Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.9.3.1 (cytochrome oxidase)
 8,822 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The induction of 5'-aminolevulinate synthase (ALV synthase) activity in adult muscle by overload occurs in the absence of proportional changes in its mRNA content. Complete interpretation of these findings is difficult because little is known of the basal regulation of ALV synthase expression in muscle. In three adult chicken muscle fiber types (n = 5 each), differences in ALV synthase activity were correlated (r greater than or equal to 0.89; P less than 0.05) to the activities of cytochrome oxidase (COX) and citrate synthase (CS) and to levels of the "liver" isoform of ALV synthase mRNA. During posthatch development, ALV synthase activity and mRNA levels (n = 3-6 per time point) also covaried with changes in COX and CS activity. The highest levels of ALV synthase mRNA in muscle are observed early in myogenesis prior to induction of COX activity. The regulation of ALV synthase is also tissue-specific because the higher basal levels of ALV synthase activity in liver mitochondria are associated with disproportionately less oxidative enzyme activity and less of the liver ALV synthase isoform mRNA than in muscle.
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PMID:Muscle-specific regulation of the heme biosynthetic enzyme 5'-aminolevulinate synthase. 192 29

The regulation of the mitochondrial enzyme 5'-aminolevulinate synthase (ALV synthase) activity during chronic weight-bearing activity (overload) in chicken skeletal muscle was investigated. Maximal enzyme activity was increased 2.5- and 4.0-fold after 3 and 7 days of overload. The content of ALV synthase mRNA (ng/mg total RNA) was not changed after 3 days but increased (20%; P less than 0.05) after 7 days of overload. Normalizing the content of ALV synthase mRNA relative to the increase in total RNA indicated that ALV synthase mRNA increased by 1.6- and 2.0-fold at 3 and 7 days, respectively. On this basis, the increase in enzyme activity per gram protein exceeded the increase in mRNA content per gram protein by 60-70%. During overload, the activity of cytochrome oxidase was unchanged after 3 days but increased by 1.5-fold (P less than 0.05) after 7 days of overload. The data indicate that 1) the initial rise in ALV synthase mRNA and activity due to overload occurs in the absence of a prior change in the level of cytochrome oxidase, an enzyme that requires heme for its assembly, and 2) induction of ALV synthase activity is regulated largely by processes at the translational or posttranslational steps.
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PMID:Regulation of 5'-aminolevulinate synthase activity in overloaded skeletal muscle. 238 4

With the electro-driven import of rhodamine 123, we used single cell fluorescence microscopy to single out the contribution of nitric oxide (NO) in controlling mitochondrial membrane potential expressed by (stationary growing) rhabdomyosarcoma and neuroblastoma cells in culture. The experimental design and the computer-aided image analysis detected and quantitated variations of fluorescence signals specific to mitochondria. We observed that 1) the two cell lines display changes of fluorescence dependent on mitochondrial energization states; 2) mitochondrial fluorescence decreases after exposure of the cells to a NO releaser; 4) the different fluorescence intensity measured under stationary growing conditions, or after activation and inhibition of constitutive NO synthase, is consistent with a steady-state production of NO. Direct comparison of single cell fluorescence with bulk cytofluorimetry proved that the results obtained by the latter method may be misleading because of the intrinsic-to-measure lack of information about distribution of fluorescence within different cell compartments. The kinetic parameters describing the reactions between cytochrome oxidase, NO, and O2 may account for the puzzling (20-fold) increase of the KM for O2 reported for cells and tissues as compared to purified cytochrome c oxidase, allowing an estimate of in vivo NO flux.
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PMID:Modulation of mitochondrial respiration by nitric oxide: investigation by single cell fluorescence microscopy. 987 43

Glucagon promotes hepatic glucose production maintaining glucose homeostasis in the fasting state. Glucagon maintains at high level in both diabetic animals and human, contributing to hyperglycemia. Mitochondria, a major place for glucose oxidation, are dysfunctional in diabetic condition. However, whether hepatic mitochondrial function can be affected by glucagon remains unknown. Recently, we reported that FOXO1 is an important mediator in glucagon signaling in control of glucose homeostasis. In this study, we further assessed the role of FOXO1 in the action of glucagon in the regulation of hepatic mitochondrial function. We found that glucagon decreased the heme production in a FOXO1-dependent manner, suppressed heme-dependent complex III (UQCRC1) and complex IV (MT-CO1) and inhibited hepatic mitochondrial function. However, the suppression of mitochondrial function by glucagon was largely rescued by deleting the Foxo1 gene in hepatocytes. Glucagon tends to reduce hepatic mitochondrial biogenesis by attenuating the expression of NRF1, TFAM and MFN2, which is mediated by FOXO1. In db/db mice, we found that hepatic mitochondrial function was suppressed and expression levels of UQCRC1, MT-CO1, NRF1 and TFAM were downregulated in the liver. These findings suggest that hepatic mitochondrial function can be impaired when hyperglucagonemia occurs in the patients with diabetes mellitus, resulting in organ failure.
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PMID:Glucagon regulates hepatic mitochondrial function and biogenesis through FOXO1. 3102 11