Molecular Regulation of Heme Biosynthesis in Higher Vertebrates
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2020, Mechanisms of Ageing and DevelopmentCitation Excerpt :NRF1 was first identified as a positive regulator of cytochrome c transcription and since then its role in the transcription of nuclear-encoded mitochondrial transcripts has expanded (Evans and Scarpulla, 1989). Particularly, NRF1 forms homodimers and positively regulates the expression of several components of the oxidative phosphorylation pathway, the mitochondrial protein import machinery, ion channel components and heme biosynthesis enzymes (Biswas and Chan, 2010; Blesa et al., 2008b, 2007; Kiyama et al., 2018; May et al., 1995; Satoh et al., 2013; Virbasius et al., 1993). In addition, it indirectly controls mitochondrial genome expression, through binding on the promoter regions of the principal mtDNA regulators, mitochondrial transcription factor A (TFAM) and the assistant factors mitochondrial transcription factor B1 (TFB1M) and mitochondrial transcription factor B2 (TFB2M), yet results about TFAM are inconsistent (Baar et al., 2003; Gleyzer et al., 2005; Virbasius and Scarpulla, 1994).
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2018, Liver ResearchCitation Excerpt :Heme is required for various cellular functions such as oxygen transport in hemoglobin and electron transport in hemoproteins like the CYPs.72,73 Heme is synthesized in the liver and bone marrow by a series of well-controlled enzymatic processes that starts with the condensation of succinyl coA and glycine by the first and rate limiting enzyme alanine synthase 1 (ALAS1); and ends with the insertion of ferrous iron into the protoporphyrin Ⅸ (PPⅨ) ring to form heme by ferrochelatase (FECH).72 Both mPXR and hPXR have been reported to upregulate the expression of ALAS1 by binding to the ALAS1 drug-responsive enhancer sequences in the 5′ flanking region of ALAS1.74,75
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2017, GeneCitation Excerpt :In general, heme plays a fundamental role in many crucial biochemical reactions, and its biosynthesis is finely tuned to these requirements which vary significantly among various cells and tissues. There is a dramatic difference in synthetic rates because 85% of organismal heme is synthesized in erythroid cells (May et al., 1995). The heme synthesis rate in erythroid cells depends on the availability of iron for ferrochelatase (Ponka, 1997).