PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 20610401-9 2010 Together, these data argue that hemopexin has a role in assuring systemic iron balance during homeostasis in addition to its established role as a scavenger during internal bleeding or hemolysis. Iron 74-78 hemopexin Homo sapiens 32-41 23350672-3 2013 Human amyloid precursor protein (hAPP), needed for iron export from neurons, is induced ~twofold after heme-hemopexin endocytosis by iron from heme catabolism via the iron-regulatory element of hAPP mRNA. Iron 51-55 hemopexin Homo sapiens 108-117 23350672-3 2013 Human amyloid precursor protein (hAPP), needed for iron export from neurons, is induced ~twofold after heme-hemopexin endocytosis by iron from heme catabolism via the iron-regulatory element of hAPP mRNA. Iron 133-137 hemopexin Homo sapiens 108-117 23350672-3 2013 Human amyloid precursor protein (hAPP), needed for iron export from neurons, is induced ~twofold after heme-hemopexin endocytosis by iron from heme catabolism via the iron-regulatory element of hAPP mRNA. Iron 133-137 hemopexin Homo sapiens 108-117 23350672-8 2013 Hemopexin sequesters heme, thus preventing unregulated heme uptake that leads to toxicity; it safely delivers heme to neuronal cells; and it activates the induction of proteins including HO1 and hAPP that keep heme and iron at safe levels in neurons. Iron 219-223 hemopexin Homo sapiens 0-9 22033148-2 2012 Iron proteins influencing the innate immune response include hepcidin, lactoferrin, siderocalin, haptoglobin, hemopexin, Nramp1, ferroportin and the transferrin receptor. Iron 0-4 hemopexin Homo sapiens 110-119 23350672-0 2013 Mechanisms of neuroprotection by hemopexin: modeling the control of heme and iron homeostasis in brain neurons in inflammatory states. Iron 77-81 hemopexin Homo sapiens 33-42 11229523-9 2000 Redox processes at the cell surface, which generate cuprous ions, are involved in the regulation of the MT-1 and HO-1 genes by heme-hemopexin before heme catabolism and intracellular release of iron. Iron 194-198 hemopexin Homo sapiens 132-141 17712531-1 2008 Hemopexin (HPX) has two principal roles: it sequesters free heme in vivo for the purpose of preventing the toxic effects of this moiety, which is largely due to heme"s ability to catalyze free radical formation, and it transports heme intracellularly thus limiting its availability as an iron source for pathogens. Iron 288-292 hemopexin Homo sapiens 0-9 12175942-0 2002 The heme-iron geometry of ferrous nitrosylated heme-serum lipoproteins, hemopexin, and albumin: a comparative EPR study. Iron 9-13 hemopexin Homo sapiens 72-81 11934617-2 2002 Some bacteria also use iron in heme, hemoglobin, hemopexin, transferrin and lactoferrin of eukaryotic hosts. Iron 23-27 hemopexin Homo sapiens 49-58 12642662-3 2003 Comparison of the structure and function of transferrins with a completely unrelated protein hemopexin, which carries out the same function for heme, identifies molecular features that contribute to a successful protein system for iron acquisition, transport, and release. Iron 231-235 hemopexin Homo sapiens 93-102 12042069-4 2002 The binding strength between heme and HPX, and the presence of a specific heme-HPX receptor able to catabolize the complex and to induce intracellular antioxidant activities, suggest that hemopexin is the major vehicle for the transportation of heme in the plasma, thus preventing heme-mediated oxidative stress and heme-bound iron loss. Iron 327-331 hemopexin Homo sapiens 79-82 12042069-4 2002 The binding strength between heme and HPX, and the presence of a specific heme-HPX receptor able to catabolize the complex and to induce intracellular antioxidant activities, suggest that hemopexin is the major vehicle for the transportation of heme in the plasma, thus preventing heme-mediated oxidative stress and heme-bound iron loss. Iron 327-331 hemopexin Homo sapiens 188-197 12042069-5 2002 In this review, we discuss the experimental data that support this view and show that the most important physiological role of HPX is to act as an antioxidant after blood heme overload, rather than to participate in iron metabolism. Iron 216-220 hemopexin Homo sapiens 127-130 11563695-0 2001 Effects of reduction and ligation of heme iron on the thermal stability of heme-hemopexin complexes. Iron 42-46 hemopexin Homo sapiens 80-89 9168799-12 1997 Thus, heme-hemopexin not only functions as an iron source for T-cells but occupancy of the hemopexin receptor itself triggers signaling pathway(s) involved in the regulation of cell growth. Iron 46-50 hemopexin Homo sapiens 11-20 10504726-3 1999 For protection, especially in conditions of trauma, inflammation and hemolysis, and to maintain iron homeostasis, a high-affinity binding protein, hemopexin, is required. Iron 96-100 hemopexin Homo sapiens 147-156 8087243-7 1994 This injury is dependent on the iron content of heme and is completely blocked when concomitant hemopexin is added. Iron 32-36 hemopexin Homo sapiens 96-105 7768617-1 1995 Haemophilus influenzae can acquire heme from hemopexin for use as a source of both essential porphyrin and iron. Iron 107-111 hemopexin Homo sapiens 45-54 7768617-2 1995 In classical ligand-binding studies, we observed time-dependent, saturable, and displaceable binding of human 125I-labelled hemopexin to intact cells of H. influenzae type b (Hib) strain 760705 grown in an iron-restricted medium. Iron 206-210 hemopexin Homo sapiens 124-133 8647926-8 1996 It is concluded, first, that toxic effects of iron and heme can be prevented by apo-transferrin or apo-hemopexin and, second, that exposure of RPE cells to free heme or hemopexin sets in motion a series of biochemical events resulting in protection against oxidative stress. Iron 46-50 hemopexin Homo sapiens 103-112 8647926-8 1996 It is concluded, first, that toxic effects of iron and heme can be prevented by apo-transferrin or apo-hemopexin and, second, that exposure of RPE cells to free heme or hemopexin sets in motion a series of biochemical events resulting in protection against oxidative stress. Iron 46-50 hemopexin Homo sapiens 169-178 8078898-0 1994 Roles of heme iron-coordinating histidine residues of human hemopexin expressed in baculovirus-infected insect cells. Iron 14-18 hemopexin Homo sapiens 60-69 8078898-9 1994 1H NMR data indicate that each of the single-mutant heme-Hx complexes is predominantly low-spin, perhaps owing to coordination of the heme iron by the Thr side-chain oxygen or water oxygen coordinating to the iron. Iron 139-143 hemopexin Homo sapiens 57-59 8078898-9 1994 1H NMR data indicate that each of the single-mutant heme-Hx complexes is predominantly low-spin, perhaps owing to coordination of the heme iron by the Thr side-chain oxygen or water oxygen coordinating to the iron. Iron 209-213 hemopexin Homo sapiens 57-59 1847276-3 1991 Iron can be taken up by the liver in several forms and by several pathways including: (1) receptor-mediated endocytosis of diferric or monoferric transferrin or ferritin, (2) reduction and carrier-facilitated internalization of iron from transferrin without internalization of the protein moiety of transferrin, (3) electrogenic uptake of low molecular weight, non-protein bound forms of iron, and (4) uptake of heme from heme-albumin, heme-hemopexin, or hemoglobin-haptoglobin complexes. Iron 0-4 hemopexin Homo sapiens 441-450 1644822-15 1992 The concomitant regulation of gene expression of MT-1 and HO in response to heme-hemopexin appears to be a concerted adaptive response of the cells, mediated at the level of the plasma membrane hemopexin receptor, and may relate to the proposed role of MT as an intracellular antioxidant or to a need to sequester zinc which otherwise would compete with iron and occupy sites on regulatory proteins such as the iron-responsive elements. Iron 354-358 hemopexin Homo sapiens 81-90 1644822-15 1992 The concomitant regulation of gene expression of MT-1 and HO in response to heme-hemopexin appears to be a concerted adaptive response of the cells, mediated at the level of the plasma membrane hemopexin receptor, and may relate to the proposed role of MT as an intracellular antioxidant or to a need to sequester zinc which otherwise would compete with iron and occupy sites on regulatory proteins such as the iron-responsive elements. Iron 411-415 hemopexin Homo sapiens 81-90 34583348-7 2021 A cross-sectional study was conducted to determine the association between plasma levels of free heme, HO-1, Hp, Hx, and malaria status in pregnant women who received routine iron supplementation and their birth outcomes. Iron 175-179 hemopexin Homo sapiens 113-115 2380200-1 1990 To investigate the regulation mechanism of the uptake of iron and heme iron by the cells and intracellular utilization of iron, we examined the interaction between iron uptake from transferrin and hemopexin-mediated uptake of heme by human leukemic U937 cells or HeLa cells. Iron 57-61 hemopexin Homo sapiens 197-206 2380200-4 1990 Treatment of both species of cells with hemopexin led to a rapid decrease in iron uptake from transferrin in a hemopexin dose-dependent manner, and the decrease seen in case of treatment with hemin was less than that seen with hemopexin. Iron 77-81 hemopexin Homo sapiens 40-49 2380200-4 1990 Treatment of both species of cells with hemopexin led to a rapid decrease in iron uptake from transferrin in a hemopexin dose-dependent manner, and the decrease seen in case of treatment with hemin was less than that seen with hemopexin. Iron 77-81 hemopexin Homo sapiens 111-120 2380200-4 1990 Treatment of both species of cells with hemopexin led to a rapid decrease in iron uptake from transferrin in a hemopexin dose-dependent manner, and the decrease seen in case of treatment with hemin was less than that seen with hemopexin. Iron 77-81 hemopexin Homo sapiens 111-120 2380200-5 1990 The decrease of iron uptake by hemopexin contributed to a decrease in cell surface transferrin receptors on hemopexin-treated cells. Iron 16-20 hemopexin Homo sapiens 31-40 2380200-5 1990 The decrease of iron uptake by hemopexin contributed to a decrease in cell surface transferrin receptors on hemopexin-treated cells. Iron 16-20 hemopexin Homo sapiens 108-117 3855550-1 1985 We have determined the complete primary structure of human hemopexin, a plasma beta-glycoprotein that specifically binds one heme with high affinity and transports it to hepatocytes for salvage of the iron. Iron 201-205 hemopexin Homo sapiens 59-68 3047970-1 1988 Problems of ferrokinetics, participation of metalloproteins transferrin, ferritin and lactoferrin in metabolism of iron at the step of the metal absorption, transport of iron by means of transferrin, haptoglobin and hemopexin, interaction of transferrin with reticulocytes, deposition of iron in ferritin, mobilization of iron from ferritin via ceruloplasmin are considered. Iron 115-119 hemopexin Homo sapiens 216-225 3031028-7 1987 When myeloperoxidase was isolated from the cells incubated with [59Fe]heme-hemopexin complex by immunoprecipitation with anti-myeloperoxidase antibody, radiolabeled iron associated with myeloperoxidase increased with time, and more than 30% of the radioactivity in the cells was present in the myeloperoxidase. Iron 165-169 hemopexin Homo sapiens 75-84 3533647-6 1986 Hepatocytes also obtain some iron from haptoglobin-hemoglobin, heme-hemopexin, and ferritin (Fn), in each case by interaction with membrane receptors and endocytosis. Iron 29-33 hemopexin Homo sapiens 68-77 4100308-2 1971 This distinctive reaction is characteristic of a coordination complex with heme iron, and is ascribed to a remarkable affinity for heme of certain plasma glycoglobulins, which include hemopexin. Iron 80-84 hemopexin Homo sapiens 184-193 31554244-5 2019 Heme toxicity, which may lead to iron toxicity, is recognized increasingly in a wide range of conditions involving hemolysis and immune system activation and, in this review, we highlight some newly identified actions of heme and hemopexin especially in situations where normal processes fail to maintain heme and iron homeostasis. Iron 33-37 hemopexin Homo sapiens 230-239 4188269-2 1970 In normal subjects, injected heme-(59)Fe was bound immediately by albumin and the beta(1)-globulin, hemopexin. Iron 38-40 hemopexin Homo sapiens 100-109 33392254-3 2020 Hemopexin both detoxifies heme to maintain iron homeostasis and bolsters antioxidant capacity via catabolic products, biliverdin and carbon monoxide to combat iron-mediated lipid peroxidation. Iron 43-47 hemopexin Homo sapiens 0-9 33392254-3 2020 Hemopexin both detoxifies heme to maintain iron homeostasis and bolsters antioxidant capacity via catabolic products, biliverdin and carbon monoxide to combat iron-mediated lipid peroxidation. Iron 159-163 hemopexin Homo sapiens 0-9 31554244-5 2019 Heme toxicity, which may lead to iron toxicity, is recognized increasingly in a wide range of conditions involving hemolysis and immune system activation and, in this review, we highlight some newly identified actions of heme and hemopexin especially in situations where normal processes fail to maintain heme and iron homeostasis. Iron 314-318 hemopexin Homo sapiens 230-239 30281034-5 2018 Tf, Hpx and Hp are being developed for hematological disorders where iron, hemin and Hb contribute to pathophysiology. Iron 69-73 hemopexin Homo sapiens 4-7 31011852-0 2019 Safe coordinated trafficking of heme and iron with copper maintain cell homeostasis: modules from the hemopexin system. Iron 41-45 hemopexin Homo sapiens 102-111 31011852-3 2019 Heme-hemopexin endocytosis leads to coordinated trafficking of heme, iron and copper as heme traffics from endosomes to heme oxygenases (HOs) in the smooth endoplasmic reticulum and to the nucleus. Iron 69-73 hemopexin Homo sapiens 5-14 29070546-4 2017 Key players in mammalian iron trafficking include several types of cells important to iron acquisition, homeostasis, and hematopoiesis (enterocytes, hepatocytes, macrophages, hematopoietic cells, and in the case of pregnancy, placental syncytiotrophoblast cells) and several forms of chaperone proteins, including, for nonheme iron, the transport protein transferrin and the intracellular iron-storage protein ferritin, and for heme iron, the chaperone proteins haptoglobin and hemopexin. Iron 25-29 hemopexin Homo sapiens 478-487 25732555-5 2015 In several pathological conditions in which free heme-Fe levels increase, the buffering capacity of plasma hemopexin is overwhelmed and most of heme-Fe binds to the fatty acid site 1 of HSA. Iron 54-56 hemopexin Homo sapiens 107-116 24344252-4 2014 Both WAP65 and HPX have been associated with iron homeostasis due to the affinity to bind the toxic-free heme circulating in the blood stream. Iron 45-49 hemopexin Homo sapiens 15-18 26768209-7 2016 The intracranial CD91-hemopexin system was active after SAH because CD91 positively correlated with iron deposition in brain tissue. Iron 100-104 hemopexin Homo sapiens 22-31