PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 17068284-0 2007 Haptoglobin genotype is a determinant of iron, lipid peroxidation, and macrophage accumulation in the atherosclerotic plaque. Iron 41-45 haptoglobin Mus musculus 0-11 28143953-7 2017 The expression levels of hemoglobin-haptoglobin receptor CD163 and hemopexin receptor CD91 were drastically reduced in both liver and spleen, resulting in heme- and hemoglobin-derived iron elimination in urine. Iron 184-188 haptoglobin Mus musculus 36-47 28286877-3 2017 Using an unbiased proteomic approach to understand the mechanistic basis of IL-22 dependent iron retention in the host, we have identified that IL-22 induces the production of the plasma hemoglobin scavenger haptoglobin and heme scavenger hemopexin. Iron 92-96 haptoglobin Mus musculus 208-219 17919498-0 2007 Lack of haptoglobin affects iron transport across duodenum by modulating ferroportin expression. Iron 28-32 haptoglobin Mus musculus 8-19 17919498-2 2007 Haptoglobin-null mice were previously shown to have an altered heme-iron distribution, thus reproducing what occurs in humans in cases of congenital or acquired anhaptoglobinemia. Iron 68-72 haptoglobin Mus musculus 0-11 17919498-3 2007 Here, we report the analysis of iron homeostasis in haptoglobin-null mice. Iron 32-36 haptoglobin Mus musculus 52-63 17919498-7 2007 RESULTS: Analysis of intestinal iron transport reveals that haptoglobin-null mice export significantly more iron from the duodenal mucosa to plasma compared with control counterparts. Iron 32-36 haptoglobin Mus musculus 60-71 17919498-7 2007 RESULTS: Analysis of intestinal iron transport reveals that haptoglobin-null mice export significantly more iron from the duodenal mucosa to plasma compared with control counterparts. Iron 108-112 haptoglobin Mus musculus 60-71 17919498-9 2007 Up-regulation of the ferroportin transcript, but not of the protein, also occurs in haptoglobin-null spleen macrophages, which accumulate free hemoglobin-derived iron. Iron 162-166 haptoglobin Mus musculus 84-95 17919498-11 2007 CONCLUSIONS: Taking together these data, we suggest that haptoglobin, by controlling plasma levels of hemoglobin, participates in the regulation of ferroportin expression, thus contributing to the regulation of iron transfer from duodenal mucosa to plasma. Iron 211-215 haptoglobin Mus musculus 57-68 17644369-0 2007 Haptoglobin is degraded by iron in C57BL/6 mice: a possible link with endoplasmic reticulum stress. Iron 27-31 haptoglobin Mus musculus 0-11 17644369-2 2007 Haptoglobin, by virtue of its high affinity for hemoglobin, protects the tissues against hemoglobin-induced oxidative damage and allows heme iron recycling. Iron 141-145 haptoglobin Mus musculus 0-11 17644369-4 2007 Haptoglobin regulation in C57BL/6 and 129sv mice fed on an iron-rich diet for 3 weeks was thus undertaken. Iron 59-63 haptoglobin Mus musculus 0-11 17644369-5 2007 RESULTS: Iron induced a dramatic post-transcriptional decrease of liver and serum haptoglobin in C57BL/6 mice. Iron 9-13 haptoglobin Mus musculus 82-93 17644369-7 2007 We assumed that the oxidative stress induced by iron in C57BL/6 mice altered the endoplasmic reticulum (ER) environment, leading to the incorrect folding of haptoglobin and its subsequent degradation. Iron 48-52 haptoglobin Mus musculus 157-168 17644369-12 2007 CONCLUSION: Our data demonstrate that iron regulates haptoglobin synthesis in C57BL/6 mice and suggest a possible link with iron-induced ER stress. Iron 38-42 haptoglobin Mus musculus 53-64 15613548-7 2005 Here, we show that Hfe and haptoglobin compound mutant mice accumulate significantly less hepatic iron than Hfe-null mice, thus demonstrating that haptoglobin-mediated heme-iron recovery may contribute significantly to iron loading in HH. Iron 98-102 haptoglobin Mus musculus 27-38 15613548-7 2005 Here, we show that Hfe and haptoglobin compound mutant mice accumulate significantly less hepatic iron than Hfe-null mice, thus demonstrating that haptoglobin-mediated heme-iron recovery may contribute significantly to iron loading in HH. Iron 98-102 haptoglobin Mus musculus 147-158 15613548-7 2005 Here, we show that Hfe and haptoglobin compound mutant mice accumulate significantly less hepatic iron than Hfe-null mice, thus demonstrating that haptoglobin-mediated heme-iron recovery may contribute significantly to iron loading in HH. Iron 173-177 haptoglobin Mus musculus 27-38 15613548-7 2005 Here, we show that Hfe and haptoglobin compound mutant mice accumulate significantly less hepatic iron than Hfe-null mice, thus demonstrating that haptoglobin-mediated heme-iron recovery may contribute significantly to iron loading in HH. Iron 173-177 haptoglobin Mus musculus 147-158 15613548-7 2005 Here, we show that Hfe and haptoglobin compound mutant mice accumulate significantly less hepatic iron than Hfe-null mice, thus demonstrating that haptoglobin-mediated heme-iron recovery may contribute significantly to iron loading in HH. Iron 173-177 haptoglobin Mus musculus 27-38 15613548-7 2005 Here, we show that Hfe and haptoglobin compound mutant mice accumulate significantly less hepatic iron than Hfe-null mice, thus demonstrating that haptoglobin-mediated heme-iron recovery may contribute significantly to iron loading in HH. Iron 173-177 haptoglobin Mus musculus 147-158 15793279-0 2005 Plasma protein haptoglobin modulates renal iron loading. Iron 43-47 haptoglobin Mus musculus 15-26 15793279-2 2005 The strength of hemoglobin binding and the existence of a specific receptor for the haptoglobin-hemoglobin complex in the monocyte/macrophage system clearly suggest that haptoglobin may have a crucial role in heme-iron recovery. Iron 214-218 haptoglobin Mus musculus 84-95 15793279-2 2005 The strength of hemoglobin binding and the existence of a specific receptor for the haptoglobin-hemoglobin complex in the monocyte/macrophage system clearly suggest that haptoglobin may have a crucial role in heme-iron recovery. Iron 214-218 haptoglobin Mus musculus 170-181 15793279-3 2005 We used haptoglobin-null mice to evaluate the impact of haptoglobin gene inactivation on iron metabolism. Iron 89-93 haptoglobin Mus musculus 56-67 15793279-7 2005 These data demonstrate that haptoglobin crucially prevents glomerular filtration of hemoglobin and, consequently, renal iron loading during aging and following acute plasma heme-protein overload. Iron 120-124 haptoglobin Mus musculus 28-39 15662028-0 2005 Haptoglobin genotype- and diabetes-dependent differences in iron-mediated oxidative stress in vitro and in vivo. Iron 60-64 haptoglobin Mus musculus 0-11 15662028-3 2005 This antioxidant function of haptoglobin is mediated in part by the ability of haptoglobin to prevent the release of iron from hemoglobin on its binding. Iron 117-121 haptoglobin Mus musculus 29-40 15662028-3 2005 This antioxidant function of haptoglobin is mediated in part by the ability of haptoglobin to prevent the release of iron from hemoglobin on its binding. Iron 117-121 haptoglobin Mus musculus 79-90 15662028-4 2005 We hypothesized that there may be diabetes- and haptoglobin genotype-dependent differences in the amount of catalytically active redox active iron derived from hemoglobin. Iron 142-146 haptoglobin Mus musculus 48-59 15662028-6 2005 First, measuring redox active iron associated with haptoglobin-hemoglobin complexes in vitro, we demonstrate a marked increase in redox active iron associated with Hp 2-2-glycohemoglobin complexes. Iron 30-34 haptoglobin Mus musculus 51-62 15662028-6 2005 First, measuring redox active iron associated with haptoglobin-hemoglobin complexes in vitro, we demonstrate a marked increase in redox active iron associated with Hp 2-2-glycohemoglobin complexes. Iron 143-147 haptoglobin Mus musculus 51-62 12420740-6 2002 Since the use of DEN is known to lead to the production of lipid peroxidation products which facilitate this reaction and haptoglobin is an acute phase reactant, acting as a radical scavenger against hemoglobin or iron stimulated lipid peroxidation, a relationship between the glycosylation of haptoglobin and the suppression of hepatoma development can not be ruled out. Iron 214-218 haptoglobin Mus musculus 122-133 12420740-6 2002 Since the use of DEN is known to lead to the production of lipid peroxidation products which facilitate this reaction and haptoglobin is an acute phase reactant, acting as a radical scavenger against hemoglobin or iron stimulated lipid peroxidation, a relationship between the glycosylation of haptoglobin and the suppression of hepatoma development can not be ruled out. Iron 214-218 haptoglobin Mus musculus 294-305