Hemoxigenasa-1: su importancia en los mecanismos de oxidación y su relación con enfermedades no infecciosas.

Lucerito E Ávila L., Omar Arroyo H, Elda M Coutiño R

Resumen


Las enzimas son catalizadores de múltiples funciones metabólicas esenciales en todos los organismos vivos. Su nombre, importancia y clasificación varían dependiendo de la función que realicen; pueden ser uniloculadas si se localizan en un solo lugar, o biloculadas si se hallan en dos lugares; por su expresión se denominan constitutivas si mantienen su función constante, o inducibles si son estimuladas por incremento en el sustrato, cofactor o inductor. Generalmente, se encuentran pequeñas cantidades de enzimas en sangre, cuyo incremento o disminución posee gran valor diagnóstico, ya que la deficiencia o falla de alguna de ellas desencadena reacciones adversas que afectan el metabolismo, volviendo al individuo susceptible a padecer múltiples trastornos y enfermedades. Algunas deficiencias enzimáticas son de carácter genético y otras obedecen a factores externos del microambiente celular, al igual que la sobreexpresión. En este artículo abordaremos el estudio de la hemoxigenasa-1, enzima inducible de interés biológico, que participa en el metabolismo del grupo hemo proveniente de las hemoproteínas, y se induce por el estrés oxidativo y algunos metales, por tanto pudiera utilizarse como marcador de estrés oxidativo, por su importancia para el funcionamiento óptimo del organismo, dada su asociación con una gran cantidad de Enfermedades Crónicas No transmisibles que aquejan a gran parte de las poblaciones, considerando que son enfermedades íntimamente ligadas con el incremento en el Estrés Oxidativo, de aquí su relevancia en la Salud Pública.


Citas


Brandan N, et al. Enzimas. Cátedra de Bioquímica; Facultad de Medicina Universidad Nacional Del Nordeste UNNE [Serie en internet]; [citado 20 de sep. 2011], pp. 1-6. Disponible en:

http://med.unne.edu.ar/catedras/bioquimica/pdf/enzimas.pdf

Colarosi C. Enzimas. Dpto. de Bioquímica, Biología Mol. Y Farmacología [Serie en internet]; [citado 20 de sep. 2011]. Disponible en:

http://www.upch.edu.pe/facien/fc/dbmbqf/pherrera/cursos/Bioquimica08/clases/Enzimas%20%20y%20cinetica%20enzimatica.pdf

Céspedes M. et al. Un acercamiento a la teoría de los radicales libres y el estrés oxidativo en el envejecimiento. Rev Cubana Invest Biomed 2000; 19 (3): 186-90.

Orozco I, Pedraza C. Hemo oxigenasa: aspectos básicos y su importancia en el sistema nervioso central. Arch Neurocien Mex. 2010; 15, (1): 47-55.

Olatunde F, Surh Y. Hemo oxigenasa-1 como una posible terapéutica diana para hepatoprotección. Journal of Biochemistry and Molecular Biology. 2006; 5 (39): 479-91.

Mahin D, Trakshel G, Kutty R. Heme oxygenase: clinical applications and functions. The journal of biological chemistry. 1986; 261 (1): 411-19.

Maines M, Gibbs P. 30 some years of heme oxygenase: from a «molecular wrecking ball» to a «mesmerizing» trigger of cellular events. Biochem Biophys Res Commun. 2005; 338: 568-77.

Braggins P, Trakshel G, Kutty R, et al. Characterization of two heme oxygenase isoforms in rat spleen: comparison with the hematin-induced and constitutive isoforms of the liver. Biochem Biophys Res Commun. 1986; 141: 528-33.

Bergeron M, Ferriero D, Sharp F. Developmental expression of heme oxygenase-1 (HSP32) in rat brain: an immunocytochemical study. Brain Res Dev Brain Res. 1998; 105: 181-94.

Colombrita C, Calabrese V, Stella A, et al. Regional rat brain distribution of heme oxygenase-1 and manganese superoxide dismutase mRNA: relevance of redox homeostasis in the aging processes. Exp Biol Med. 2003; 228: 517-24.

Parfenova H, Neff III R, Alonso J, et al. Cerebral vascular endothelial heme oxygenase: expression, localization, and activation by glutamate. Am J Physiol Cell Physiol. 2001; 281: 1954-63.

Orozco I, Pedraza C. Hemooxigenasa. Radicales libres y estrés oxidativo. Aplicaciones médicas. Konigsberg M, editor, México: Manual Moderno, 2008.

Haase A, Arlinghaus H, Tentschert J, et al. Application of laser postionization secondary neutral mass spectrometry/time-of flight secondary ion mass spectromertry in nanotoxicology. Visualization of nanosilver in human macrophages and cellular responses. ACS Nano 5: 3059-68.

Deshane J, Wright M, Agarwal A. Heme oxygenase-1 expression in disease states. Acta biochimica polonica. Article the review. 2005; 52 (2): 273-84.

Ishikawa K. Heme oxygenase-1 against vascular insufficiency: roles of atherosclerotic disorders. Curr Pharm Des. 2003; 9: 2489-97. Disponible en:

http://www.ingentaconnect.com/content/ben/cpd/2003/00000009/00000030/art00003

Cuadrado A, Rojo A. Heme oxygenase-1 as a therapeutic target in neurodegenerative diseases and brain infections. Curr Pharm Des. 2008; 14: 429-42.

Soares M, Bach F. Heme oxygenase-1: from biology to therapeutic potential. Trends Mol Med. 2009; 15: 50-8.

Smith M, Kutty R, Richey P, et al. Heme oxygenase-1 is associated with the neurofibrillary pathology of Alzheimer’s disease. Am J Pathol. 1994; 145: 42-7.

Schipper H, Cisse S, Stopa E. Expression of heme oxygenase-1 in the senescent and Alzheimer-diseased brain. Ann Neurol. 1995; 37: 758-68.

Ferrante R, Browne S, Shinobu L, et al. Evidence of increased oxidative damage in both sporadic and familial amyotrophic lateral sclerosis. J Neurochem. 1997; 69: 2064-74.

Willis D, Moore AR, Frederick R, et al. Heme oxygenase: A novel target for the modulation of inflammatory response. Nature Medicine 2, 87-93 1996.Disponible en:

http://www.nature.com/nm/journal/v2/n1/pdf/nm0196-87.pdf

Kapturczak M, Wasserfall C, Brusko T, et al. Heme Oxygenase-1 Modulates Early Inflammatory Responses: Evidence from the Heme Oxygenase-1-Deficient Mouse. The American Journal of Pathology. 2004; 165: 1045-53.

Disponible en:

http://www.sciencedirect.com/science/article/pii/S0002944010633652

Vogt B, Shanley T, Croa A, et al. Glomerular inflammation induces resistance to tubular injury in the rat. A novel form of acquired, heme oxygenase-dependent resistance to renal injury. Journal Clin Invest. 1996; 98: 2139-45. Disponible en:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC507659/pdf/982139.pdf

Siow R, Sato H, Mann G. Heme oxygenase-carbon monoxide signalling pathway in atherosclerosis: anti-atherogenic actions of bilirubin and carbon monoxide? Cardiovasc Research. 1999; 41: 385-94. Disponible en:

http://cardiovascres.oxfordjournals.org/content/41/2/385.full.pdf+html

Attuwaybi B, Kozar R, Moore-Olufemi S, et al. Heme oxygenase-1 induction by hemin protects against gut ischemia/reperfusion injury. J Surg Res. 2004; 118: 53-57. Disponible en:

http://www.sciencedirect.com/science/article/pii/S0022480404000289

Agarwal A, Kim Y, Matas A, et al. Gas-generating systems in acute renal allograft rejection in the rat. Co-induction of heme oxygenase and nitric oxide synthase. Transplantation. 1996b; 61: 93-98. Disponible en:

http://journals.lww.com/transplantjournal/Abstract/1996/01150/GAS_GENERATING_SYSTEMS_IN_ACUTE_RENAL_ALLOGRAFT.19.aspx

Avihingsanon Y, Ma N, Csizmadia E, et al. Expression of protective genes in human renal allografts: a regulatory response to injury associated with graft rejection. Transplantation. 2002; 73: 1079-85. Disponible en:

http://journals.lww.com/transplantjournal/Abstract/2002/04150/Expression_of_protective_genes_in_human_renal.11.aspx

Soares M, Seldon M, Gregoire I, et al. Heme oxygenase-1 modulates the expression of adhesion molecules associated with endothelial cell activation. J Immunol. 2004; 172: 3553-63. Disponible en:

http://www.jimmunol.org/content/172/6/3553.full.pdf+html

Holweg C, Balk A, Snaathorst J, et al. Intragraft heme oxygenase-1 and coronary artery disease after heart transplantation. Transpl Immunol. 2004; 13: 265-272. Disponible en:

http://www.sciencedirect.com/science/article/pii/S0966327404000759

Wang L, Lee T, Lee F, et al. Expression of heme oxygenase-1 in atherosclerotic lesions. Am J Pathol. 1998; 152: 711-20. Disponible en:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1858397/pdf/amjpathol00015-0090.pdf

Juan S, Lee T, Tseng K, et al. Adenovirus-mediated heme oxygenase-1 gene transfer inhibits the development of atherosclerosis in apolipoprotein E-deficient mice. Circulation. 2001; 104: 1519-25. Disponible en:

http://circ.ahajournals.org/content/104/13/1519.full.pdf+html

Shi W, Haberland M, Jien M, et al. Endothelial responses to oxidized lipoproteins determine genetic susceptibility to atherosclerosis in mice circulation 2000; 102: 75-81. Disponible en:

http://circ.ahajournals.org/content/102/1/75.full.pdf+html

Furnkranz A, Schober A, Bochkov V, et al. Oxidized phospholipids trigger atherogenic inflammation in murine arteries. Arterioscler Thromb Vasc Biol. 2005; 25: 633–38. Disponible en:

http://atvb.ahajournals.org/content/25/3/633.full.pdf+html

Ishikawa K, Navab M, Leitinger N, et al. Induction of heme oxygenase-1 inhibits the monocyte transmigration induced by mildly oxidized LDL. J Clin Invest.1997;100:1209-16. Disponible en:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC508298/pdf/1001209.pdf

Schillinger M, Exner M, Mlekusch W, et al. Heme oxygenase-1 gene promoter polymorphism is associated with abdominal aortic aneurysm. Thromb Res. 2002; 106: 131-36. Disponible en:

http://www.sciencedirect.com/science/article/pii/S0049384802001007

Nath K, Balla G, Vercelloi G, et al. Induction of heme oxygenase is a rapid, protective response in rhabdomyolysis in the rat. J Clin Invest. 1992; 90: 267-70. Disponible en:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC443091/pdf/jcinvest00050-0273.pdf

Zhang X, Shan P, Jiang D, et al. Small interfering RNA targeting heme oxygenase-1 enhances ischemia-reperfusion-induced lung apoptosis. J Biol Chem. 2004; 279: 10677-684. Disponible en:

http://www.jbc.org/content/279/11/10677.full.pdf+html

Yamada N, Yamaya M, Okinaga S, et al. Microsatellite polymorphism in the heme oxygenase-1 gene promoter is associated with susceptibility to emphysema. Am J Hum Genet. 2000; 66: 187-95. Disponible en:

http://ac.els-cdn.com/S0002929707622460/1-s2.0-S0002929707622460-main.pdf?_tid=9f82b86729e1f60466aa59fc49526adf&acdnat=1339824303_f8ab4593c144688fc2109500ee55f649

Lum H, Roebuck K. Oxidant stress and endothelial cell dysfunction. Am J Physiol Cell Physiol. 2001; 280: 719–41. Disponible en:

http://ajpcell.physiology.org/content/280/4/C719.full.pdf+html

Wang Y, Yu Y. Expression of endogenous heme oxygenase on surface of placental trophoblasts of pregnant women with intrauterine growth retardation of the fetus. Di Yi Jun Yi Da Xue Xue Bao. 2002; 22: 637-39. Disponible en:

http://ukpmc.ac.uk/abstract/MED/12376298/reload=0;jsessionid=DKTNOTPLkcVWoeTfmRUh.0

Johnson R, Teran F, Durante W, et al. Enhanced heme oxygenase-mediated coronary vasodilation in Dahl salt-sensitive hypertension. Am J Hypertens. 2004b; 17: 25-30. Disponible en:

http://www.sciencedirect.com/science/article/pii/S0895706103011166

Yang L, Quan S, Nasjle A, et al. Heme oxygenase-1 gene expression modulates angiotensin II-induced increase in blood pressure. Hypertension. 2004; 43: 1221-26. Disponible en:

http://hyper.ahajournals.org/content/43/6/1221.full.pdf+html

Aizawa T, Ishizaka N, Taguchi J, et al. Heme oxygenase-1 is upregulated in the kidney of angiotensin II-induced hypertensive rats: possible role in renoprotection. Hypertension. 2000; 35: 800-06. Disponible en:

http://hyper.ahajournals.org/content/35/3/800.full.pdf+html

Cosso L, Maineri E, Traverso N, et al. Induction of heme oxygenase 1 in liver of spontaneously diabetic rats. Free Radic Res. 2001; 34: 189-191. Disponible en:

http://informahealthcare.com/doi/abs/10.1080/10715760100300171

Abraham N, Kushida T, Mcclung J, et al. Heme oxygenase-1 attenuates glucose-mediated cell growth arrest and apoptosis in human microvessel endothelial cells. Circ Res. 2003; 93: 507-14.

Chang S, Garcia J, Melendez J, et al. Haem oxygenase 1 gene induction by glucose deprivation is mediated by reactive oxygen species via the mitochondrial electron-transport chain. Biochem J. 2003; 1; 371 (3): 877-85. Disponible en:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1223354/pdf/12585963.pdf

Abraham N, Rezzani R, Rodella L, et al. Overexpression of human heme oxygenase-1 attenuates endothelial cell sloughing in experimental diabetes. Am J Physiol. Heart Circ Physiol. 2004; 287: H2468-77.

Goodman A, Choudhury M, Da Silva J, et al. Overexpression of the heme oxygenase gene in renal cell carcinoma. Proc Soc Exp Biol Med. 1997; 214: 54-61. Disponible en:

http://ebm.rsmjournals.com/content/214/1/54.extract

Doi K, Akaike T, Fujii S, et al. Induction of haem oxygenase-1 nitric oxide and ischaemia in experimental solid tumours and implications for tumour growth. Br J Cancer. 1999; 80: 1945-54. Disponible en:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2363152/pdf/80-6690624a.pdf

Liu X, Chapman G, Peyton K, et al. Carbon monoxide inhibits apoptosis in vascular smooth muscle cells. Cardiovasc Res. 2002; 55: 396-405. Disponible en:

http://cardiovascres.oxfordjournals.org/content/55/2/396.full.pdf+html

Fang J, Sawa T, Akaike T, et al. In vivo antitumor activity of pegylated zinc protoporphyrin: targeted inhibition of heme oxygenase in solid tumor. Cancer Res. 2003; 63: 3567-74.

Disponible en:

http://cancerres.aacrjournals.org/content/63/13/3567.full.pdf+html

Beschorner R, Adjodah D, Schwab J, et al. Long-term expression of heme oxygenase-1 (Ho-1, HSP-32) following focal cerebral infarctions and traumatic brain injury in humans. Acta Neuropathol. 2000; 100: 377-84.

Visner G, Lu F, Zhou H, et al. Rapamycin induces heme oxygenase-1 in human pulmonary vascular cells: implications in the antiproliferative response to rapamycin. Circulation. 2003; 107: 911-16. Disponible en:

http://circ.ahajournals.org/content/107/6/911.full.pdf+html

Grosser N, Erdmann K, Hemmerle A, et al. Rosuvastatin upregulates the antioxidant defense protein heme oxygenase-1. Biochem Biophys Res Commun. 2004a; 325: 871-76.

Grosser N, Hemmerle A, Berndt G, et al. The antioxidant defense protein heme oxygenase 1 is a novel target for statins in endothelial cells. Free Radic Biol Med. 2004b; 37: 2064-71.

Lee T, Chang C, Zhu Y, et al. Simvastatin induces heme oxygenase-1: a novel mechanism of vessel protection. Circulation. 2004; 110: 1296-1302. Disponible en:

http://circ.ahajournals.org/content/110/10/1296.full.pdf+html

Berger S, Hunger M, Yard B, et al. Dopamine induces the expression of heme oxygenase-1 by human endothelial cells in vitro. Kidney Int. 2000; 58: 2314-19. Disponible en:

http://www.nature.com/ki/journal/v58/n6/pdf/4491903a.pdf


Texto completo: PDF

Refbacks

  • No hay Refbacks actualmente.


Creative Commons License
This work is licensed under a Creative Commons Attribution 3.0 License.

UniverSalud ISSN:2007-3526