Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.14.99.3 (heme oxygenase)
 4,196 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Physiological heme degradation is mediated by the heme oxygenase system consisting of heme oxygenase and NADPH-cytochrome P-450 reductase. Biliverdin IX alpha is formed by elimination of one methene bridge carbon atom as CO. Purified NADPH-cytochrome P-450 reductase alone will also degrade heme but biliverdin is a minor product (15%). The enzymatic mechanisms of heme degradation in the presence and absence of heme oxygenase were compared by analyzing the recovery of 14CO from the degradation of [14C]heme. 14CO recovery from purified NADPH-cytochrome P-450 reductase-catalyzed degradation of [14C]methemalbumin was 15% of the predicted value for one molecule of CO liberated per mole of heme degraded. 14CO2 and [14C]formic acid were formed in amounts (18 and 98%, respectively), suggesting oxidative cleavage of more than one methene bridge per heme degraded, similar to heme degradation by hydrogen peroxide. The reaction was strongly inhibited by catalase, but superoxide dismutase had no effect. [14C]Heme degradation by the reconstituted heme oxygenase system yielded 33% 14CO. Near-stoichiometric recovery of 14CO was achieved after addition of catalase to eliminate side reactions. Near-quantitative recovery of 14CO was also achieved using spleen microsomal preparations. Heme degradation by purified NADPH-cytochrome P-450 reductase appeared to be mediated by hydrogen peroxide. The major products were not bile pigments, and only small amounts of CO were formed. The presence of heme oxygenase, and possibly an intact membrane structure, were essential for efficient heme degradation to bile pigments, possibly by protecting the heme from indiscriminate attack by active oxygen species.
 ...
PMID:Methene bridge carbon atom elimination in oxidative heme degradation catalyzed by heme oxygenase and NADPH-cytochrome P-450 reductase. 644 Apr 89

The bioactivity of cell wall component(s) of fungi has not been fully investigated, especially in vivo. We have successfully extracted a soluble cell wall beta-glucan from C. albicans (CSBG), and shown that pulmonary exposure to CSBG induces lung inflammation in mice. CSBG-induced lung inflammation was concomitant with the nuclear translocation of signal transducer and activator of transcription (STAT)6 and enhanced lung expression of various cytokines and chemokines. However, the effects of CSBG on the murine respiratory system and their mechanisms have not been fully investigated. In this study, we further explored the effects of pulmonary exposure to CSBG on lung pathophysiology in terms of the induction of apoptosis and enhancement of oxidative stress. ICR mice were intratracheally instilled with vehicle, CSBG, or structurally degraded products of CSBG by formic acid (DEG-CSBG), and 24 h later, the lungs were isolated and evaluated for apoptosis by the TUNEL assay and oxidative stress by immunohistochemistry of 8-hydroxy-2'-deoxyguanosine (8-OHdG), a proper marker of the oxidative DNA damage. In another experiment, the mice were sacrificed and lungs were isolated 4 h after the instillation with vehicle or CSBG for evaluation of transcriptional level of heme oxygenase (HO)-1, a stress responsive protein. Pulmonary exposure to CSBG significantly induced apoptosis and enhanced the formation of 8-OHdG in the lung parenchyma as compared to vehicle or DEG-CSBG exposure. CSBG significantly induced HO-1 in the lung. Taken together, CSBG induces/enhances apoptosis and oxidative stress in the lung in association with lung inflammation/injury.
 ...
PMID:Soluble cell wall beta-glucan of Candida induces/enhances apoptosis and oxidative stress in murine lung. 1995 Oct 74