina e proteína C-reativa. Foi utilizada regressão linear múltipla para estimar o efeito de variáveis independentes sobre o log das concentrações plasmáticas de ferritina. Estas variáveis foram condições socioeconômicas, demográficas, maternas, gestacionais, antropomêtricas, amamentação, uso de suplemento, e parâmetros bioquímicos. RESULTADOS: Com relação ao estado nutricional de ferro, as prevalências de deficiência de ferro e anemia por deficiência de ferro foram de 14,1% e 1,5% respectivamente. Além disso, foi encontrada prevalência de 5,6% de anemia nos lactentes estudados. Os fatores associados a ferritina foram o folato, a vitamina B12 e o uso de suplemento de ferro no momento da coleta, os quais cada unidade elevaram o log da concentração plasmática de ferritina em 0,009 μg/L, 0,001 μg/L e 0,315 μg/L, respectivamente. CONCLUSÃO: Os dados do presente estudo evidenciaram baixas prevalências de deficiência de ferro e anemia nas crianças estudadas. O uso de suplemento de ferro e as concentrações séricas das vitaminas B12 e folato correlacionaram-se as concentrações de ferritina e consequentemente, o estado nutricional de ferro nesta população.
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Thomas, Carla. "The validation and use of the rat intestinal epithelial cell line 6 (IEC-6) to study the role of ferroportin1 and divalent metal transporter 1 in the uptake of iron from Fe(II) and Fe(III)." University of Western Australia. Physiology Discipline Group, 2003. http://theses.library.uwa.edu.au/adt-WU2004.0019.

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[Formulae and special characters can only be approximated here. Please see the pdf version of the abstract for an accurate reproduction.] Iron is vital for almost all living organisms by participating in a wide variety of metabolic processes, including oxygen transport, DNA synthesis, and electron transport. However, iron concentrations in body tissues must be tightly regulated because excessive iron leads to tissue damage, as a result of formation of free radicals. In mammals since no controlled means of eliminating unwanted iron has evolved, body iron balance is maintained by alterations in dietary iron intake. This occurs in the duodenum where most dietary iron is absorbed. Absorption involves at least two steps, uptake of iron from the intestinal lumen and then its transport into the body, processes that occur at the apical and basal membranes of enterocytes, respectively. In chapter one of this thesis the background information relevant to iron absorption is described. Despite numerous studies, the role of these proteins in iron absorption remains unclear, partly because many studies have reported them in non-enterocyte cell lines where the expression of the proteins involved in iron absorption is unlikely and therefore the physiological significance of the findings uncertain. Therefore, the study of iron absorption would value from additional cell lines of intestinal origin being used, preferably derived from a species used to comprehensively study this process in vivo, namely the rat. Validation of such a model would enable comparisons to be made from a molecular level to its relevance in the whole organism. In chapter 3 of this thesis, the rat intestinal cell line 6 (IEC-6) was examined as a model of intestinal iron transport. IEC-6 cells expressed many of the proteins involved in iron absorption, but not the ferrireductase Dcytb, sucrase or αvβ3 integrin. In addition, in IEC-6 cells the expression of the apical transporter divalent metal transporter 1 (DMT1), the iron storage protein ferritin, the uptake of Fe(II) and Fe(III) were regulated by cellular iron stores as is seen in vivo. This suggests that IEC-6 cells are of a lower villus enterocyte phenotype. Presented in chapter 4 is the study of the uptake of iron from Fe(II):ascorbate and Fe(III):citrate by IEC-6 cells in the presence of a blocking antibody to the putative basolateral transporter ferroportin1 and of colchicine and vinblastine, different pHs, and over-expression of DMT1. It was shown that optimal Fe(II) uptake required a low extracellular pH and was dependent on DMT1. Uptake of Fe(III) functioned optimally at a neutral pH, did not require surface ferrireduction, and was increased during over-expression of DMT1. These observations suggest that intravesicular ferrireduction takes place before transport of Fe(II) to the cytoplasm by DMT1. This pathway was not blocked by a functional antibody against αvβ3 integrin but was inhibited by competition with unlabeled iron citrate or citrate alone. Surprisingly, a functional antibody against ferroportin1 had no effect on efflux but significantly reduced (p<0.05) uptake of Fe(II) by 40-50% and Fe(III) by 90%, indicating two separate pathways for the uptake of iron from Fe(II)-ascorbate and from Fe(III)-citrate in IEC-6 cells. Presented in chapter 5 is the development and validation of a technique for the removal of freshly isolated enterocytes from the rat duodenum and their use to study iron transport processes that enabled comparisons to be made between these cells, IEC-6 cells and the human enterocyte cell line Caco-2 cells. In chapter 6 a blocking antibody to ferroportin1 was shown to inhibit uptake of Fe(II) but not release of iron in freshly isolated duodenal enterocytes from rats and Caco-2 cells supporting the findings obtained with IEC-6 cells described in chapter 4. Fe(II) uptake was reduced only when the antibody was in contact with the apical membrane indicating its expression at the microvillus membrane. Confirming this, ferroportin1 was shown along the microvillus membrane of Caco-2 cells, in enriched microvillus membrane preparations and in enterocytes of duodenum tissue of rats where it co-localised with lactase. The significant findings to emerge from this thesis are that the IEC-6 cell is a valid model to study iron absorption producing results consistent with those found in freshly isolated enterocytes and in human enterocyte-like cells. In particular, ferroportin1 functions in the uptake of iron at the apical membrane possibly by modulating surface binding of Fe(II) to DMT1 or the activity of DMT1. In addition to this in Fe(II) uptake from Fe(III) ferroportin1 may also affect the number of Fe(III): citrate binding sites. Preliminary studies further characterizing the function of ferroportin1 at the apical membrane and at intracellular sites of IEC-6 cells along with integration of these data are discussed in chapter 7.
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Navaroli, Deanna M. "Molecular Mechanisms of Endocytosis: Trafficking and Functional Requirements for the Transferrin Receptor, Small Interfering RNAs and Dopamine Transporter: A Dissertation." eScholarship@UMMS, 2004. http://escholarship.umassmed.edu/gsbs_diss/592.

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Endocytosis is an essential function of eukaryotic cells, providing crucial nutrients and playing key roles in interactions of the plasma membrane with the environment. The classical view of the endocytic pathway, where vesicles from the plasma membrane fuse with a homogenous population of early endosomes from which cargo is sorted, has recently been challenged by the finding of multiple subpopulations of endosomes. These subpopulations vary in their content of phosphatidylinositol 3- phosphate (PI3P) and Rab binding proteins. The role of these endosomal subpopulations is unclear, as is the role of multiple PI3P effectors, which are ubiquitously expressed and highly conserved. One possibility is that the different subpopulations represent stages in the maturation of the endocytic pathway. Alternatively, endosome subpopulations may be specialized for different functions, such as preferential trafficking of specific endocytosed cargo. To determine whether specific receptors are targeted to distinct populations of endosomes, we have built a platform for total internal reflection fluorescence (TIRF) microscopy coupled with structured illumination capabilities named TESM (TIRF Epifluorescence Structured light Microscope.) In this study, TESM, along with standard biochemical and molecular biological tools, was used to analyze the dynamic distribution of two highly conserved Rab5 and PI3P effectors, EEA1 and Rabenosyn-5, and systematically study the trafficking of transferrin. Rabenosyn-5 is necessary for proper expression of the transferrin receptor as well as internalization and recycling of transferrin-transferrin receptor complexes. Results of combining TIRF with structured light Epifluorescence (SLE) indicate that the endogenous populations of EEA1 and Rabenoysn-5 are both distinct and partially overlapping. The application of antisense oligonucleotides as potential therapeutic agents requires effective methods for their delivery to the cytoplasm of target cells. In collaboration with RXi Pharmaceuticals we show the efficient cellular uptake of the antisense oligonucleotide sd-rxRNA® in the absence of delivery vehicle or protein carrier. In this study TIRF, SLE, and biochemical approaches were utilized to determine whether sd-rxRNA traffics and functions along specific endosomal pathways. Sd-rxRNA was found to traffic along the degradative pathway and require EEA1 to functionally silence its target. These new findings will help define the cellular pathways involved in RNA silencing. Neurotransmitter reuptake and reuse by neurotransmitter transport proteins is fundamental to transmitter homeostasis and synaptic signaling. In order to understand how trafficking regulates transporters in the brain and how this system may be disregulated in monoamine-related pathologies, the transporter internalization signals and their molecular partners must be defined. We utilized a yeast two-hybrid system to identify proteins that interact with the dopamine transporter (DAT) endocytic signal. The small, membrane associated, GTPase Rin was determined to specifically and functionally interact with the DAT endocytic signal, regulating constitutive and protein kinase C (PKC) – stimulated DAT endocytosis. The results presented in this study provide new insights into functions and components of endocytosis and enhance the understanding of endocytic organization.
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Navaroli, Deanna M. "Molecular Mechanisms of Endocytosis: Trafficking and Functional Requirements for the Transferrin Receptor, Small Interfering RNAs and Dopamine Transporter: A Dissertation." eScholarship@UMMS, 2012. https://escholarship.umassmed.edu/gsbs_diss/592.

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Endocytosis is an essential function of eukaryotic cells, providing crucial nutrients and playing key roles in interactions of the plasma membrane with the environment. The classical view of the endocytic pathway, where vesicles from the plasma membrane fuse with a homogenous population of early endosomes from which cargo is sorted, has recently been challenged by the finding of multiple subpopulations of endosomes. These subpopulations vary in their content of phosphatidylinositol 3- phosphate (PI3P) and Rab binding proteins. The role of these endosomal subpopulations is unclear, as is the role of multiple PI3P effectors, which are ubiquitously expressed and highly conserved. One possibility is that the different subpopulations represent stages in the maturation of the endocytic pathway. Alternatively, endosome subpopulations may be specialized for different functions, such as preferential trafficking of specific endocytosed cargo. To determine whether specific receptors are targeted to distinct populations of endosomes, we have built a platform for total internal reflection fluorescence (TIRF) microscopy coupled with structured illumination capabilities named TESM (TIRF Epifluorescence Structured light Microscope.) In this study, TESM, along with standard biochemical and molecular biological tools, was used to analyze the dynamic distribution of two highly conserved Rab5 and PI3P effectors, EEA1 and Rabenosyn-5, and systematically study the trafficking of transferrin. Rabenosyn-5 is necessary for proper expression of the transferrin receptor as well as internalization and recycling of transferrin-transferrin receptor complexes. Results of combining TIRF with structured light Epifluorescence (SLE) indicate that the endogenous populations of EEA1 and Rabenoysn-5 are both distinct and partially overlapping. The application of antisense oligonucleotides as potential therapeutic agents requires effective methods for their delivery to the cytoplasm of target cells. In collaboration with RXi Pharmaceuticals we show the efficient cellular uptake of the antisense oligonucleotide sd-rxRNA® in the absence of delivery vehicle or protein carrier. In this study TIRF, SLE, and biochemical approaches were utilized to determine whether sd-rxRNA traffics and functions along specific endosomal pathways. Sd-rxRNA was found to traffic along the degradative pathway and require EEA1 to functionally silence its target. These new findings will help define the cellular pathways involved in RNA silencing. Neurotransmitter reuptake and reuse by neurotransmitter transport proteins is fundamental to transmitter homeostasis and synaptic signaling. In order to understand how trafficking regulates transporters in the brain and how this system may be disregulated in monoamine-related pathologies, the transporter internalization signals and their molecular partners must be defined. We utilized a yeast two-hybrid system to identify proteins that interact with the dopamine transporter (DAT) endocytic signal. The small, membrane associated, GTPase Rin was determined to specifically and functionally interact with the DAT endocytic signal, regulating constitutive and protein kinase C (PKC) – stimulated DAT endocytosis. The results presented in this study provide new insights into functions and components of endocytosis and enhance the understanding of endocytic organization.
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Fouquet, Guillemette. "Régulation de l’érythropoïèse : rôle des récepteurs à la transferrine et d’un phytoestrogène." Thesis, Université Paris-Saclay (ComUE), 2019. http://www.theses.fr/2019SACLS293.

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L’érythropoïèse est un processus extrêmement prolifératif, et qui doit donc être très étroitement régulé. L’érythropoïétine (EPO) est l’un des facteurs absolument nécessaires à l’érythropoïèse. Cependant, dans la moelle osseuse, la quantité d'EPO circulante est sous-optimale et la capacité des érythroblastes à survivre dépend donc de leur sensibilité à l'EPO. Les facteurs modulant la réponse à l'EPO au cours de l'érythropoïèse sont encore largement inconnus.Nous avons donc voulu explorer plusieurs facteurs pouvant potentiellement être impliqués dans la régulation de l’érythropoïèse et plus précisément dans la réponse à l’EPO : tout d’abord, la transferrine ainsi que ses récepteurs (TfR), la transferrine et le TfR1 étant également essentiels à l’érythropoïèse, ainsi qu’un phytoestrogène provenant d’une plante nommée Curcuma comosa, les oestrogènes étant eux aussi connus pour favoriser l’érythropoïèse.Concernant la transferrine, nous avons voulu principalement explorer son rôle sur la signalisation, ayant récemment montré au laboratoire que le TfR1, essentiellement connu pour son rôle dans l’endocytose du fer, est également capable d’entraîner une signalisation.Nous avons montré que la transferrine potentialise la stimulation induite par l’EPO des voies ERK, AKT et STAT5. Cet effet est conservé même en l’absence d’endocytose du TfR1. Aucune coopération n’a été trouvée entre la transferrine et le stem cell factor (SCF).Nous avons également observé qu’en l’absence du TfR2, il existe une augmentation de l’expression de l’EPO-R et de la signalisation induite par l’EPO, sans impact de la transferrine dans ce contexte. Par ailleurs, nous avons montré que le Curcuma comosa améliore la prolifération et la différenciation des progéniteurs érythroïdes précoces, par un mécanisme de potentialisation de la signalisation induite par l’EPO impliquant le récepteur aux oestrogènes ER-α.En conclusion, la transferrine et ses récepteurs, ainsi qu’un phytoestrogène et l’ER-α, sont impliqués dans la régulation de l’érythropoïèse via leur action sur la signalisation induite par l’EPO. L’approfondissement de ces données pourrait ouvrir de nouvelles pistes thérapeutiques dans le traitement de l’anémie
Erythropoiesis is an extremely proliferative process and must be very closely regulated. Erythropoietin (EPO) is one of the major factors necessary for erythropoiesis. However, in the bone marrow, the amount of circulating EPO is suboptimal and the ability of erythroblasts to survive therefore depends on their sensitivity to EPO. The factors modulating the response to EPO during erythropoiesis are still largely unknown. We therefore wanted to explore several factors that could potentially be involved in the regulation of erythropoiesis and more specifically in the response to EPO: first, transferrin and its receptors (TfR), transferrin and TfR1 being also essential for erythropoiesis, as well as a phytoestrogen from a plant called Curcuma comosa, as estrogens are also known to promote erythropoiesis. Regarding transferrin, we mainly wanted to explore its role on signaling, having recently shown in the laboratory that TfR1, essentially known for its role in iron endocytosis, is a signaling-competent receptor. We have shown that transferrin potentiates EPO-induced stimulation of the ERK, AKT and STAT5 pathways. This effect is maintained even in the absence of TfR1 endocytosis. No cooperation was found between transferrin and stem cell factor (SCF). We also observed that in the absence of TfR2, there is an increase in EPO-R expression and EPO-induced signaling, without any impact of transferrin in this context.In addition, we have shown that Curcuma comosa improves the proliferation and differentiation of early erythroid progenitors through a mechanism involving the ER-α estrogen receptor, able to potentiate EPO-induced signaling. In conclusion, transferrin and its receptors, as well as a phytoestrogen and ER-α, are involved in the regulation of erythropoiesis through their action on EPO-induced signaling. Further investigation of these data could provide new therapeutic strategies in the treatment of anemia
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Books on the topic "Transferrin – Receptors"

1

Proteins of iron metabolism. Boca Raton, Fla: CRC Press, 2002.

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Khesaifan, Mahler M. K. Transferrin and haemopoietic growth factor receptors on the human leukaemia U937 cell line: Observation by confocal microscopy. [S.l: The Author], 1994.

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Papatheodorou, Panagiotis. Clostridium difficile binary toxin CDT induces clustering of the lipolysis-stimulated lipoprotein receptor into lipid rafts. Freiburg: Universität, 2013.

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Cooper, Marcia Janet. Biological and analytical variability of repeated transferrin receptor and ferritin measurements. Ottawa: National Library of Canada, 1995.

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Beauchamp, James Richard. Control of clathrin-mediated endocytosis and transferrin receptor recycling by protein phosphorylation. Manchester: University of Manchester, 1996.

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Coppolino, Marc Gabriel. Identification of a convalent association between transferrin receptor and integrin gasb3s. Ottawa: National Library of Canada, 1993.

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Salmon, Michael. Transferrin receptor bearing cells in rheumatoid arthritis and an in vitro model of lymphocyte activation. Birmingham: University of Birmingham, 1986.

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Proteins of Iron Metabolism. Taylor & Francis Group, 2019.

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Testa, Ugo. Proteins of Iron Metabolism. Taylor & Francis Group, 2001.

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Testa, Ugo. Proteins of Iron Metabolism. Taylor & Francis Group, 2001.

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Book chapters on the topic "Transferrin – Receptors"

1

de los Monteros, Araceli Espinosa, and Jean de Vellis. "Transferrin and the Developing Nervous System." In Receptors in the Developing Nervous System, 63–81. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-1540-7_4.

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Cook, James D., Roy D. Baynes, and Barry S. Skikne. "The Physiological Significance of Circulating Transferrin Receptors." In Advances in Experimental Medicine and Biology, 119–26. Boston, MA: Springer US, 1994. http://dx.doi.org/10.1007/978-1-4899-2575-6_9.

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Moos, T., and T. M. Hansen. "Intracerebral Expression of Transferrin Receptors in Iron-Deficient Rats." In Biology and Physiology of the Blood-Brain Barrier, 55–61. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4757-9489-2_11.

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Vannelli, G. B., T. Barni, C. Orlando, A. Natali, M. Serio, and G. C. Balboni. "Localization of transferrin and somatomedin-C receptors in human seminiferous epithelium." In Morphological Basis of Human Reproductive Function, 49–54. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1953-5_8.

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Sigman, M., and B. Lönnerdal. "Transferrin Receptors and Iron Uptake of Rat Mammary Gland Membranes during Lactation." In Trace Elements in Man and Animals 6, 433–34. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-0723-5_150.

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Raivich, G., M. Graeber, J. Gehrmann, M. T. Moreno-Flores, and G. W. Kreutzberg. "Regulation of Transferrin Receptors and Iron Uptake in Normal and Injured Nervous System." In The Facial Nerve, 51–54. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-85090-5_13.

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Trowbridge, Ian S. "Transferrin Receptor." In Hybridoma Technology in the Biosciences and Medicine, 177–89. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-4964-8_10.

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Schryvers, A. B., S. W. Irwin, M. J. Middelveen, J. A. Ogunnariwo, and J. Alcantara. "Iron Acquisition in Neisseria: Bacterial Receptors for Human Transferrin and Human Lactoferrin in Neisseria meningitidis." In Neisseriae 1990, edited by Mark Achtman, Peter Kohl, Christian Marchal, Giovanna Morelli, Andrea Seiler, and Burghard Thiesen, 481–86. Berlin, Boston: De Gruyter, 1991. http://dx.doi.org/10.1515/9783110867787-085.

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Joshi, Harsh A., Esha S. Attar, Prajakta Dandekar, and Padma V. Devarajan. "Transferrin Receptor and Targeting Strategies." In Targeted Intracellular Drug Delivery by Receptor Mediated Endocytosis, 457–80. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-29168-6_16.

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Bjerner, J., L. M. Amlie, L. S. Rusten, and E. Jakobsen. "Serum Levels Of Soluble Transferrin Receptors (STFR) Correlate Better With Severity Of Disease Than With Iron Stores In Patients With Malignant Lymphomas." In Advances in Critical Care Testing, 119. Berlin, Heidelberg: Springer Berlin Heidelberg, 2004. http://dx.doi.org/10.1007/978-3-642-18480-2_13.

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Conference papers on the topic "Transferrin – Receptors"

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Wallrabe, Horst, Ammasi Periasamy, Ronak Talati, Christine Kim, and Margarida Barroso. "Confocal FRET and FLIM microscopy to characterize the distribution of transferrin receptors in membranes." In Biomedical Optics 2006, edited by Ammasi Periasamy and Peter T. C. So. SPIE, 2006. http://dx.doi.org/10.1117/12.661760.

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Kindrat, Iryna, Volodymyr Tryndyak, Aline de Conti, Svitlana Shpyleva, Anna Erstenyuk, Frederick A. Beland, and Igor Pogribny. "Abstract 920: Mechanism of the transferrin receptor 1 dysregulation in hepatocarcinogenesis." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-920.

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Shigeta, Shogo, Masafumi Toyoshima, Kazuyuki Kitatani, Masumi Ishibashi, Toshinori Usui, and Nobuo Yaegashi. "Abstract A13: Transferrin facilitates the formation of DNA-double strand breaks via transferrin receptor 1 in fallopian tube epithelial cells." In Abstracts: AACR Special Conference: Advances in Ovarian Cancer Research: Exploiting Vulnerabilities; October 17-20, 2015; Orlando, FL. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1557-3265.ovca15-a13.

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Lima, Rennan Ribeiro Mano de, Maria Isabela de Andrade Pereira, Rafaella Bezerra de Lima Henrique, Beate Saegesser Santos, Goreti Pereira Pereira, and Adriana Fontes. "SISTEMAS MULTIMODAIS ÓPTICO-PARAMAGNÉTICOS PARA O ESTUDO DE RECEPTORES DE TRANSFERRINA." In Encontro Anual da biofisica 2019. São Paulo: Editora Blucher, 2019. http://dx.doi.org/10.5151/biofisica2019-84.

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Xue, Xiang, and Hyeoncheol Kim. "IDDF2022-ABS-0024 Transferrin receptor-mediated iron uptake is essential for colon tumorigenesis." In Abstracts of the International Digestive Disease Forum (IDDF), Hong Kong, 2–4 September 2022. BMJ Publishing Group Ltd and British Society of Gastroenterology, 2022. http://dx.doi.org/10.1136/gutjnl-2022-iddf.33.

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Nicholson, RI, HO Habashy, JM Gee, P. Finlay, L. Farrow, B. Jasani, P. Barrett-Lee, JF Robertson, and IO Ellis. "Abstract P2-06-19: Transferrin Receptor (CD71) Identifies Poor Response to Tamoxifen in Oestrogen Receptor Positive Breast Cancer Patients." In Abstracts: Thirty-Third Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 8‐12, 2010; San Antonio, TX. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/0008-5472.sabcs10-p2-06-19.

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McDonald, Michael A., Tighe A. Spurlin, Alessandro Tona, John T. Elliott, Michael Halter, and Anne L. Plant. "Transferrin protein nanospheres: a nanoplatform for receptor-mediated cancer cell labeling and gene delivery." In BiOS, edited by Samuel Achilefu and Ramesh Raghavachari. SPIE, 2010. http://dx.doi.org/10.1117/12.842757.

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Fegan, Jamie, Epshita Islam, Charles Calmettes, Rong-Hua Yu, Steven Ahn, Trevor Moraes, Anthony Schryvers, and Scott Gray-Owen. "O01.3 Engineering hybrid bacterial transferrin receptor-based vaccines to confer broad protection againstneisseria gonorrhoeae." In Abstracts for the STI & HIV World Congress (Joint Meeting of the 23rd ISSTDR and 20th IUSTI), July 14–17, 2019, Vancouver, Canada. BMJ Publishing Group Ltd, 2019. http://dx.doi.org/10.1136/sextrans-2019-sti.106.

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Pillar, A., A. Brown, J. Mayall, J. Weaver, A. Essilfie, G. Hoefel, M. K. Ali, et al. "Relationship between interleukin-13 and transferrin receptor-1 responses in the pathogenesis of asthma." In ERS International Congress 2022 abstracts. European Respiratory Society, 2022. http://dx.doi.org/10.1183/13993003.congress-2022.4211.

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Cabral Filho, Paulo E. "SONDAS MULTIMODAIS FLUORESCENTE-MAGNÉTICAS PARA MARCAÇÃO DO RECEPTOR DE TRANSFERRINA EM CÉLULAS CANCERÍGENAS." In Encontro Anual da Biofísica 2017. São Paulo: Editora Blucher, 2017. http://dx.doi.org/10.5151/biofisica2017-041.

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Reports on the topic "Transferrin – Receptors"

1

Coplin, David, Isaac Barash, and Shulamit Manulis. Role of Proteins Secreted by the Hrp-Pathways of Erwinia stewartii and E. herbicola pv. gypsophilae in Eliciting Water-Soaking Symptoms and Initiating Galls. United States Department of Agriculture, June 2001. http://dx.doi.org/10.32747/2001.7580675.bard.

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Many bacterial pathogens of plants can inject pathogenicity proteins into host cells using a specialized type III secretion system encoded by hrpgenes. This system deliver effector proteins, into plant cells that function in both susceptible and resistant interactions. We have found that the virulence of Erwinia stewartii(Es; syn. Pantoea stewartii) and Erwinia herbicola pv. gypsophilae (Ehg, syn. Pantoea agglomerans), which cause Stewart's wilt of corn and galls on Gypsophila, respectively, depends on hrpgenes. The major objectives of this project were: To increase expression of hrpgenes in order to identify secreted proteins; to identify genes for proteins secreted by the type-III systems and determine if they are required for pathogenicity; and to determine if the secreted proteins can function within eukaryotic cells. We found that transcription of the hrp and effector genes in Es and Ehg is controlled by at least four genes that constitute a regulatory cascade. Environmental and/or physiological signaling appears to be mediated by the HrpX/HrpY two component system, with HrpX functioning as a sensor-kinase and HrpY as a response regulator. HrpYupregulateshrpS, which encodes a transcriptional enhancer. HrpS then activates hrpL, which encodes an alternate sigma factor that recognizes "hrp boxes". All of the regulatory genes are essential for pathogenicity, except HrpX, which appears only to be required for induction of the HR in tobacco by Es. In elucidating this regulatory pathway in both species, we made a number of significant new discoveries. HrpX is unusual for a sensor-kinase because it is cytoplasmic and contains PAS domains, which may sense the redox state of the bacterium. In Es, a novel methyl-accepting protein may function upstream of hrpY and repress hrp gene expression in planta. The esaIR quorum sensing system in Es represses hrp gene expression in Es in response to cell-density. We have discovered six new type III effector proteins in these species, one of which (DspE in Ehg and WtsE in Es) is common to both pathogens. In addition, Es wtsG, which is a homolog of an avrPpiB from P. syringae pv. pisi, and an Ehg ORF, which is a homolog of P. syringae pv. phaseolicola AvrPphD, were both demonstrated to encode virulence proteins. Two plasmidborne, Ehg Hop proteins, HsvG and PthG, are required for infection of gypsophilia, but interestingly, PthG also acts as an Avr elicitor in beets. Using a calmodulin-dependent adenylate cyclase (cyaA) reporter gene, we were successful in demonstrating that an HsvG-CyaA fusion protein can be transferred into human HeLa cells by the type-III system of enteropathogenic E. coli. This is a highly significant accomplishment because it is the first direct demonstration that an effector protein from a plant pathogenic bacterium is capable of being translocated into a eukaryotic cell by a type-III secretion system. Ehg is considered a limiting factor in Gypsophila production in Israel and Stewart’s Wilt is a serious disease in the Eastern and North Central USA, especially on sweet corn in epidemic years. We believe that our basic research on the characterization of type III virulence effectors should enable future identification of their receptors in plant cells. This may lead to novel approaches for genetically engineering resistant plants by modifying their receptors or inactivating effectors and thus blocking the induction of the susceptible response. Alternatively, hrp gene regulation might also provide a target for plant produced compounds that interfere with recognition of the host by the pathogen. Such strategies would be broadly applicable to a wide range of serious bacterial diseases on many crops throughout the USA and Israel.
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Tzfira, Tzvi, Michael Elbaum, and Sharon Wolf. DNA transfer by Agrobacterium: a cooperative interaction of ssDNA, virulence proteins, and plant host factors. United States Department of Agriculture, December 2005. http://dx.doi.org/10.32747/2005.7695881.bard.

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Agrobacteriumtumefaciensmediates genetic transformation of plants. The possibility of exchanging the natural genes for other DNA has led to Agrobacterium’s emergence as the primary vector for genetic modification of plants. The similarity among eukaryotic mechanisms of nuclear import also suggests use of its active elements as media for non-viral genetic therapy in animals. These considerations motivate the present study of the process that carries DNA of bacterial origin into the host nucleus. The infective pathway of Agrobacterium involves excision of a single-stranded DNA molecule (T-strand) from the bacterial tumor-inducing plasmid. This transferred DNA (T-DNA) travels to the host cell cytoplasm along with two virulence proteins, VirD2 and VirE2, through a specific bacteriumplant channel(s). Little is known about the precise structure and composition of the resulting complex within the host cell and even less is known about the mechanism of its nuclear import and integration into the host cell genome. In the present proposal we combined the expertise of the US and Israeli labs and revealed many of the biophysical and biological properties of the genetic transformation process, thus enhancing our understanding of the processes leading to nuclear import and integration of the Agrobacterium T-DNA. Specifically, we sought to: I. Elucidate the interaction of the T-strand with its chaperones. II. Analyzing the three-dimensional structure of the T-complex and its chaperones in vitro. III. Analyze kinetics of T-complex formation and T-complex nuclear import. During the past three years we accomplished our goals and made the following major discoveries: (1) Resolved the VirE2-ssDNA three-dimensional structure. (2) Characterized VirE2-ssDNA assembly and aggregation, along with regulation by VirE1. (3) Studied VirE2-ssDNA nuclear import by electron tomography. (4) Showed that T-DNA integrates via double-stranded (ds) intermediates. (5) Identified that Arabidopsis Ku80 interacts with dsT-DNA intermediates and is essential for T-DNA integration. (6) Found a role of targeted proteolysis in T-DNA uncoating. Our research provide significant physical, molecular, and structural insights into the Tcomplex structure and composition, the effect of host receptors on its nuclear import, the mechanism of T-DNA nuclear import, proteolysis and integration in host cells. Understanding the mechanical and molecular basis for T-DNA nuclear import and integration is an essential key for the development of new strategies for genetic transformation of recalcitrant plant species. Thus, the knowledge gained in this study can potentially be applied to enhance the transformation process by interfering with key steps of the transformation process (i.e. nuclear import, proteolysis and integration). Finally, in addition to the study of Agrobacterium-host interaction, our research also revealed some fundamental insights into basic cellular mechanisms of nuclear import, targeted proteolysis, protein-DNA interactions and DNA repair.
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Hansen, Peter J., and Amir Arav. Embryo transfer as a tool for improving fertility of heat-stressed dairy cattle. United States Department of Agriculture, September 2007. http://dx.doi.org/10.32747/2007.7587730.bard.

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The overall objective of the current proposal is to develop procedures to improve the pregnancy rate achieved following transfer of fresh or cryopreserved embryos produced in the laboratory into heat-stress recipients. The overall hypothesis is that pregnancy rate in heat-stressed lactating cows can be improved by use of embryo transfer and that additional gains in pregnancy rate can be achieved through development of procedures to cryopreserve embryos, select embryos most likely to establish and maintain pregnancy after transfer, and to enhance embryo competence for post-transfer survival through manipulation of culture conditions. The original specific objectives were to 1) optimize procedures for cryopreservation (Israel/US), 2) develop procedures for identifying embryos with the greatest potential for development and survival using the remote monitoring system called EmbryoGuard (Israel), 3) perform field trials to test the efficacy of cryopreservation and the EmbryoGuard selection system for improving pregnancy rates in heat-stressed, lactating cows (US/Israel), 4) test whether selection of fresh or frozen-thawed blastocysts based on measurement of group II caspase activity is an effective means of increasing survival after cryopreservation and post-transfer pregnancy rate (US), and 5) identify genes in blastocysts induced by insulin-like growth factor-1 (IGF-1) (US). In addition to these objectives, additional work was carried out to determine additional cellular determinants of embryonic resistance to heat shock. There were several major achievements. Results of one experiment indicated that survival of embryos to freezing could be improved by treating embryos with cytochalasin B to disrupt the cytoskeleton. An additional improvement in the efficacy of embryo transfer for achieving pregnancy in heat-stressed cows follows from the finding that IGF-1 can improve post-transfer survival of in vitro produced embryos in the summer but not winter. Expression of several genes in the blastocyst was regulated by IGF-1 including IGF binding protein-3, desmocollin II, Na/K ATPase, Bax, heat shock protein 70 and IGF-1 receptor. These genes are likely candidates 1) for developing assays for selection of embryos for transfer and 2) as marker genes for improving culture conditions for embryo production. The fact that IGF-1 improved survival of embryos in heat-stressed recipients only is consistent with the hypothesis that IGF-1 confers cellular thermotolerance to bovine embryos. Other experiments confirmed this action of IGF-1. One action of IGF-1, the ability to block heat-shock induced apoptosis, was shown to be mediated through activation of the phosphatidylinositol 3-kinase pathway. Other cellular determinants of resistance of embryos to elevated temperature were identified including redox status of the embryo and the ceramide signaling pathway. Developmental changes in embryonic apoptosis responses in response to heat shock were described and found to include alterations in the capacity of the embryo to undergo caspase-9 and caspase-3 activation as well as events downstream from caspase-3 activation. With the exception of IGF-1, other possible treatments to improve pregnancy rate to embryo transfer were not effective including selection of embryos for caspase activity, treatment of recipients with GnRH.and bilateral transfer of twin embryos. In conclusion, accomplishments achieved during the grant period have resulted in methods for improving post-transfer survival of in vitro produced embryos transferred into heat-stressed cows and have lead to additional avenues for research to increase embryo resistance to elevated temperature and improve survival to cryopreservation. In addition, embryo transfer of vitrified IVF embryos increased significantly the pregnancy rate in repeated breeder cows.
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