The Role of Heme and Iron-Sulfur Clusters in Mitochondrial Biogenesis, Maintenance, and Decay with Age

Atamna, Hani; Walter, Patrick; Ames, Bruce N.

doi:10.1006/abbi.2001.2671

Cited by 108 publications

(104 citation statements)

References 113 publications

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“…The four complexes of the electron transport chain are essential for ATP production by oxidative phosphorylation and are the main source of free radicals that contribute to mitochondrial damage associated with aging and various diseases [109][110][111][112][113]. In heme-deficient conditions, the activity and protein content of complex IV decreases by more than 95% [7]. Complex II and cytochrome c are affected by heme deficiency to a lesser extent, while complexes I and III remain intact during heme shortage [7].…”

Section: Dysregulation Of Heme Levels Can Cause Serious Diseasesmentioning

confidence: 99%

“…In heme-deficient conditions, the activity and protein content of complex IV decreases by more than 95% [7]. Complex II and cytochrome c are affected by heme deficiency to a lesser extent, while complexes I and III remain intact during heme shortage [7]. The activity of complex IV undergoes a 30% to 50% reduction with aging and in Alzheimer's patients; however, the reason for this decline remains unclear [102,114,115].…”

Section: Dysregulation Of Heme Levels Can Cause Serious Diseasesmentioning

confidence: 99%

“…The remaining four enzymes involved in heme synthesis are localized in the cytosol [1,3,4]. The control of heme biosynthesis is complex and is dependent on multiple factors, including cell type and the availability of substrates [5][6][7]. Heme synthesis requires the key precursor 5-aminolevulinic acid (ALA) and two substrates, oxygen and ferrous iron (Fe 2+ ) ( Figure 1, Table 1) [1,3,7].…”

Section: Introductionmentioning

confidence: 99%

“…The control of heme biosynthesis is complex and is dependent on multiple factors, including cell type and the availability of substrates [5][6][7]. Heme synthesis requires the key precursor 5-aminolevulinic acid (ALA) and two substrates, oxygen and ferrous iron (Fe 2+ ) ( Figure 1, Table 1) [1,3,7]. The availability of each of these molecules may be limiting and may dictate the rate of heme synthesis, under certain circumstances [7].…”

Section: Introductionmentioning

confidence: 99%

“…Heme synthesis requires the key precursor 5-aminolevulinic acid (ALA) and two substrates, oxygen and ferrous iron (Fe 2+ ) ( Figure 1, Table 1) [1,3,7]. The availability of each of these molecules may be limiting and may dictate the rate of heme synthesis, under certain circumstances [7]. For example, in yeast, heme synthesis is under the control of oxygen level [3,5,8].…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

Heme: a versatile signaling molecule controlling the activities of diverse regulators ranging from transcription factors to MAP kinases

2006

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Section: Dysregulation Of Heme Levels Can Cause Serious Diseasesmentioning

confidence: 99%

Section: Dysregulation Of Heme Levels Can Cause Serious Diseasesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Heme: a versatile signaling molecule controlling the activities of diverse regulators ranging from transcription factors to MAP kinases

2006

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Isatin, an endogenous nonpeptide biofactor: A review of its molecular targets, mechanisms of actions, and their biomedical implications

et al. 2018

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Isatin (indole-2,3-dione) is an oxidized indole. It is widely distributed in mammalian tissues and body fluids, where isatin concentrations vary significantly from <0.1 to > 10 µM. Isatin output is increased under conditions of stress. Exogenously administered isatin is characterized by low toxicity, mutagenicity, and genotoxicity in vivo. Cytotoxic effects of isatin on various cell cultures are usually observed at concentrations exceeding 100 µM. Binding of [ H]isatin to rat brain sections is consistent with its physiological concentrations. Proteomic analysis of mouse and rat brain isatin-binding proteins revealed about 90 individual proteins, which demonstrated significant interspecies differences (rat versus mouse). Certain evidence exist that redox state(s) and possibly other types of posttranslational modifications regulate affinity of target proteins to isatin. Recent data suggest that interacting with numerous intracellular isatin binding proteins, isatin can act as a regulator of complex protein networks in norm and pathology. Physiological concentrations of isatin in vitro inhibit monoamine oxidase B and natriuretic peptide receptor guanylate cyclase, higher (neuroprotective) concentrations (50-400 μM) cause apoptosis of various (including malignant tumor) cell lines and influence expression of certain apoptosis-related genes. Being administered in vivo, isatin exhibits various behavioral effects; it attenuates manifestations of MPTP-induced parkinsonism and tumor growth in experimental animal models. © 2017 BioFactors, 44(2):95-108, 2018.

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Regulatory Fe^II/III Heme: The Reconstruction of a Molecule's Biography

Kühl

Imhof

2014

ChemBioChem

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More than 20 years of research on heme as a temporary effector molecule of proteins have revealed its widespread impact on virtually all primary functions in the human organism. As our understanding of this influence is still growing, a comprehensive overview of compiled data will give fresh impetus for creativity and developing new strategies in heme-related research. From known data concerning heme-regulated proteins and their involvement in the development of diseases, we provide concise information of Fe(II/III) heme as a regulator and the availability of "regulatory heme". The latter is dependent on the balance between free and bound Fe(II/III) heme, here termed "hemeostasis". Imbalance of this system can lead to the development of diseases that were not always attributed to this small molecule. Diseases such as cancer or Alzheimer's disease highlight the reawakened interest in heme, whose function was previously believed to be completely understood.

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The Role of Heme and Iron-Sulfur Clusters in Mitochondrial Biogenesis, Maintenance, and Decay with Age

Cited by 108 publications

References 113 publications

Heme: a versatile signaling molecule controlling the activities of diverse regulators ranging from transcription factors to MAP kinases

Heme: a versatile signaling molecule controlling the activities of diverse regulators ranging from transcription factors to MAP kinases

Isatin, an endogenous nonpeptide biofactor: A review of its molecular targets, mechanisms of actions, and their biomedical implications

Regulatory Fe^II/III Heme: The Reconstruction of a Molecule's Biography

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The Role of Heme and Iron-Sulfur Clusters in Mitochondrial Biogenesis, Maintenance, and Decay with Age

Cited by 108 publications

References 113 publications

Heme: a versatile signaling molecule controlling the activities of diverse regulators ranging from transcription factors to MAP kinases

Heme: a versatile signaling molecule controlling the activities of diverse regulators ranging from transcription factors to MAP kinases

Isatin, an endogenous nonpeptide biofactor: A review of its molecular targets, mechanisms of actions, and their biomedical implications

Regulatory FeII/III Heme: The Reconstruction of a Molecule's Biography

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Product

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Regulatory Fe^II/III Heme: The Reconstruction of a Molecule's Biography