Microsomal Heme Oxygenase
نویسندگان
چکیده
منابع مشابه
Microsomal Heme Oxygenase
This study characterizes microsomal heme oxygenase, a previously undescribed enzyme which catalyzes the oxidation of heme at the cr-methene bridge to form biliverdin. This step is then coupled with soluble NADPH-dependent biliverdin reductase to form bilirubin; microsomal heme oxygenase is rate-limiting in this pathway. By all analytical criteria, the product of this reaction is bilirubin. Most...
متن کاملFeatures of the reaction of heme degradation catalyzed by the reconstituted microsomal heme oxygenase system.
The heme oxygenase system was reconstituted from a heme oxygenase preparation highly purified from pig spleen microsomes and a partially purified NADPHcytochrome c reductase from pig liver microsomes. In the reconstituted heme oxygenase reaction, the relationship between the rate of heme degradation and the heme concentration was sigmoidal, and the heme concentration which gave the half-maximum...
متن کاملHeme oxygenase and atherosclerosis.
Overproduction of reactive oxygen species under pathophysiological conditions, including dyslipidemia, hypertension, diabetes, and smoking, is integral in the development of cardiovascular diseases (CVD). The reactive oxygen species released from all types of vascular cells regulate various signaling pathways that mediate not only vascular inflammation in atherogenesis but also antioxidative an...
متن کاملDifferent faces of the heme-heme oxygenase system in inflammation.
The heme-heme oxygenase system has recently been recognized to possess important regulatory properties. It is tightly involved in both physiological as well as pathophysiological processes, such as cytoprotection, apoptosis, and inflammation. Heme functions as a double-edged sword. In moderate quantities and bound to protein, it forms an essential element for various biological processes, but w...
متن کاملHow Heme Oxygenase-1 Prevents Heme-Induced Cell Death
Earlier observations indicate that free heme is selectively toxic to cells lacking heme oxygenase-1 (HO-1) but how this enzyme prevents heme toxicity remains unexplained. Here, using A549 (human lung cancer) and immortalized human bronchial epithelial cells incubated with exogenous heme, we find knock-down of HO-1 using siRNA does promote the accumulation of cell-associated heme and heme-induce...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1969
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)63477-5