Cytoprotective Effects of Heme Oxygenase in Acute Renal Failure

Akagi, Reiko; Takahashi, Toru; Sassa, Shigeru

doi:10.1159/000086044

Cited by 53Heme Oxygenase-1 and Carbon MonoxideAcute Kidney Injury ResearchHemoglobin structure and function

Cytoprotective Effects of Heme Oxygenase in Acute Renal Failure

Akagi, Reiko, Takahashi, Toru, Sassa, Shigeru·2005·Contributions to Nephrology

DOI 10.1159/000086044

Open this paper in CoChat — free account

Abstract

Following ischemia, superoxide is produced during the reperfusion phase in various organs. In renal pathophysiology, excess of free heme, which is released from hemeproteins under these conditions, catalyzes the formation of further reactive oxygen species to accelerate cellular injuries. There is accumulating evidence suggesting that transcriptional activation of heme oxygenase (HO)-1, the rate-limiting enzyme in heme degradation as well as the 32-kDa heat shock protein, participates in the defense against oxidative tissue injuries. Ischemia followed by reperfusion of the rat kidney accompanies significant induction of HO-1 mRNA, protein and enzyme activity, which is in part mediated through a rapid and transient increase in microsomal heme concentration. Inhibition of HO activity by tin mesoporphyrin results in a sustained and enhanced increase in microsomal heme content, and significantly exacerbates renal function. In contrast, SnCl2 treatment, which specifically induces HO-1 mRNA and protein in the proximal tubular epithelial cells, prevents the ischemia-reperfusion-mediated increase in microsomal heme concentration, and ameliorates the ischemic renal injury. In addition to these findings, recent evidence on the role of HO-1 in the kidney pathophysiology is summarized, with a particular emphasis on its protective role in the ischemic acute renal failure.

Integrity signals

Registry

Crossref · 10.1159/000086044

Cites

85 of 85 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Exogenously administered NGAL markedly upregulates heme oxygenase-1, a protective agent in experimental acute kidney injury.
“Exogenously administered NGAL also markedly upregulates heme oxygenase-1, a proven multifunctional protective agent in experimental Acute Kidney Injury (AKI) that is thought to work by limiting iron uptake, promoting intracellular iron release, enhancing production of antioxidants such as biliverdin and carbon monoxide, and inducing the cell cycle regulatory protein p21 [279,395,396].”
From Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases (2009) · cites this paper as [279]

Bilirubin Is an Antioxidant of Possible Physiological Importance
Stocker, R., Yamamoto, Y., McDonagh, A. F., Glazer, A. N., & Ames, B. N. (1987) · Science · doi:10.1126/science.3029864 · Cited by 3,502 · see citing works
Carbon monoxide has anti-inflammatory effects involving the mitogen-activated protein kinase pathway
Otterbein, L. E., Bach, F. H., Alam, J., Soares, M., Tao Lu, H., Wysk, M., Davis, R. J., Flavell, R. A., & Choi, A. M. K. (2000) · Nature Medicine · doi:10.1038/74680 · Cited by 2,153 · see citing works
The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase.
Tenhunen, R., Marver, H. S., & Schmid, R. (1968) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.61.2.748 · Cited by 1,803 · see citing works
Heme oxygenase: Function, multiplicity, regulatory mechanisms, and clinical applications
Maines, M. D. (1988) · The FASEB Journal · doi:10.1096/fasebj.2.10.3290025 · Cited by 1,707 · see citing works
Transcription Factor Nrf2 Coordinately Regulates a Group of Oxidative Stress-inducible Genes in Macrophages
Ishii, T., Itoh, K., Takahashi, S., Sato, H., Yanagawa, T., Katoh, Y., Bannai, S., & Yamamoto, M. P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.21.16023 · Cited by 1,460 · see citing works
Reduced stress defense in heme oxygenase 1-deficient cells
Poss, K. D., & Tonegawa, S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.20.10925 · Cited by 1,293 · see citing works
Nrf2, a Cap'n'Collar Transcription Factor, Regulates Induction of the Heme Oxygenase-1 Gene
Alam, J., Stewart, D. P., Touchard, C. L., Boinapally, S., Choi, A. M. K., & Cook, J. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.37.26071 · Cited by 1,284 · see citing works
Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite.
Keyse, S. M., & Tyrrell, R. M. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.1.99 · Cited by 1,271 · see citing works
Oxidative stress causes enhanced endothelial cell injury in human heme oxygenase-1 deficiency
Yachie, A., Niida, Y., Wada, T., Igarashi, N., Kaneda, H., Toma, T., Ohta, K., Kasahara, Y., & Koizumi, S. (1999) · Journal of Clinical Investigation · doi:10.1172/jci4165 · Cited by 1,256 · see citing works
Biliverdin reductase: A major physiologic cytoprotectant
Barañano, D. E., Rao, M., Ferris, C. D., & Snyder, S. H. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252626999 · Cited by 1,091 · see citing works
Heme oxygenase 1 is required for mammalian iron reutilization
Poss, K. D., & Tonegawa, S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.20.10919 · Cited by 1,016 · see citing works
Heme oxygenase: colors of defense against cellular stress
Otterbein, L. E., & Choi, A. M. K. (2000) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.2000.279.6.l1029 · Cited by 870 · see citing works
Acute renal failure in intensive care units--Causes, outcome, and prognostic factors of hospital mortality
Brivet, F. G., Kleinknecht, D., Loirat, P., & Landais, P. (1996) · Critical Care Medicine · doi:10.1097/00003246-199602000-00003 · Cited by 859 · see citing works
Isolation and Characterization of a cDNA from the Rat Brain that Encodes Hemoprotein Heme Oxygenase‐3
McCoubrey, W. K., Huang, T. J., & Maines, M. D. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.00725.x · Cited by 823 · see citing works
Induction of heme oxygenase is a rapid, protective response in rhabdomyolysis in the rat.
Nath, K. A., Balla, G., Vercellotti, G. M., Balla, J., Jacob, H. S., Levitt, M. D., & Rosenberg, M. E. (1992) · Journal of Clinical Investigation · doi:10.1172/jci115847 · Cited by 685 · see citing works
Bach Proteins Belong to a Novel Family of BTB-Basic Leucine Zipper Transcription Factors That Interact with MafK and Regulate Transcription through the NF-E2 Site
Oyake, T., Itoh, K., Motohashi, H., Hayashi, N., Hoshino, H., Nishizawa, M., Yamamoto, M. P., & Igarashi, K. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.11.6083 · Cited by 656 · see citing works
Hemoprotein Bach1 regulates enhancer availability of heme oxygenase‐1 gene
Sun, J., Hoshino, H., Takaku, K., Nakajima, O., Muto, A., Suzuki, H., Tashiro, S., Takahashi, S., Shibahara, S., Alam, J., et al. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf516 · Cited by 637 · see citing works
Heme mediates derepression of Maf recognition element through direct binding to transcription repressor Bach1
Ogawa, K., Sun, J., Taketani, S., Nakajima, O., Nishitani, C., Sassa, S., Hayashi, N., Yamamoto, M., Shibahara, S., Fujita, H., et al. (2001) · The EMBO Journal · doi:10.1093/emboj/20.11.2835 · Cited by 532 · see citing works
Self-citation
Haem oxygenase-1 prevents cell death by regulating cellular iron
Ferris, C. D., Jaffrey, S. R., Sawa, A., Takahashi, M., Brady, S. D., Barrow, R. K., Tysoe, S. A., Wolosker, H., Barañano, D. E., Doré, S., et al. (1999) · Nature Cell Biology · doi:10.1038/11072 · Cited by 509 · see citing works
Carbon Monoxide Generated by Heme Oxygenase-1 Suppresses the Rejection of Mouse-to-Rat Cardiac Transplants
Sato, K., Balla, J., Otterbein, L. E., Smith, R. N., Brouard, S., Lin, Y., Csizmadia, E., Sévigny, J., Robson, S. C., Vercellotti, G. M., et al. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.6.4185 · Cited by 462 · see citing works
The spectrum of acute renal failure in the intensive care unit compared with that seen in other settings. The Madrid Acute Renal Failure Study Group.
Liaño, F., Junco, E., Pascual, J., Madero, R., & Verde, E. (1998) · PubMed · Cited by 442 · see citing works
Maf nuclear oncoprotein recognizes sequences related to an AP-1 site and forms heterodimers with both Fos and Jun
Kataoka, K., Noda, M., & Nishizawa, M. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.1.700 · Cited by 436 · see citing works
Heme is a potent inducer of inflammation in mice and is counteracted by heme oxygenase
Wagener, F. A. D. T. G., Eggert, A. O., Boerman, O. C., Oyen, W. J. G., Verhofstad, A. A. J., Abraham, N. G., Adema, G. J., van Kooyk, Y., de Witte, T., & Figdor, C. G. (2001) · Blood · doi:10.1182/blood.v98.6.1802 · Cited by 423 · see citing works
Transcriptional control of rat heme oxygenase by heat shock.
Shibahara, S., Müller, R., & Taguchi, H. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45138-1 · Cited by 415 · see citing works
Nrf2 Transcription Factor, a Novel Target of Keratinocyte Growth Factor Action Which Regulates Gene Expression and Inflammation in the Healing Skin Wound
Braun, S., Hanselmann, C., Gassmann, M. G., auf dem Keller, U., Born-Berclaz, C., Chan, K., Kan, Y. W., & Werner, S. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.15.5492-5505.2002 · Cited by 410 · see citing works
Nitric oxide: a mediator in rat tubularhypoxia/reoxygenation injury.
Yu, L., Gengaro, P. E., Niederberger, M., Burke, T. J., & Schrier, R. W. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.5.1691 · Cited by 318 · see citing works
Exposure of endothelial cells to free heme potentiates damage mediated by granulocytes and toxic oxygen species.
Balla, G., Vercellotti, G. M., Müller‐Eberhard, U., Eaton, J. W., & Jacob, H. S. (1991) · PubMed · Cited by 298 · see citing works
The Indispensability of Heme Oxygenase-1 in Protecting against Acute Heme Protein-Induced Toxicity in Vivo
Nath, K. A., Haggard, J. J., Croatt, A. J., Grande, J. P., Poss, K. D., & Alam, J. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65024-9 · Cited by 263 · see citing works
Induction of heme oxygenase in toxic renal injury: A protective role in cisplatin nephrotoxicity in the rat
Agarwal, A., Balla, J., Alam, J., et al. (1995) · Kidney International · doi:10.1038/ki.1995.414 · Cited by 262 · see citing works
Transcriptional Activation of the Heme Oxygenase Gene by Heme and Cadmium in Mouse Hepatoma Cells
Alam, J., Shibahara, S., & Smith, A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83358-0 · Cited by 226 · see citing works
A Prospective, Multicenter Study of the Epidemiology, Management, and Outcome of Severe Acute Renal Failure in a “Closed” ICU System
Cole, L., Bellomo, R., Silvester, W., & JOHN H.REEVES for th e Victorian Severe Acute Renal Failure Study Group (2000) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.162.1.9907016 · Cited by 215 · see citing works
Oxygen toxicity and iron accumulation in the lungs of mice lacking heme oxygenase-2.
Dennery, P. A., Spitz, D. R., Yang, G., Tatarov, A., Lee, C. S., Shegog, M., & Poss, K. D. (1998) · Journal of Clinical Investigation · doi:10.1172/jci448 · Cited by 212 · see citing works
Nucleotide sequence and organization of the rat heme oxygenase gene.
Müller, R., Taguchi, H., & Shibahara, S. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48315-9 · Cited by 207 · see citing works
Studies on the mechanism of induction of haem oxygenase by cobalt and other metal ions
Maines, M. D., & Kappas, A. (1976) · Biochemical Journal · doi:10.1042/bj1540125 · Cited by 202 · see citing works
The Heme-Responsive Element of the Mouse Heme Oxygenase-1 Gene Is an Extended AP-1 Binding Site That Resembles the Recognition Sequences for MAF and NF-E2 Transcription Factors
Inamdar, N. M., Ahn, Y. I., & Alam, J. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.0637 · Cited by 194 · see citing works
Multivalent DNA Binding Complex Generated by Small Maf and Bach1 as a Possible Biochemical Basis for β-Globin Locus Control Region Complex
Igarashi, K., Hoshino, H., Muto, A., Suwabe, N., Nishikawa, S., Nakauchi, H., & Yamamoto, M. P. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.19.11783 · Cited by 191 · see citing works
Protective effect of heme oxygenase induction in ischemic acute renal failure
Shimizu, H., Takahashi, T., Suzuki, T., et al. (2000) · Critical Care Medicine · doi:10.1097/00003246-200003000-00033 · Cited by 185 · see citing works
Self-citation
Induction of kidney heme oxygenase-1 (HSP32) mRNA and protein by ischemia/reperfusion: possible role of heme as both promotor of tissue damage and regulator of HSP32.
Maines, M. D., Mayer, R., Ewing, J. F., & McCoubrey, W. K. (1993) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(25)10290-5 · Cited by 182 · see citing works
Control of Jaundice in Preterm Newborns by an Inhibitor of Bilirubin Production: Studies With Tin-Mesoporphyrin
Valaes, T., Petmezaki, S., Henschke, C. I., et al. (1994) · PEDIATRICS · doi:10.1542/peds.93.1.1 · Cited by 179 · see citing works
Bilirubin attenuates radical‐mediated damage to serum albumin
Neužil, J., & Stocker, R. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80353-v · Cited by 176 · see citing works
Acquired resistance to acute oxidative stress. Possible role of heme oxygenase and ferritin.
Vogt, B. A., Alam, J., Croatt, A. J., Vercellotti, G. M., & Nath, K. A. (1995) · PubMed · Cited by 168 · see citing works
Regulation of Heme Oxygenase-1 by Redox Signals Involving Nitric Oxide
Motterlini, R., Green, C. J., & Foresti, R. (2002) · Antioxidants and Redox Signaling · doi:10.1089/15230860260220111 · Cited by 150 · see citing works
Control of heme metabolism with synthetic metalloporphyrins.
Kappas, A., & Drummond, G. S. (1986) · Journal of Clinical Investigation · doi:10.1172/jci112309 · Cited by 145 · see citing works
Regulation of human heme oxygenase-1 gene expression under thermal stress
Okinaga, S., Takahashi, K., Takeda, K., et al. (1996) · Blood · doi:10.1182/blood.v87.12.5074.bloodjournal87125074 · Cited by 135 · see citing works
Transcriptional Activation of the HO-1 Gene by Lipopolysaccharide Is Mediated by 5′ Distal Enhancers: Role of Reactive Oxygen Intermediates and AP-1
Camhi, S. L., Alam, J., Wiegand, G. W., Chin, B. Y., & Choi, A. M. K. (1998) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.18.2.2910 · Cited by 130 · see citing works
Intracellular targets in heme protein-induced renal injury
Nath, K. A., Grande, J. P., Croatt, A. J., Likely, S., Hebbel, R. P., & Enright, H. (1998) · Kidney International · doi:10.1046/j.1523-1755.1998.00731.x · Cited by 127 · see citing works
Recovery from postischemic acute renal failure in the rat
Finn, W. F., & Chevalier, R. L. (1979) · Kidney International · doi:10.1038/ki.1979.112 · Cited by 121 · see citing works
Pathobiology of heme interaction with the erythrocyte membrane.
Hebbel, R. P., & Eaton, J. W. (1989) · PubMed · Cited by 120 · see citing works
Glomerular inflammation induces resistance to tubular injury in the rat. A novel form of acquired, heme oxygenase-dependent resistance to renal injury.
Vogt, B. A., Shanley, T. P., Croatt, A. J., et al. (1996) · Journal of Clinical Investigation · doi:10.1172/jci119020 · Cited by 120 · see citing works
Regulation of heme oxygenase gene expression.
Shibahara, S. (1988) · PubMed · Cited by 111 · see citing works
Tin: A Potent Inducer of Heme Oxygenase in Kidney
Kappas, A., & Maines, M. D. (1976) · Science · doi:10.1126/science.1257757 · Cited by 108 · see citing works
Heme Oxygenase-1 Induction Attenuates Inducible Nitric Oxide Synthase Expression and Proteinuria in Glomerulonephritis
Datta, P. K., Koukouritaki, S. B., Hopp, K. A., & Lianos, E. A. (1999) · Journal of the American Society of Nephrology · doi:10.1681/asn.v10122540 · Cited by 108 · see citing works
Tubular injury as a cardinal pathologic feature in human heme oxygenase-1 deficiency
Ohta, K., Yachie, A., Fujimoto, K., Kaneda, H., Wada, T., Toma, T., Seno, A., Kasahara, Y., Yokoyama, H., Seki, H., et al. (2000) · American Journal of Kidney Diseases · doi:10.1016/s0272-6386(00)70256-3 · Cited by 107 · see citing works
Exacerbation of Chronic Renovascular Hypertension and Acute Renal Failure in Heme Oxygenase-1–Deficient Mice
Wiesel, P., Patel, A. P., Carvajal, I. M., Wang, Z. Y., Pellacani, A. U. E., Maemura, K., DiFonzo, N., Rennke, H. G., Layne, M. D., Yet, S., et al. (2001) · Circulation Research · doi:10.1161/hh1001.091521 · Cited by 101 · see citing works
TGF-β1stimulates HO-1 via the p38 mitogen-activated protein kinase in A549 pulmonary epithelial cells
Ning, W., Song, R., Li, C., Park, E., Mohsenin, A., Choi, A. M. K., & Choi, M. E. (2002) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00151.2002 · Cited by 101 · see citing works
Reduction of the C2 and C4 vinyl groups of Sn-protoporphyrin to form Sn-mesoporphyrin markedly enhances the ability of the metalloporphyrin to inhibit in vivo heme catabolism
Drummond, G. S., Galbraith, R. A., Sardana, M. K., et al. (1987) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(87)90294-3 · Cited by 96 · see citing works
Heme biosynthesis and drug metabolism in mice with hereditary hemolytic anemia. Heme oxygenase induction as an adaptive response for maintaining cytochrome P-450 in chronic hemolysis.
Sassa, S., Kappas, A., Bernstein, S. E., et al. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37866-3 · Cited by 95 · see citing works
Self-citation
Transitory Renal Failure Following Rapid Administration of a Relatively Large Amount of Hematin in a Patient with Acute Intermittent Porphyria in Clinical Remission
Dhar, G. J., Bossenmaier, I. C., Cardinal, R. A., et al. (1978) · Acta Medica Scandinavica · doi:10.1111/j.0954-6820.1978.tb14903.x · Cited by 84 · see citing works
Systemic Rather Than Local Heme Oxygenase-1 Overexpression Improves Cardiac Allograft Outcomes in a New Transgenic Mouse
Araujo, J. A., Meng, L., Tward, A. D., et al. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.3.1572 · Cited by 82 · see citing works
Nitric oxide induces heme oxygenase-1 gene expression in mesangial cells
Datta, P. K., & Lianos, E. A. (1999) · Kidney International · doi:10.1046/j.1523-1755.1999.00429.x · Cited by 82 · see citing works
Heme oxygenase is a positive acute-phase reactant in human Hep3B hepatoma cells
Mitani, K., Fujita, H., Kappas, A., et al. (1992) · Blood · doi:10.1182/blood.v79.5.1255.1255 · Cited by 79 · see citing works
Platelet-Derived Growth Factor Stimulates Heme Oxygenase-1 Gene Expression and Carbon Monoxide Production in Vascular Smooth Muscle Cells
Durante, W., Peyton, K. J., & Schafer, A. I. (1999) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.19.11.2666 · Cited by 76 · see citing works
Heme oxygenase-1 fused to a TAT peptide transduces and protects pancreatic β-cells
Ribeiro, M., Klein, D., Pileggi, A., Molano, R., Fraker, C., Ricordi, C., Inverardi, L., & Pastori, R. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00856-8 · Cited by 65 · see citing works
A comparative study of heme degradation by NADPH-cytochrome c reductase alone and by the complete heme oxygenase system. Distinctive aspects of heme degradation by NADPH-cytochrome c reductase.
Yoshinaga, T., Sassa, S., & Kappas, A. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34451-x · Cited by 61 · see citing works
Self-citation
Interaction of upstream stimulatory factor with the human heme oxygenase gene promoter
Sato, M., Ishizawa, S., Yoshida, T., et al. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb15394.x · Cited by 61 · see citing works
Identification of a cis-Regulatory Element and Putative trans-Acting Factors Responsible for 12-O-Tetradecanoylphorbol-13-Acetate (TPA)-Mediated Induction of Heme Oxygenase Expression in Myelomonocytic Cell Lines
Muraosa, Y., & Shibahara, S. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.12.7881 · Cited by 57 · see citing works
Acute cholestatic liver disease protects against glycerol-induced acute renal failure in the rat
Leung, N., Croatt, A. J., Haggard, J. J., et al. (2001) · Kidney International · doi:10.1046/j.1523-1755.2001.0600031047.x · Cited by 50 · see citing works
Tin chloride pretreatment prevents renal injury in rats with ischemic acute renal failure
Toda, N., Takahashi, T., Mizobuchi, S., et al. (2002) · Critical Care Medicine · doi:10.1097/00003246-200207000-00020 · Cited by 50 · see citing works
Self-citation
Identification of a nuclear protein that constitutively recognizes the sequence containing a heat‐shock element
Okinaga, S., & SHBAHARA, S. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb17647.x · Cited by 49 · see citing works
GENE TRANSFER OF IMMUNOMODULATORY PEPTIDES CORRELATES WITH HEME OXYGENASE-1 INDUCTION AND ENHANCED ALLOGRAFT SURVIVAL 1
DeBruyne, L. A., Magee, J. C., Buelow, R., et al. (2000) · Transplantation · doi:10.1097/00007890-200001150-00021 · Cited by 44 · see citing works
Tissue-specific gene expression of heme oxygenase-1 (HO-1) and non-specific δ-aminolevulinate synthase (ALAS-N) in a rat model of septic multiple organ dysfunction syndrome
Suzuki, T., Takahashi, T., Yamasaki, A., Fujiwara, T., Hirakawa, M., & Akagi, R. (2000) · Biochemical Pharmacology · doi:10.1016/s0006-2952(00)00324-5 · Cited by 43 · see citing works
Self-citation
Tumor promoters increase the synthesis of a 32,000-dalton protein in BALB/c 3T3 cells.
Hiwasa, T., Fujimura, S., & Sakiyama, S. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.6.1800 · Cited by 40 · see citing works
Metal Induction of Heme Oxygenasea
Sunderman, F. W. (1987) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1987.tb48762.x · Cited by 40 · see citing works
Pyrrolidine dithiocarbamate provides protection against hypothermic preservation and transplantation injury in the rat liver: The role of heme oxygenase-1
Tsuchihashi, S.-I., Tamaki, T., Tanaka, M., et al. (2003) · Surgery · doi:10.1067/msy.2003.124 · Cited by 39 · see citing works
Heme protein-induced tubular cytoresistance: Expression at the plasma membrane level
Zager, R. A. (1995) · Kidney International · doi:10.1038/ki.1995.189 · Cited by 37 · see citing works
Prior induction of heme oxygenase‐1 with glutathione depletor ameliorates the renal ischemia and reperfusion injury in the rat
Horikawa, S., Yoneya, R., Nagashima, Y., Hagiwara, K., & Ozasa, H. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)03270-7 · Cited by 37 · see citing works
Fundamental Role of Heme Oxygenase in the Protection Against Ischemic Acute Renal Failure
Akagi, R., Takahashi, T., & Sassa, S. (2002) · The Japanese Journal of Pharmacology · doi:10.1254/jjp.88.127 · Cited by 35 · see citing works
Self-citation
Short-term immunosuppressive treatment of the donor ameliorates consequences of ischemia/ reperfusion injury and long-term graft function in renal allografts from older donors1
Reutzel‐Selke, A., Zschockelt, T., Denecke, C., et al. (2003) · Transplantation · doi:10.1097/01.tp.0000063408.97289.89 · Cited by 29 · see citing works
A heat-inducible nuclear factor that binds to the heat-shock element of the human haem oxygenase gene
Mitani, K., Fujita, H., Sassa, S., et al. (1991) · Biochemical Journal · doi:10.1042/bj2770895 · Cited by 28 · see citing works
Self-citation
Control of Heme Metabolism by Synthetic Metalloporphyrinsa
Drummond, G. S. (1987) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1987.tb48764.x · Cited by 27 · see citing works
Regulation and Immunohistochemical Analysis of Stress Protein Heme Oxygenase-1 in Rat Kidney with Myoglobinuric Acute Renal Failure
Ishizuka, S., Nagashima, Y., Numata, M., et al. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7573 · Cited by 26 · see citing works
Heme oxygenase inhibits nitric oxide synthase by degrading heme: a negative feedback regulation mechanism for nitric oxide production
Turcanu, V., Dhouib, M., & Poindron, P. (1998) · Transplantation Proceedings · doi:10.1016/s0041-1345(98)01385-2 · Cited by 17 · see citing works
Heme oxygenase is not expressed as a stress protein after renal ischemia.
Paller, M. S., Nath, K. A., & Rosenberg, M. E. (1993) · PubMed · Cited by 13 · see citing works
Hemolysate Pretreatment Ameliorates Ischemic Acute Renal Injury in Rats
Yoneya, R., Nagashima, Y., Sakaki, K., et al. (2002) · The Nephron journals/Nephron journals · doi:10.1159/000063318 · Cited by 7 · see citing works
Recent progress in heme synthesis and metabolism
Sassa, S. (1994) · Stem Cells · doi:10.1002/stem.5530120704 · Cited by 6 · see citing works
Self-citation

Flagged first, then by citations

Sorted by citations

Update on Mechanisms of Ischemic Acute Kidney Injury
Devarajan, P. (2006) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006010017 · Cited by 1,026 · see citing works
Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases
Kell, D. B. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-2 · Cited by 554 · see citing works
Heme as key regulator of major mammalian cellular functions: Molecular, cellular, and pharmacological aspects
Tsiftsoglou, A. S., Tsamadou, A. I., & Papadopoulou, L. C. (2006) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2005.10.017 · Cited by 281 · see citing works

Mechanism of induction of heme oxygenase by metalloporphyrins in primary chick embryo liver cells: Evidence against a stress-mediated response
Cable, E. E., Gildemeister, O. S., Pepe, J. A., et al. (1997) · Molecular and Cellular Biochemistry · doi:10.1023/a:1006817207166 · Cited by 19 · see citing works
Heme oxygenase—regulation of and physiological implication in heme catabolism
Shibahara, S. (1994) · Stem Cells · doi:10.1002/stem.5530120713 · Cited by 27 · see citing works
The heme-heme oxygenase system: a molecular switch in wound healing
Wagener, F. A. D. T. G., Beurden, H. E. V., den Hoff, J. W. V., Adema, G. J., & Figdor, C. G. (2003) · Blood · doi:10.1182/blood-2002-07-2248 · Cited by 132 · see citing works
Heme catabolism in cultured hepatocytes: evidence that heme oxygenase is the predominant pathway and that a proportion of synthesized heme is converted rapidly to biliverdin
Lincoln, B. C., Aw, T. Y., & Bonkovsky, H. L. (1989) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(89)90049-4 · Cited by 39 · see citing works
Supramolecular Hemoprotein Linear Assembly by Successive Interprotein Heme−Heme Pocket Interactions
Kitagishi, H., Oohora, K., Yamaguchi, H., et al. (2007) · Journal of the American Chemical Society · doi:10.1021/ja073295q · Cited by 115 · see citing works

Authors: Akagi, R., Takahashi, T., & Sassa, S.
Affiliations: Okayama Prefectural University (JP)
Okayama University (JP)
Rockefeller University (US)
ORCID: Takahashi, Toru
Venue: Contributions to Nephrology
Publisher: KARGER
Published: 2005
Volume: 148
Pages: 70-85
DOI: 10.1159/000086044
OpenAlex: W1588064010
Cited by: 53
References: 85
Citations by year: 2024: 1 · 2022: 1 · 2021: 2 · 2019: 1 · 2018: 2 · 2017: 2 · 2016: 1 · 2015: 3 · 2014: 3 · 2013: 3 · 2012: 7
FWCI: 7.46
Type: book chapter
Language: en
Open access: closed
Locations: KARGER eBooks (publishedVersion)
PubMed (publishedVersion)
Funders: U.S. Public Health Service
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
Health Sciences › Medicine › Nephrology › Acute Kidney Injury Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
Keywords: heme oxygenase-1, acute kidney injury, ischemia-reperfusion injury, renal ischemia, oxidative stress, superoxide, heme degradation, tin mesoporphyrin, tin(II) chloride, proximal tubular epithelial cells, cytoprotection
MeSH terms: Animals, Heme Oxygenase (Decyclizing), Humans, Membrane Proteins, Cytoprotection, Heme Oxygenase-1, Acute Kidney Injury

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Cytoprotective Effects of Heme Oxygenase in Acute Renal Failure

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Cites

Cited by

Related

Record

About these checks