FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2013148369> ?p ?o ?g. }

• W2013148369 endingPage "118" @default.
• W2013148369 startingPage "113" @default.
• W2013148369 abstract "American Journal of HematologyVolume 39, Issue 2 p. 113-118 Concise Review Receptor-mediated iron uptake and intracellular iron transport Dr. Simeon Pollack, Corresponding Author Dr. Simeon Pollack Department of Medicine, Albert Einstein College of Medicine, Bronx, New YorkDepartment of Medicine, Albert Einstein College of Medicine, 1300 Morris Avenue, Bronx, NY 10461Search for more papers by this author Dr. Simeon Pollack, Corresponding Author Dr. Simeon Pollack Department of Medicine, Albert Einstein College of Medicine, Bronx, New YorkDepartment of Medicine, Albert Einstein College of Medicine, 1300 Morris Avenue, Bronx, NY 10461Search for more papers by this author First published: February 1992 https://doi.org/10.1002/ajh.2830390208Citations: 21AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat References 1 Ward JH, Kushner JP, Kaplan J: Regulation of HeLa cell transferrin receptors. J Biol Chem 257: 10317, 1982. 2 Louache F, Testa U, Pellicci P, Thomopoulos P, Titeux M, Rochent H: Regulation of transferrin receptors in human hematopoietic cell lines. J Biol Chem 259: 11576–11582, 1984. 3 Roualt T, Rao K, Harford J, Mattia E, Klausner RD: Hemin, chelatable iron, and the regulation of transferrin receptor biosynthesis. J Biol Chem 260: 14862–14866, 1985. 4 Muller-Eberhard U, Liem HH, Grasso JA, Giffhorn-Katz S, DeFalco MG, Katz NR: Increase in surface expression of transferrin receptors on cultured hepatocytes of adult rats in response to iron deficiency. J Biol Chem 263: 14753–14756, 1988. 5 Pelosi-Testa E, Testa U, Samoggia P, Salvo G, Camagna A, Peschle C: Expression of transferrin receptors in human erythroleukemic lines: rcgulation in the plateau and exponential phase of growth. Cancer Res 46: 5330–5334, 1986. 6 Iacopetta BJ, Morgan EH, Yeoh GCT: Transferrin receptors and iron uptake during erythroid development. Biochim Biophys Actd 687: 204–210, 1982. 7 Nunez MT, Glass J, Fischer S, Lavidor LM, Lenk EM, Robinson SH: Transferrin receptors in developing murine erythroid cells. Br J Haematol 36: 519–526, 1977. 8 Testa U, Petrini M, Quaranta MT, Pelosi-Testa E, Mastroberardino G, Camagna A, Boccoli G, Sargiacomo M, Isacchi G, Cozzi A, Arosio P, Peschle C: Iron up-Modulates the expression of transferrin receptors during nionocyte-Macrophage maturation. J Biol Chem 264: 13181–13187, 1989. 9 Hradilek A, Neuwirt J: Iron uptake from transferrin and transferrin endocytic cycle in Friend erythroleukemia cells. J Cell Physiol 133: 192–196, 1987. 10 Intragumtornchai T, Huebers HA, Eng M, Finch CA: In vivo transferrin-Iron receptor relationships in erythron of rats. Am J Physiol 255: R326–R331, 1988. 11 Black C, Glass J, Nunez MT, Robinson SH: Transferrin binding and iron transport in iron-Deficient and iron-Replete rat reticulocytes. J Lab Clin Med 93: 645–651, 1979. 12 Sorokin LM, Morgan EH, Yeoh GCT: Transformation-Induced changes in transferrin and iron metabolism in myogenic cells. Cancer Res 49: 1941–1947, 1989. 13 Muta K, Nishimura J, Yamamoto M, Ldeguchi H, Katsuno M, Ibayashi H: Possible mechanism of ineffective erythropoiesis by an altered transferrin receptor cycle in erythroleukemia. Eur J Haematol 40: 309–314, 1988. 14 Bowen BJ, Morgan EH: Anemia of the Belgrade rat : Evidence for defective membrane transport of iron. Blood 70: 38–44, 1987. 15 Renswoude JV, Bridges KR, Harford JB, Klausner RD: Receptormediated endocytosis of transferrin and the uptake of Fe in K562 cells: Identification of a nonlysosomal acidic compartment. Proc Natl Acad Sci USA 79: 6186–6190, 1982. 16 Glass J, Nunez MT: Amines as inhibitors of iron transport in rabbit reticulocytes. J Biol Chem 261: 8298–8302, 1986. 17 Chan RYY, Loh TT: Perturbation of intracellular pH by DIDS on endocytosis of transferrin and iron uptake in rabbit reticulocytes. Biochem Biophys Res Commun 150: 12. 56–1262, 1988. 18 Bali PK, Zak O, Aisen P: A new role for the transferrin receptor in the release of iron from transferrin. Biochemistry 30: 324–328, 1991. 19 Pollack S, Vanderhoff G, Lasky F: Iron removal from transferrin—an experimental study. Biochim Biophys Acta 497: 481–487, 1977. 20 Steinberg TH, Newman AS, Swanson JA, Silverstein SC: ATP 4-Permeabilizes the plasma membrane of mouse macrophages to fluorescent dyes. J Biol Chem 262: 8884–8888, 1987. 21 Painter GR, Diliberto EJ, Knoth J: 31P nuclear magnetic resonance study of the metabolic pools of adenosine triphosphate in cultured bovine adrenal medullary chromaffin cells. Proc Natl Acad Sci USA 86: 2239–2242, 1989. 22 Egyed A: Carrier mediated iron transport through erythroid membrane. Br J Haematol 68: 483–486, 1988. 23 Morgan EH: Membrane transport of non-Transferrin bound iron by reticulocytes. Biochim Biophys Acta 943: 428–439, 1988. 24 Basset P, Quesneau Y, Zwiller J: Iron induced L1210 cell growth: Evidence of a transferrin-Independent iron transport. Cancer Res 46: 1644–1647, 1986. 25 Taetle R, Rhyner K, Castagnola J, To D, Mendelsohn J: Role of transferrin, Fe and transferrin receptors in myeloid leukemia cell growth. J Clin Invest 75: 1061–1067, 1985. 26 Surrock A, Alexander J, Lamb J, Craven CM, Kaplan J: Characterization of a transferrin-Independent uptake system for iron in HeLa cells. J Biol Chem 265: 3139–3145, 1990. 27 Glass J, Nunez MT, Robinson SH: Transferrin-Binding and iron-Binding proteins of rabbit reticulocyte plasma membranes. Biochim Biophys Acta 598: 293–304, 1980. 28 Simpson RJ, Moore R, Peters TJ: Significance of non-Esterified fatty acids in iron uptake by intestinal brush-Border membrane vesicles. Biochim Biophys Acta 941: 3947, 1988. 29 Nunez MT, Pinto I, Glass J: Assay and characteristics of the iron binding moiety of reticulocyte endocytic vesicles. J Membr Biol 107: 129–135, 1989. 30 Nunez M, Gaete V, Watkins JA, Glass J: Mobilization of iron from endocytic vesicles. The effects of acidification and reduction. J Biol Chem 265: 6688–6692, 1990. 31 Sun IL, Navas P, Crane FL, Morre DJ, Low H: NADH diferric transferrin reductase in liver plasma membrane. J Biol Chem 262: 15915–15921, 1987. 32 Jasaitis AA, Nemecek IB, Severina LI, Skulachev VP, Smirnova SM: Membrane potential generation by two reconstituted mitochondrial systems: Liposomes inlayed with mitochondrial oxidase or with ATPase. Biochim Biophys Acta 275: 485–490, 1972. 33 Halliwell B, Gutteridge JMC: “ Free Radicals in Biology and Medicine.” Oxford: Clarendon Press, 1985. 34 Thorstensen K, Aisen P: Release of iron from diferric transferrin in the presence of rat liver plasma membrane: No evidence of a plasma membrane diferric transferrin reductase. Biochim Biophys Acta 1052: 29–32, 1990. 35 Weaver J, Pollack S: Low MW Fe isolated from guinea pig reticulocytes as AMP-Fe and ATP-Fe complexes. Biochem J 261: 787–792, 1989. 36 Bartlett GR: Patterns of phosphate compounds in red blood cells of man and animals. Adv Exp Med Biol 6: 245–256, 1970. 37 Meyers NL, Brewer GJ, Oelshlegel FJ: Iron-APT a by-Product of acid extraction of whole blood or red blood cells. Biochim Biophys Acta 320: 397–405, 1973. 38 Hedman K, Goldenthal KL, Rutherford AV, Pastan I, Willingham MC: Comparison of the intracellular pathways of transferrin recycling and vesicular stomatitis virus membrane glycoprotein exocytosis by ultrastructural double-Label cytochemistry. J Histochem Cytochem 35: 233–243, 1987. 39 Stoorvogel W, Geuze HJ, Griffith JM, Schwartz AL, Strous GJ: Relations between the intracellular pathways of the receptors for transferrin, asialoglycoprotein and mannose-6-Phosphate in human hepatoma cells. J Cell Biol 108: 2137–2148, 1989. 40 Hoy TG, Harrison PM: The uptake of ferric iron by rat liver ferritin in vivo and in vitro. Br J Haematol 33: 497–504, 1976. 41 Benham CD, Tsien RW: A novel receptor operated Ca2+ permeable channel activated by ATP in smooth muscle. Nature 328: 275–278, 1987. 42 Sung SJ, Young JD, Origlio AM, Heiple JM, Kaback HR, Silverstein SC: Extracellular ATP perturbs transmembrane ion fluxes, elevates cytosolic Ca and inhibits phagocytosis in mouse macrophages. J Biol Chem 260: 13442–13449, 1985. 43 Boyer JL, Downes CP, Harden TK: Kinetics of activation of phospholipase C by P2Y purinergic receptor agonists and guanine nucleotides. J Biol Chem 264: 884–890, 1989. 44 Blackburn GW, Morgan EH: Factors affecting iron and transferrin release from rabbit reticulocyte ghosts to cytosol. Biochim Biophys Acta 497: 728–744, 1977 45 Nunez M, Cole ES, Glass J: Cytosol intermediates in the transport of iron. Blood 55: 1051–1055, 1980. 46 Pollack S, Campana T: Early events in guinea pig reticulocyte iron uptake. Biochim Biophys Acta 672: 366–373, 1981. 47 Zhan H, Gupta RK, Weaver J, Pollack S: Iron bound to low MW ligands: Interactions with mitochondria and cytosolic proteins. Eur J Haematol 44: 124–130, 1990. 48 Minotti G: Adriamycin-Dependent release of iron from microsomal membranes. Arch Biochem Biophys 268: 398–403, 1989. 49 Pollack S, Weaver J, Zhan H: Intracellular iron. Blood 76: 15A, 1990. 50 Weaver J, Zhan H, Pollack S: Mitochondria have Fe(iII) receptors. Biochem J 265: 415–419, 1990. 51 Weaver J, Pollack S: Two types of receptors for iron on mitochondria. Biochem J 271: 463–466, 1990. 52 Fishman JB, Fine RE: A Trans golgi-Derived exocytic coated vesicle can contain both newly synthesized cholinesterase and internalized transferrin. Cell 48: 157–164, 1987. 53 Stein BS, Sussman HH: Demonstration of two distinct transferrin receptor recycling pathways and transferrin-Independent receptor internalization in K 562 cells. J Biol Chem 261: 10319–10331, 1986. 54 Okeefe DO, Draper RK: Two pathways of transferrin recycling evident in a variation of mouse LMTK-Cells. Somat Cell Mol Genet 14: 473–487, 1988. 55 Zhan H, Pollack S, Weaver J: Two pathways for iron uptake by guinea pig reticulocytes. Eur J Haematol 45: 15–18, 1990. 56 Cotner T, Gupta AD, Papayannopoulou T, Stamatoyannopoulos G: Characterization of a novel form of transferrin receptor preferentially expressed on normal erythroid progenitors and precursors. Blood 73: 214–221, 1989. 57 Bolli R, Patel BS, Zhu W, O'neill PG, Hartley CG, Charlat ML, Roberts R: The chelator desferrioxamine attenuates postischemic ventricular dysfunction. Am J Physiol 253: H1372–H1380, 1987. 58 Gutteridge JMC, Halliwell B: Reoxygenation injury and antioxidant protection: A tale of two paradoxes. Arch Biochem Biophys 283: 223–226, 1990. 59 Downey JM: Free radicals and their involvement during long term myocardial ischemia and reperfusion. Annu Rev Physiol 52: 487–504, 1990. 60 Bolli R, Patel BS, Jeroudi MO, Li X, Triana JF, Lai EK, McCay PB: Iron mediated radical reactions upon reperfusion contribute to myocardial stunning. Am J Physiol 259: H1901–H1911, 1990. 61 Lesnefsy EJ, Repine JE, Horwitz LD: Desferoxamine pretreatment reduces canine infarct size and oxidative injury. J Pharmacol Exp Ther 253: 1103–1109, 1990. 62 Williams RE, Zweier JL, Flaherty JT: Treatment with deferoxamine during ischemia improves functional and metabolic recovery and reduces reperfusion-Induced oxygen radical generation in rabbit hearts. Circulation 83: 1006–1014, 1991. 63 Holt S, Gunderson M, Joyce K, Nayini NR, Eyster F, Garutabi AM, Zonia C, Krause GS, Aust SD, White BC: Myocardial tissue iron delocalization and evidence for lipid peroxidation after two hours of ischemia. Ann Emerg Med 15: 1155–1159, 1986. 64 Kraaij, AMM, Mostert LJ, van Eijk HG, Koster JF: Iron-Load increase the susceptibility of rat hearts to oxygen reperfusion damage. Circulation 78: 442–449, 1988. 65 Kraaij AMM, van Eijk HG, Koster JF: Prevention of postischemic cardiac injury by the orally active iron chelator 1,2 dimethyl-3-Hydroxy-4-Pyridone (lI) and the antioxidant (+) cyanidanol-3. Circulation 80: 158–164, 1989. 66 Biemond P, Swaak AJG, Beindorff CM, Koster JF: Superoxide-De pendent and -Independent mechanisms of iron mobilization from ferritin by xanthine oxidase. Biochem J 239: 169–173, 1986. 67 Bolann BJ, Ulvik RJ: On the limited ability of superoxide to release iron from ferritin. Eur J Biochem 193: 899–904, 1990. 68 Stone D, Darley-Usmar WM, Smith DR, O'leary V: Hypoxia-Reoxygenation induced increase in cellular Ca2+ in myocytes and perfused hearts: The role of mitochondria. J Mol Cell Cardiol 21: 963–973, 1989. 69 Darley-Usmar VM, Smith DR, O'leary DJ, Stone D, Hardy DI, Clark JB: Hypoxia-Reoxygenation induced damage in the myocardium: The role of mitochondria. Biochem Soc Trans 18: 526–528, 1990. 70 Merryfield ML, Lardy HA: Ca2+ from rat liver mitochondria. J Biol Chem 257: 3628–3635, 1982. 71 Park Y, Bowles DK, Kehrer JP: Protection against hypoxic injury in isolated-Perfused rat heart by ruthernium red. J Pharmacol Exp Ther 253: 628–635, 1990. 72 Jandl JH, Katz JH: The plasma-To-Cell cycle of transferrin. J Clin Invest 42: 314–326, 1963. 73 Huekbers HA, Beguin Y, Pootrakul P, Einspahr D, Finch CA: Intact trasnsferrin receptors in human plasma and their relation to erythropoiesis. Blood 75: 102–107, 1990. 74 Skikne BS, Flowers CH, Cook JD: Serum transferrin receptor: A quantitative measure of tissue iron deficiency. Blood 75: 1870–1876, 1990. Citing Literature Volume39, Issue2February 1992Pages 113-118 ReferencesRelatedInformation" @default.
• W2013148369 created "2016-06-24" @default.
• W2013148369 creator A5057321775 @default.
• W2013148369 date "1992-02-01" @default.
• W2013148369 modified "2023-09-25" @default.
• W2013148369 title "Receptor-mediated iron uptake and intracellular iron transport" @default.
• W2013148369 cites W104831399 @default.
• W2013148369 cites W1489733138 @default.
• W2013148369 cites W1498549327 @default.
• W2013148369 cites W1516729867 @default.
• W2013148369 cites W1545646101 @default.
• W2013148369 cites W1559051892 @default.
• W2013148369 cites W1560836239 @default.
• W2013148369 cites W1575369553 @default.
• W2013148369 cites W1579613226 @default.
• W2013148369 cites W1579992296 @default.
• W2013148369 cites W1590684642 @default.
• W2013148369 cites W1591755807 @default.
• W2013148369 cites W1595375154 @default.
• W2013148369 cites W1599567494 @default.
• W2013148369 cites W1669232021 @default.
• W2013148369 cites W1671669579 @default.
• W2013148369 cites W1860804592 @default.
• W2013148369 cites W1970526262 @default.
• W2013148369 cites W1974629714 @default.
• W2013148369 cites W1977342487 @default.
• W2013148369 cites W1987881941 @default.
• W2013148369 cites W1991967206 @default.
• W2013148369 cites W1999491269 @default.
• W2013148369 cites W2002811180 @default.
• W2013148369 cites W2004156444 @default.
• W2013148369 cites W2009935511 @default.
• W2013148369 cites W2012708231 @default.
• W2013148369 cites W2013323121 @default.
• W2013148369 cites W2021200424 @default.
• W2013148369 cites W2021434884 @default.
• W2013148369 cites W2022371229 @default.
• W2013148369 cites W2024706720 @default.
• W2013148369 cites W2028996539 @default.
• W2013148369 cites W2033199106 @default.
• W2013148369 cites W2037577591 @default.
• W2013148369 cites W2038692354 @default.
• W2013148369 cites W2039817098 @default.
• W2013148369 cites W2040122565 @default.
• W2013148369 cites W2041718235 @default.
• W2013148369 cites W2052630833 @default.
• W2013148369 cites W2055653778 @default.
• W2013148369 cites W2060024545 @default.
• W2013148369 cites W2065960770 @default.
• W2013148369 cites W2080272123 @default.
• W2013148369 cites W2081751147 @default.
• W2013148369 cites W2081893935 @default.
• W2013148369 cites W2087468929 @default.
• W2013148369 cites W2110408216 @default.
• W2013148369 cites W2121194065 @default.
• W2013148369 cites W2129309714 @default.
• W2013148369 cites W2132632471 @default.
• W2013148369 cites W2139831220 @default.
• W2013148369 cites W2148631173 @default.
• W2013148369 cites W2151738872 @default.
• W2013148369 cites W2160998626 @default.
• W2013148369 cites W22065194 @default.
• W2013148369 cites W2257793149 @default.
• W2013148369 cites W2344732003 @default.
• W2013148369 cites W2409059129 @default.
• W2013148369 cites W2412176019 @default.
• W2013148369 cites W61711944 @default.
• W2013148369 cites W87517964 @default.
• W2013148369 doi "https://doi.org/10.1002/ajh.2830390208" @default.
• W2013148369 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/1550102" @default.
• W2013148369 hasPublicationYear "1992" @default.
• W2013148369 type Work @default.
• W2013148369 sameAs 2013148369 @default.
• W2013148369 citedByCount "29" @default.
• W2013148369 countsByYear W20131483692012 @default.
• W2013148369 crossrefType "journal-article" @default.
• W2013148369 hasAuthorship W2013148369A5057321775 @default.
• W2013148369 hasConcept C12554922 @default.
• W2013148369 hasConcept C170493617 @default.
• W2013148369 hasConcept C185592680 @default.
• W2013148369 hasConcept C55493867 @default.
• W2013148369 hasConcept C79879829 @default.
• W2013148369 hasConcept C86803240 @default.
• W2013148369 hasConcept C95444343 @default.
• W2013148369 hasConceptScore W2013148369C12554922 @default.
• W2013148369 hasConceptScore W2013148369C170493617 @default.
• W2013148369 hasConceptScore W2013148369C185592680 @default.
• W2013148369 hasConceptScore W2013148369C55493867 @default.
• W2013148369 hasConceptScore W2013148369C79879829 @default.
• W2013148369 hasConceptScore W2013148369C86803240 @default.
• W2013148369 hasConceptScore W2013148369C95444343 @default.
• W2013148369 hasIssue "2" @default.
• W2013148369 hasLocation W20131483691 @default.
• W2013148369 hasLocation W20131483692 @default.
• W2013148369 hasOpenAccess W2013148369 @default.
• W2013148369 hasPrimaryLocation W20131483691 @default.
• W2013148369 hasRelatedWork W1488216507 @default.
• W2013148369 hasRelatedWork W1549554643 @default.

• next