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All rights reserved. http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/dc/elements/1.1/title BEL Framework Large Corpus Document http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/pav/authoredBy http://www.tkuhn.ch/bel2nanopub/RAw62zOLPMALX_5ClzCPdKlShzASkstX61STCJjMk8BX0#_5 http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/pav/version 20131211 http://www.tkuhn.ch/bel2nanopub/RAw62zOLPMALX_5ClzCPdKlShzASkstX61STCJjMk8BX0#_4 http://www.w3.org/ns/prov#value D. Recent Insights in Heme Oxygenase and a Novel Role for Heme-Derived Metabolites In addition to the role of HO in recycling iron for heme synthesis, current understanding of HO has demonstrated that HO is important in a wide variety of other physiological and pathological processes. To date, no other known enzyme is induced by so many stimuli of diverse origin as HO-1 (Maines, 1997; Otterbein and Choi, 2000) (Table 2). It is this diversity of non-heme inducers and the existence of different HO isoforms that has led to the hypothesis that HO-1 plays a vital function in maintaining cellular homeostasis in addition to heme degradation (Maines, 2000). Elevated HO-1 expression levels are detected in a variety of pathological conditions (Otterbein and Choi, 2000) (Table 3). HO-1 induction protects against ischemia/reperfusion injury, oxidative stress, inflammation, transplant rejection, apoptosis, and many more conditions (Amersi et al., 1999; Yang et al., 1999; Brouard et al., 2000, 2002; Willoughby et al., 2000; Inguaggiato et al., 2001; Sato et al., 2001; Ke et al., 2002; Melo et al., 2002). 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