+ Site Statistics
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on Google+Follow on Google+
Follow on LinkedInFollow on LinkedIn

+ Translate

Regulation of heme metabolism during senescence activity of several heme containing enzymes and heme oxygenase in the liver and kidney of aging rats

Mechanisms of Ageing & Development 12(1): 81-92
Regulation of heme metabolism during senescence activity of several heme containing enzymes and heme oxygenase in the liver and kidney of aging rats
The activities of several heme-containing enzymes plus succinate dehydrogenase, the content of mitochondrial cytochromes, the amount of microsomal cytochrome P-450, and the activity of heme oxygenase, the major enzyme of heme degradation, have been compared in young, mature and senescent rats. Measurements were made in liver, a tissue previously reported to have an age-related decrease in .delta.-aminolevulinic acid synthetase, and in kidney, a tissue previously reported to have no age-related change in this enzyme, the rate-limiting enzyme of heme biosynthesis. The activity of cytochrome oxidase in liver mitochondria did not decrease with age while this activity in kidney mitochondria was highest in animals 1 yr old and decreased in the 2 yr olds. Succinate dehydrogenase of both kidney and liver mitochondria decreased markedly in the aging rats. No age-related change in the content of cytochromes b, c or aa3 was observed in liver mitochondria; however, a marked age-related decrease in cytochrome aa3 was observed in kidney mitochondria. Similarly no change in cytochrome P-450 levels was observed in either tissue obtained from aging animals. In the liver, catalase activity increased while in the kidney it decreased in senescent as compared to mature animals. Heme degradation does not decrease with age as the activity of heme oxygenase increased in both liver and kidney of 2 yr old rats as compared to 1 yr olds. The lower activity of .delta.-aminolevulinic acid synthetase observed in the aging rat may not be correlated with a decrease in the activity of heme-containing proteins and the regulation of the heme pool used for the synthesis of various intracellular hemoproteins may be complex.

Accession: 006288341

PMID: 6243730

Related references

Heme and heme biosynthesis intermediates induce heme oxygenase-1 and cytochrome P450 2A5, enzymes with putative sequential roles in heme and bilirubin metabolism: different requirement for transcription factor nuclear factor erythroid- derived 2-like 2. Toxicological Sciences 130(1): 132-144, 2013

Regulation of heme metabolism in rat hepatocytes and hepatocyte cell lines: delta-aminolevulinic acid synthase and heme oxygenase are regulated by different heme-dependent mechanisms. Archives of Biochemistry and Biophysics 384(2): 280-295, 2001

Implication for using heme methyl hyperfine shifts as indicators of heme seating as related to stereoselectivity in the catabolism of heme by heme oxygenase: in-plane heme versus axial his rotation. Biochemistry 47(1): 421-430, 2007

Hepatic heme metabolism possible role of biliverdin in the regulation of heme oxygenase activity. Biochemical & Biophysical Research Communications 122(1): 40-46, 1984

Enzymes of heme metabolism in the kidney: regulation by trace metals which do not form heme complexes. Journal of Experimental Medicine 146(5): 1286-1293, 1977

Oxidation of heme c derivatives by purified heme oxygenase. Evidence for the presence of one molecular species of heme oxygenase in the rat liver. Journal of Biological Chemistry 257(17): 9944-9952, 1982

Regulation of human hepatic DELTA-aminolevulinate synthase and heme oxygenase by heme and non-heme metalloporphyrins. Hepatology 34(4 Pt 2): 356A, October, 2001

Oxidation of heme c derivatives by purified heme oxygenase evidence for the presence of 1 molecular species of heme oxygen in the rat liver. Journal of Biological Chemistry 257(17): 9944-9952, 1982

Heme oxygenase-2 is a hemoprotein and binds heme through heme regulatory motifs that are not involved in heme catalysis. Journal of Biological Chemistry 272(19): 12568-12574, 1997

Effects of phorone diisopropylidene acetone a glutathione gsh depletor on hepatic enzymes involved in drug and heme metabolism in rats evidence that phorone is a potent inducer of heme oxygenase. Biochemical & Biophysical Research Communications 145(1): 502-508, 1987