Relevant bibliographies by topics / Transferrin

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Transferrin'

Author: Grafiati
Published: 4 June 2021
Last updated: 28 July 2024

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Journal articles on the topic "Transferrin"

1

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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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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Carlevaro, Mariella F., Adriana Albini, Domenico Ribatti, Chiara Gentili, Roberto Benelli, Silvia Cermelli, Ranieri Cancedda, and Fiorella Descalzi Cancedda. "Transferrin Promotes Endothelial Cell Migration and Invasion: Implication in Cartilage Neovascularization." Journal of Cell Biology 136, no. 6 (March 24, 1997): 1375–84. http://dx.doi.org/10.1083/jcb.136.6.1375.

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During endochondral bone formation, avascular cartilage differentiates to hypertrophic cartilage that then undergoes erosion and vascularization leading to bone deposition. Resting cartilage produces inhibitors of angiogenesis, shifting to production of angiogenic stimulators in hypertrophic cartilage. A major protein synthesized by hypertrophic cartilage both in vivo and in vitro is transferrin. Here we show that transferrin is a major angiogenic molecule released by hypertrophic cartilage. Endothelial cell migration and invasion is stimulated by transferrins from a number of different sources, including hypertrophic cartilage. Checkerboard analysis demonstrates that transferrin is a chemotactic and chemokinetic molecule. Chondrocyte-conditioned media show similar properties. Polyclonal anti-transferrin antibodies completely block endothelial cell migration and invasion induced by purified transferrin and inhibit the activity produced by hypertrophic chondrocytes by 50–70% as compared with controls. Function-blocking mAbs directed against the transferrin receptor similarly reduce the endothelial migratory response. Chondrocytes differentiating in the presence of serum produce transferrin, whereas those that differentiate in the absence of serum do not. Conditioned media from differentiated chondrocytes not producing transferrin have only 30% of the endothelial cell migratory activity of parallel cultures that synthesize transferrin. The angiogenic activity of transferrins was confirmed by in vivo assays on chicken egg chorioallantoic membrane, showing promotion of neovascularization by transferrins purified from different sources including conditioned culture medium. Based on the above results, we suggest that transferrin is a major angiogenic molecule produced by hypertrophic chondrocytes during endochondral bone formation.
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Sarich, V. M. "Transferrin." Transactions of the Zoological Society of London 33, no. 2 (July 8, 2010): 165–71. http://dx.doi.org/10.1111/j.1096-3642.1976.tb00050.x.

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Li, Hongyan, and Zhong Ming Qian. "Transferrin/transferrin receptor-mediated drug delivery." Medicinal Research Reviews 22, no. 3 (March 26, 2002): 225–50. http://dx.doi.org/10.1002/med.10008.

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Farhud, D. D., P. Daneshmand, M. Saffari, R. Hackler, and K. Altland. "Transferrin subtypes in Iran." Anthropologischer Anzeiger 48, no. 4 (December 19, 1990): 347–50. http://dx.doi.org/10.1127/anthranz/48/1990/347.

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Xin, Vechtova, Shaliutina-Kolesova, Fussy, Loginov, Dzyuba, Linhart, et al. "Transferrin Identification in Sterlet (Acipenser ruthenus) Reproductive System." Animals 9, no. 10 (September 30, 2019): 753. http://dx.doi.org/10.3390/ani9100753.

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Transferrins are a superfamily of iron-binding proteins and are recognized as multifunctional proteins. In the present study, transcriptomic and proteomic methods were used to identify transferrins in the reproductive organs and sperm of out-of-spawning and spermiating sterlet (Acipenser ruthenus) males. The results showed that seven transferrin transcripts were identified in the transcriptome of sterlet, and these transcripts were qualified as two different transferrin genes, serotransferrin and melanotransferrin, with several isoforms present for serotransferrin. The relative abundance of serotransferrin isoforms was higher in the kidneys and Wolffian ducts in the spermiating males compared to out-of-spawning males. In addition, transferrin was immunodetected in sterlet seminal plasma, but not in sterlet spermatozoa extract. Mass spectrometry identification of transferrin in seminal plasma but not in spermatozoa corroborates immunodetection. The identification of transferrin in the reproductive organs and seminal plasma of sterlet in this study provides the potential function of transferrin during sturgeon male reproduction.
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Bou Abdallah, Fadi, and Jean-Michel El Hage Chahine. "Transferrins. Hen ovo-transferrin, interaction with bicarbonate and iron uptake." European Journal of Biochemistry 258, no. 3 (December 15, 1998): 1022–31. http://dx.doi.org/10.1046/j.1432-1327.1998.2581022.x.

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9

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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Yu, Ronghua, and Anthony B. Schryvers. "Transferrin receptors on ruminant pathogens vary in their interaction with the C-lobe and N-lobe of ruminant transferrins." Canadian Journal of Microbiology 40, no. 7 (July 1, 1994): 532–40. http://dx.doi.org/10.1139/m94-086.

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The interaction between ruminant transferrins and receptor proteins on the surface of the ruminant pathogens Pasteuerella haemolytica, Haemophilus somnus, Pasteurella multocida, Haemophilus agnii, and Moraxella bovis was evaluated by a combination of binding assays and affinity isolation procedures. Membranes isolated from P. haemolytica, P. multocida, and H. agnii were capable of binding sheep, goat, and cattle transferrins whereas binding by membranes from H. somnus and M. bovis was specific for bovine transferrin. Proteolytically derived bovine transferrin C-lobe was capable of inhibiting the interaction between bovine transferrin and both Tbpl and Tbp2 from P. haemolytica and M. bovis but only Tbpl from H. somnus and P. multocida. Proteolytically derived N-lobe inhibited the binding of P. multocida and H. somnus Tbp2 to bovine transferrin and the binding of bovine transferrin to the single receptor protein identified in H. agnii. The implications of these results regarding the nature of the ligand–receptor interaction and similarities of this interaction with ligand–receptor interactions in different species are discussed.Key words: iron acquisition, transferrin receptor, binding specificity, Pasteurella, ruminants.
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Dissertations / Theses on the topic "Transferrin"

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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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Sharma, Nita Devi. "Molecular definition of the interaction of transferrin with the meningococcal and human transferrin receptor." Thesis, Birkbeck (University of London), 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.338641.

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Stokes, Russell Hayden. "Meningococcal transferrin binding proteins A and B form a functional human serum transferrin receptor." Thesis, King's College London (University of London), 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.313503.

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Booyjzsen, Claire. "Fibril formation by human transferrin." Thesis, University of Warwick, 2011. http://wrap.warwick.ac.uk/51615/.

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There is a well-established connection between anomalous protein aggregates and disease, exemplified by the amyloidoses. Many neurological disorders such as Al heimer’s and Parkinson’s disease also show increased concentrations of iron deposits along with protein fibres. The increased metal concentrations observed in these instances have yet to be fully understood or explained. The research in this thesis is concerned with the aggregation of the protein transferrin, especially on surfaces. Human serum transferrin is an ~80 kDa iron-transporting glycoprotein found at 35 μM in the blood. It is also the body’s generic metal transporter, not only of the “natural” metals iron and manganese but also of metals used to detect or treat disease such as gallium and ruthenium. It has recently been reported from this laboratory that some batches of human serum transferrin can form fibrils on surfaces. This appeared to occur preferentially at lower salt and protein concentrations. The fibres exhibited a distinctive subunit structure with a consistent width of ca. 200 nm, and dark periodic striations along the length of the fibres apparently due to deposition of ferric (oxy)hydroxo mineral, lepidocrocite. The ability of human serum transferrin and recombinant (largely deglycosylated) transferrin to form fibres on surfaces has been investigated. Batches which formed fibres appeared to have normal primary, secondary and tertiary structures, and iron-binding properties, as determined by UV-visible and circular dichroism, spectroscopy, isothermal titration calorimetry, and ion-mobility-mass spectrometry. Dye binding experiments in solution suggested that classical amyloid fibres are not formed in solution. However, investigations of gas-phase conformations of transferrin from fibre-forming solutions, by ion mobility mass spectrometry, revealed an intrinsic transferrin dimer and higher order structures. These were separated by chromatography. Dimeric and monomeric transferrin were imaged on surfaces using transmission electron microscopy and atomic force microscopy. Only the dimer yielded structured aggregates, circular subunits composed of transferrin fibres. Dynamic light scattering and polyacrylamide gel electrophoresis further confirmed the presence of higher order structures in solution. Hence dimerisation of transferrin appears to trigger the initiation formation of fibrils possibly by pre-ordering of the protein in solution. Further atomic force microscopy analysis of deposited transferrin on mica surfaces by atomic force microscopy revealed the deformation (flattening) of the protein perhaps indicating structural flexibility that may be important for fibril formation. Some long, thin fibrils with distinct curvature were detectable by AFM. This appears to support the hypothesis that many proteins can exhibit fibril-like behaviour under specific conditions. If transferrin aggregation can occur when the protein is deposited on natural surfaces in the body, these findings may have important implications for certain physiological disorders including neurological conditions and lead to new treatments.
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Baptista, Rafaela Speranza [UNESP]. "Proteinograma sérico de cordeiros nascidos a termo ou prematuros." Universidade Estadual Paulista (UNESP), 2016. http://hdl.handle.net/11449/146742.

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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
Ao final da gestação o neonato deve estar preparado, por meio de modificações funcionais e estruturais de órgãos e sistemas para dar início à vida extra-uterina. Os animais prematuros nascem antes deste processo estar completo, apresentando falhas na maturação. O objetivo deste estudo foi tentar identificar por meio da técnica de eletroforese em gel de poliacrilamida em dodecil sulfato de sódio (SDS-PAGE) proteínas de fase aguda, dentre elas, albumina, ceruloplasmina, transferrina, haptoglobina, glicoproteína ácida e imunoglobulinas A e G, que possam indicar a maturação no neonato prematuro. Os cordeiros foram divididos em seis grupos experimentais (parto normal, cesárea a termo, cesárea prematura, cesárea prematura com administração pré-parto materna de dexametasona, cesárea com administração de surfactante nos prematuros e cesárea prematura com administração pré-parto materna de dexametasona e surfactante ao neonato). Os resultados indicaram que após a administração de colostro, independente do tratamento, os valores séricos de proteína total e imunoglobulinas G aumentaram, indicando que há transferência de imunidade passiva através do trato gastrointestinal. A transferrina tem seus teores superiores em animais com idade gestacional superior, demonstrando potencial para ser utilizado como marcador de maturação neonatal.
At the end of gestation the neonate should be prepared, with functional and structural modifications of organs and systems to initiate extrauterine life. Premature animals are born before this process is complete, presenting maturation failures. The aim of this study was to identify an acute phase protein, such as albumin, ceruloplasmin, transferrin, haptoglobin, acid glycoprotein and immunoglobulins A and G, that demonstrates that different treatments indicate a maturation in the premature neonate using sodium dodecyl sulfate polyacrylamide gel electrophoresis technique (SDS-PAGE). The lambs were divided into six experimental groups (normal birth, full-term cesarean section at normal time of gestation, premature cesarean section, premature cesarean section whose mothers received prepartum dexamethasone, cesarean section giving surfactante to the prematures and premature cesarean giving prepartum dexamethasone to the mothers and surfactant to the neonate). The results indicated that after administration of colostrum, regardless of treatment, total serum protein and immunoglobulins increased, showing the transfer of passive immunity through the gastrointestinal tract. Transferrin has higher levels in animals with higher gestational age, demonstrating potential as a marker of neonatal maturation.
FAPESP: 2011/18810-3
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Baptista, Rafaela Speranza. "Proteinograma sérico de cordeiros nascidos a termo ou prematuros /." Araçatuba, 2016. http://hdl.handle.net/11449/146742.

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Orientador: Luiz Claudio Nogueira Mendes
Coorientadora: Fernanda Bovino
Banca:Francisco Leydson Formiga Feitosa
Banca:Marcio Carvalho da Costa
Resumo: Ao final da gestação o neonato deve estar preparado, por meio de modificações funcionais e estruturais de órgãos e sistemas para dar início à vida extra-uterina. Os animais prematuros nascem antes deste processo estar completo, apresentando falhas na maturação. O objetivo deste estudo foi tentar identificar por meio da técnica de eletroforese em gel de poliacrilamida em dodecil sulfato de sódio (SDS-PAGE) proteínas de fase aguda, dentre elas, albumina, ceruloplasmina, transferrina, haptoglobina, glicoproteína ácida e imunoglobulinas A e G, que possam indicar a maturação no neonato prematuro. Os cordeiros foram divididos em seis grupos experimentais (parto normal, cesárea a termo, cesárea prematura, cesárea prematura com administração pré-parto materna de dexametasona, cesárea com administração de surfactante nos prematuros e cesárea prematura com administração pré-parto materna de dexametasona e surfactante ao neonato). Os resultados indicaram que após a administração de colostro, independente do tratamento, os valores séricos de proteína total e imunoglobulinas G aumentaram, indicando que há transferência de imunidade passiva através do trato gastrointestinal. A transferrina tem seus teores superiores em animais com idade gestacional superior, demonstrando potencial para ser utilizado como marcador de maturação neonatal.
Abstract:At the end of gestation the neonate should be prepared, with functional and structural modifications of organs and systems to initiate extrauterine life. Premature animals are born before this process is complete, presenting maturation failures. The aim of this study was to identify an acute phase protein, such as a lbumin, ceruloplasmin, transferrin, haptoglobin, acid glycoprotein and immunoglobulins A and G, that demonstrates that different treatments indicate a maturation in the premature neonate using sodium dodecyl sulfate polyacrylamide gel electrophoresis technique (SDS - PAGE) . The lambs were divided into six experimental groups (normal birth, full - term cesarean section at norma l time of gestation, premature cesarean section, premature cesarean section whose mothers received prepartum dexamethasone, cesarean section giving surfactante to the prematures and premature cesarean giving prepartum dexamethasone to the mothers and surfactant to the n eonate). The results indicated that after administration of colostrum, regardless of treatment, total serum protein and immunoglobulins increased, showing the transfer of passive immunity through the gastrointestinal tract. Transfer rin has higher levels in animals with higher gestational age, demonstrating potential as a marker of neonatal maturation
Mestre
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7

Trimble, Esther R. "Carbohydrate-deficient transferrin and alcohol abuse." Thesis, Queen's University Belfast, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.388195.

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Kaur, Ishwinder. "Nuclear translocation and transferrin-transferrin receptor interaction of IPSE/[alpha}-1, a secretory glycoprotein from Schistosoma mansoni." Thesis, University of Nottingham, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.508222.

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Helminthic parasites have evolved with immune modulating machinery to manipulate their host's immune response and thus survive unscathed for years and in some cases even decades. However, the underlying molecular mechanisms governing the host-parasite relationship are still largely unknown. Therefore detailed investigation and evaluation of parasitic molecules is desirable. One such molecule worthy of attention is IPSE/a-1 (lnterleukin-4 inducing principle from schistosome eggs). IPSE/a-1 is a secretory glycoprotein produced exclusively by the egg stage of Schistosoma mansoni, which activates human basophils in non-antigen specific IgE dependent mechanisn;t. Sequence analyses of IPSE/a-1 using bioinformatic subcellular localisation prediction tools revealed a putative nuclear localisation signal (NLS) at the C-terminus. The present work was conducted to confirm whether this sequence ('125-PKRRRTY-131') was both necessary and sufficient for nuclear localisation of IPSE/a-1 and other heterologous GFP proteins. A plasmid encoding EGFP-IPSE/a-1, as well as a truncated mutant lacking amino acids 125-134, was transfected into Huh7 and U2-0S cell lines, and fluorescence of the fusion protein was determined by confocal laser scanning microscopy. EGFP-IPSE/a-1 was found to be exclusively nuclear, whereas the mutant displayed both nuclear and cytoplasmic staining. Furthermore, insertion of the IPSE/a-1 NLS into a tetra-EGFP construct showed nuclear localisation, and alanine scanning mutagenesis revealed a requirement for the KRRR residues. IPSE/a-l also binds to transferrin, which lead to downstream effect on cellular proliferation. Besides, fluorescence microscopy revealed that recombinant IPSE/a-l protein added exogenously to culture medium was internalized by variant Chinese hamster ovary (CRO) cells expressing the human transferrin receptor and was found in the nuclei of these cells Western blotting further confirmed this temporal relocalisation of IPSE/a-l from cytosolic to nuclear fractions. In addition, IPSE/a-l exhibited a DNA-binding activity that appeared to be dependent on the C-terminal NLS sequence. In summary, the main achievement of this work is the identification and characterization of a NLS in IPSE/a-l that is functional in mammalian cells, which will form the basis for further investigations into the biological significance of this nuclear targeting and DNA interaction e.g. IPSE/a-l may function as transcription factor in the nucleus. The properties of IPSE/a-l described here also make it an interesting potential vehicle for intracellular and nuclear drug delivery.
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Bergström, Jonas P. "Human serum transferrin glycosylation pattern : population differencies, analytical methodology and application as biomarker for testing of alcohol abuse and CDG /." Stockholm, 2007. http://diss.kib.ki.se/2007/978-91-7357-432-7/.

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Houldershaw, David. "The electrostatics of iron binding to transferrin." Thesis, Birkbeck (University of London), 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.244463.

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Books on the topic "Transferrin"

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Hodgkins, Paul Spencer. Reduced metal transferrin binding in neurological diseases. Birmingham: Aston University. Department ofPharmaceutical Sciences, 1992.

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International, Conference on Proteins of Iron Metabolism (7th 1985 Villeneuve-d'Ascq France). Proteins of iron storage and transport: Proceedings of the 7th International Conference on Proteins of Iron Metabolism held in Villeneuve d' Ascq (France) on 30 June-5 July, 1985. Amsterdam: Elsevier Science Publishers, 1985.

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

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Winsper, Sarah Jane. Metal binding to transferrin and immune reactions in Parkinson's disease. Birmingham: Aston University. Department of Pharmaceutical and Biological Sciences, 1995.

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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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Pétren, Sven. Non-genetic heterogeneity of serum transferrin as a marker of liver dysfunction. Solna [Sweden]: Arbetsmiljöinstitutet, 1988.

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Marwah, Sukhjinder Singh. Role of non-transferrin bound iron in acute leukaemia and sickle cell disease. Wolverhampton: University of Wolverhampton, 2001.

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Jong, Gerardus de. The physiological significance of transferrin microheterogeneity: An interpretation of the role of N-linked glycans in transferrin and iron metabolism ...Proeefschrift ter verkrijging van de graad van doctor... 1993 ... Rotterdam: [Department of Chemical Pathology, Erasmus University Rotherham?], 1993.

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Book chapters on the topic "Transferrin"

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Papanikolaou, George, Konstantinos Gkouvatsos, and Kostas Pantopoulos. "Transferrin." In Encyclopedia of Signaling Molecules, 5615–23. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101940.

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Töpfer, G. "Transferrin." In Springer Reference Medizin, 2333–35. Berlin, Heidelberg: Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_3081.

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Töpfer, G. "Transferrin." In Lexikon der Medizinischen Laboratoriumsdiagnostik, 1–3. Berlin, Heidelberg: Springer Berlin Heidelberg, 2018. http://dx.doi.org/10.1007/978-3-662-49054-9_3081-1.

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Ward, Tony Milford. "Transferrin." In Proteins and Tumour Markers May 1995, 1390–93. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-0681-8_79.

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Mehlhorn, Heinz. "Transferrin." In Encyclopedia of Parasitology, 2786. Berlin, Heidelberg: Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-43978-4_4909.

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Mehlhorn, Heinz. "Transferrin." In Encyclopedia of Parasitology, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-642-27769-6_4909-1.

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von Bonsdorff, Leni, Hennie ter Hart, Ingrid Prins-De Nijs, Anky Koenderman, Jan Over, and Jaakko Parkkinen. "Transferrin." In Production of Plasma Proteins for Therapeutic Use, 301–10. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2012. http://dx.doi.org/10.1002/9781118356807.ch21.

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Papanikolaou, George, Konstantinos Gkouvatsos, and Kostas Pantopoulos. "Transferrin." In Encyclopedia of Signaling Molecules, 1–9. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_101940-1.

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Arampatzis, Adamantios, Lida Mademli, Thomas Reilly, Mike I. Lambert, Laurent Bosquet, Jean-Paul Richalet, Thierry Busso, et al. "Transferrin." In Encyclopedia of Exercise Medicine in Health and Disease, 867–68. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-540-29807-6_3141.

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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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Conference papers on the topic "Transferrin"

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Chandra, D., and P. Karande. "Transferrin mediated drug delivery to brain." In 2011 37th Annual Northeast Bioengineering Conference (NEBEC). IEEE, 2011. http://dx.doi.org/10.1109/nebc.2011.5778697.

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Girard, A., F. Bendriaa, O. De Sagazan, M. Harnois, F. Le Bihan, A. C. Salaun, T. Mohammed-Brahim, P. Brissot, and O. Loreal. "Transferrin Electronic Detector for Iron Disease Diagnostics." In 2006 5th IEEE Conference on Sensors. IEEE, 2006. http://dx.doi.org/10.1109/icsens.2007.355509.

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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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Gorman, Maureen J. "Transferrin-1 as an immune protein inManduca sextaandDrosophila melanogaster." In 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.113056.

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Sinsuebphon, Nattawut, Travis Bevington, Lingling Zhao, Abe Ken, Margarida Barroso, and Xavier Intes. "Comparison of NIR FRET pairs for quantitative transferrin-based assay." In SPIE BiOS, edited by Fred S. Azar and Xavier Intes. SPIE, 2014. http://dx.doi.org/10.1117/12.2040097.

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Khoo, Ting Chean, Kate Tubbesing, Cat Pham, Habben Desta, Anna Sharikova, Margarida Barroso, and Alexander T. Khmaladze. "Raman hyperspectral imaging of transferrin-bound iron in cancer cells." In Label-free Biomedical Imaging and Sensing (LBIS) 2019, edited by Natan T. Shaked and Oliver Hayden. SPIE, 2019. http://dx.doi.org/10.1117/12.2511397.

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Chen, Sez-Jade, Nattawut Sinsuebphon, Alena Rudkouskaya, Margarida Barroso, and Xavier Intes. "Noninvasive Characterization of PEGylated Transferrin Probe Delivery Using Lifetime-based FRET." In Clinical and Translational Biophotonics. Washington, D.C.: OSA, 2018. http://dx.doi.org/10.1364/translational.2018.jth3a.19.

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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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Tubbesing, Kate, Ting Khoo, Anna Sharikova, Margarida Barroso, and Alexander Khmaladze. "Raman mapping of transferrin and ferritin distributions in breast cancer cells." In Label-free Biomedical Imaging and Sensing (LBIS) 2021, edited by Natan T. Shaked and Oliver Hayden. SPIE, 2021. http://dx.doi.org/10.1117/12.2579413.

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Konduru, N., K. Zagorovsky, D. Diaz-Diiestra, F. Fisol, M. Sanches, A. Swami, J. D. Brain, and R. Molina. "Pulmonary Fate and Consequences of Albumin- and Transferrin-Coated Gold Nanoparticles." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a2247.

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Reports on the topic "Transferrin"

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Author, Not Given. Transferred Electron Photoemitters. Office of Scientific and Technical Information (OSTI), November 2018. http://dx.doi.org/10.2172/1483867.

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LaVine, Nils D., Robert Kehlet, Michael J. O'Connor, and Dennis L. Jones. Transferring Ownership of ModSAF Behavioral Attributes. Fort Belvoir, VA: Defense Technical Information Center, January 1999. http://dx.doi.org/10.21236/ada530486.

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Hu, Patricia S., Tim Reuscher, Richard L. Schmoyer, and Shih-Miao Chin. Transferring 2001 National Household Travel Survey. Office of Scientific and Technical Information (OSTI), May 2007. http://dx.doi.org/10.2172/931511.

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Heyland, D. J. Transferring Space Technology, A Success Story. Natural Resources Canada/CMSS/Information Management, 1987. http://dx.doi.org/10.4095/217428.

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Smith, Bernard N., Spencer Jr, Horne David, Blazer Michael, Ohnemus Doug, and Robert. Reporting, Recording, and Transferring Contingency Demand Data. Fort Belvoir, VA: Defense Technical Information Center, March 2000. http://dx.doi.org/10.21236/ada379918.

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Farhar, B. C., M. A. Brown, B. L. Mohler, M. Wilde, and F. H. Abel. A planning framework for transferring building energy technologies. Office of Scientific and Technical Information (OSTI), July 1990. http://dx.doi.org/10.2172/6887188.

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Rocklemore, Chiquita, Olubunmi Osinloye, Angela Uta, and Tracy McClinton. Transferring Patients to a Higher Level of Care. University of Tennessee Health Science Center, May 2022. http://dx.doi.org/10.21007/con.dnp.2022.0039.

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Schlossberg, Marc. Transferring Community-based, Active Transportation GIS Assessment Tools Nationwide. Portland State University Library, August 2009. http://dx.doi.org/10.15760/trec.9.

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Hollis, K., B. Bartram, R. Strom, J. Withers, and J. Massarello. Plasma Transferred Arc Deposition of Beryllium (Preprint). Fort Belvoir, VA: Defense Technical Information Center, January 2005. http://dx.doi.org/10.21236/ada442194.

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Farhar, B. C., M. A. Brown, B. L. Mohler, M. Wilde, and F. H. Abel. A planning framework for transferring building energy technologies: Executive Summary. Office of Scientific and Technical Information (OSTI), August 1990. http://dx.doi.org/10.2172/6541446.

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