Heme oxygenase function

Low-Friedrich I, Schoeppe W (1991) Effects of calcium channel blockers on stress protein synthesis in cardiac myocytes. J Cardiovasc Pharmacol 17 800-806 Maines MD (1988) Heme oxygenase function. Multiplicity, regulatory mechanisms, and clinical applications. FASEB J 2 2557-2568 Maines MD, Kappas A (1977) Metals as regulators of heme metabolism physiological and toxicological implications. Science 198 1215-1221 Maines MD, Chung A-S, Kutty RK (1982) Inhibition of testicular heme oxygenase activity by cadmium a novel cellular response. J Biochem 257 14116-14121... 

Maines MD. Heme oxygenase function, multiplicity, regulatory mechanisms, and clinical applications. FASEB J 1988 2 2557-2568. 

Suits MDL, GP Pal, K Nakatsu, A Matte, M Cygler, Z Jia (2005) Identification of an Escherichia coli 0157 H7 heme oxygenase with tandem functional repeats. Proc Natl Acad USA 102 16955-16960. 

Improving functionality may involve a complex biocatalytic system including more than one biocatalyst, as it is the case in BDM reactions. Additionally to the BDS for instance, another biocatalyst active for BDM [395,406], which consists of a heme oxygenase or a Cytochrome reductase could be used to widen up the functionality. 

Biological Function of Heme Oxygenase Heme Oxygenase Model Systems Heme Oxygenase The Protein... 

Maines, M. D. Heme Oxygenase Clinical Applications and Functions CRC Press Boca Raton, FL, 1992 p. 145. 

The second heme oxygenase (HO-2) is distributed widely among tissues, but it is most abundant in certain neurons in the brain.437 4373 Its major function may be to generate CO, which is now recognized as a probable neurohormone (Chapter 30). Bacteria, such as Corynebacterium diphtheriae, employ their own heme oxygenase as a means of recovering iron that they need for growth.438... 

Ryter, Stefan W. Ottenbein, Leo E. Morse Danielle et al. Heme oxygenase/carbon monoxide signaling pathways Regulation and functional significance. Mol Cell Biochem, No. 234/235 249-263 2002. 

Essentially, all organ systems must be evaluated. Thus laboratory tests, should include complete blood count, liver and renal functional tests, and blood, nail and urine arsenic levels. Other biomarkers of arsenic exposure include nonerythrocyte porphyrin enzyme activities and urine transforming growth factor TNF-a, accompanied by induction of heme oxygenase, mitogen-activated protein kinases, the ubiquitin-dependent proteolytic pathway, and protein kinase C in various tissues. These tests are still being investigated in laboratories and their clinical usefulness remains to be proven (Chapell et al, 2001). 

At the same time there are differences between CO and NO. For example, NO is an unstable gas and radical while CO is a stable gas and not a radical. CO binds only ferrous heme but NO binds to both ferrous and ferric hemoprotein (Hartsfield, 2002). The combination rate of NO with hemoglobin is faster and dissociation slower than that of CO (Sharma and Ranney, 1978) so that the affinity of NO for hemoglobin is 1,500 times that of CO (Foresti and Motterlini, 1999). Formation of endogenous CO in a variety of tissues has been demonstrated (Marks et al, 2002). Given the complexity of colocalization and activities of heme oxygenase and nitric oxide synthase, it has been speculated that CO and NO could function in a synergistic, compensatory, and/or counterregulatory way (Hartsfield, 2002). 

Chauveau, C., Remy, S., Royer, P.J., Hill, M., Tanguy-Royer, S., Hubert, F.X., Tesson, L., Brion, R., Beriou, G., Gregoire, M., Josien, R., Cuturi, M.C., Anegon, I. (2005). Heme oxygenase-1 expression inhibits dendritic cell maturation and proin-flammatory function but conserves IL-10 expression. Blood 106 1694-1702. 

Kitamuro T, Takahashi K, Ogawa K, Udono-Fujimori R, Takeda K, Furuyama K, Nakayama M, Sun J, Fujita H, Hida W, Hattori T, Shirato K, Igarashi K, Shibahara S. Bachl functions as a hypoxia-inducible repressor for the heme oxygenase-1 gene in human cells. J. Biol. Chem. 2003 278 9125-9133. 

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