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Gene Review

Alas1  -  5'-aminolevulinate synthase 1

Rattus norvegicus

Synonyms: 5-aminolevulinate synthase, nonspecific, mitochondrial, 5-aminolevulinic acid synthase 1, ALAS-H, Delta-ALA synthase 1, Delta-aminolevulinate synthase 1
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Disease relevance of Alas1


High impact information on Alas1


Chemical compound and disease context of Alas1

  • Our findings indicate that chloroquine acts by reduction of the delta-aminolevulinate synthase activity, probably by influencing the regulation of the key enzyme of the heme biosynthesis, which is enhanced in human porphyria cutanea tarda, as well as in the HCB-induced porphyria of the rats [10].

Biological context of Alas1


Anatomical context of Alas1


Associations of Alas1 with chemical compounds


Other interactions of Alas1


Analytical, diagnostic and therapeutic context of Alas1

  • In this study, we examined expression of HO-1 as well as non-specific delta-aminolevulinate synthase (ALAS1), the rate-limiting enzyme in heme catabolism and biosynthesis, respectively, in a rat model of PH produced by subcutaneous injection of MCT (60 mg/kg) [1].
  • These data indicate that hydrocortisone and adrenalectomy can significantly influence the extent of the induction of heme oxygenase produced by CoCl2, but that both the initial decline and the rebound induction of delta-aminolevulinate synthase associated with this metal treatment are apparently independent of these endocrine controls [7].
  • Partial hepatectomy produced a significant depression in delta-ALA synthetase and delta-ALA dehydratase, and induction in haem oxygenase at an early stage of regeneration [29].


  1. Increased pulmonary heme oxygenase-1 and delta-aminolevulinate synthase expression in monocrotaline-induced pulmonary hypertension. Iwasaki, T., Takahashi, T., Shimizu, H., Ohmori, E., Morimoto, T., Kajiya, M., Takeuchi, M., Morita, K., Akagi, R., Kajiya, F. Current neurovascular research. (2005) [Pubmed]
  2. Tissue-specific gene expression of heme oxygenase-1 (HO-1) and non-specific delta-aminolevulinate synthase (ALAS-N) in a rat model of septic multiple organ dysfunction syndrome. Suzuki, T., Takahashi, T., Yamasaki, A., Fujiwara, T., Hirakawa, M., Akagi, R. Biochem. Pharmacol. (2000) [Pubmed]
  3. Cimetidine suppresses chemically induced experimental hepatic porphyria. Marcus, D.L., Nadel, H., Lew, G., Freedman, M.L. Am. J. Med. Sci. (1990) [Pubmed]
  4. Aging-related decreases in hepatic mitochondrial and cytosolic delta-aminolevulinic acid synthase during experimental porphyria. Scotto, A.W., Rinehart, R.W., Beattie, D.S. Arch. Biochem. Biophys. (1983) [Pubmed]
  5. The cytochrome P-450-depleted animal: an experimental model for in vivo studies in chemical biology. Drummond, G.S., Kappas, A. Proc. Natl. Acad. Sci. U.S.A. (1982) [Pubmed]
  6. Cobalt inhibition of synthesis and induction of delta-aminolevulinate synthase in liver. Maines, M.D., Janousĕk, V., Tomio, J.M., Kappas, A. Proc. Natl. Acad. Sci. U.S.A. (1976) [Pubmed]
  7. Adrenalectomy enhances the induction of heme oxygenase and the degradation of cytochrome P-450 in liver. Sardana, M.K., Sassa, S., Kappas, A. J. Biol. Chem. (1980) [Pubmed]
  8. Translocation of delta-aminolevulinate synthase from the cytosol to the mitochondria and its regulation by hemin in the rat liver. Yamauchi, K., Hayashi, N., Kikuchi, G. J. Biol. Chem. (1980) [Pubmed]
  9. Thyroid hormone regulation of heme synthesis in rat liver. Smith, T.J., Drummond, G.S. Endocrinology (1988) [Pubmed]
  10. Influence of chloroquine on the porphyrin metabolism. Goerz, G., Bolsen, K., Merk, H. Arch. Dermatol. Res. (1985) [Pubmed]
  11. Paraquat-generated oxidative stress in rat liver induces heme oxygenase-1 and aminolevulinic acid synthase. Noriega, G.O., Gonzales, S., Tomaro, M.L., Batlle, A.M. Free Radic. Res. (2002) [Pubmed]
  12. Gene expression of heme oxygenase-1 during glial activation by lipopolysaccharide. Tsukiji, T., Takahashi, T., Mizobuchi, S., Suzuki, T., Hirakawa, M., Watanabe, S., Akagi, R. Res. Commun. Mol. Pathol. Pharmacol. (2000) [Pubmed]
  13. Heme metabolism and erythropoiesis in abnormal iron states: role of delta-aminolevulinic acid synthase and heme oxygenase. Abraham, N.G., Lutton, J.D., Levere, R.D. Exp. Hematol. (1985) [Pubmed]
  14. Lead-induced oxidative stress and hematological alterations and their response to combined administration of calcium disodium EDTA with a thiol chelator in rats. Saxena, G., Flora, S.J. J. Biochem. Mol. Toxicol. (2004) [Pubmed]
  15. Novel regulation of delta-aminolevulinate synthase in the rat harderian gland. Nagai, M., Nagai, T., Yamamoto, M., Goto, K., Bishop, T.R., Hayashi, N., Kondo, H., Seyama, Y., Kano, K., Fujita, H., Sassa, S. Biochem. Pharmacol. (1997) [Pubmed]
  16. Purification and some properties of delta-aminolevulinate synthase from the rat liver cytosol fraction and immunochemical identity of the cytosolic enzyme and the mitochondrial enzyme. Nakakuki, M., Yamauchi, K., Hayashi, N., Kikuchi, G. J. Biol. Chem. (1980) [Pubmed]
  17. Studies on induction of delta-aminolevulinic acid synthase, ferrochelatase, cytochrome P-450 and cyclic AMP by phenformin. Chlorpropamide, allylisopropylacetamide and lead in hepatocytes from normal and experimental diabetic rats. Cánepa, E.T., Llambías, E.B., Grinstein, M. Biochem. Pharmacol. (1990) [Pubmed]
  18. Impairment of mitochondrial 5-aminolevulinic acid synthase activity in Gunn rat liver. Celier, C., Francois, D., Marsac, C., Cresteil, T. Biochem. Pharmacol. (1992) [Pubmed]
  19. Structure, turnover, and heme-mediated suppression of the level of mRNA encoding rat liver delta-aminolevulinate synthase. Yamamoto, M., Kure, S., Engel, J.D., Hiraga, K. J. Biol. Chem. (1988) [Pubmed]
  20. Effect of aluminum on hematopoiesis after intraperitoneal exposure in rats. Chmielnicka, J., Nasiadek, M., Lewandowska-Zyndul, E., Pińkowski, R. Ecotoxicol. Environ. Saf. (1996) [Pubmed]
  21. Effect of gossypol in association with chromium protoporphyrin on heme metabolic enzymes. Aneja, R., Dass, S.K., Prakash, S., Chandra, R. Artificial cells, blood substitutes, and immobilization biotechnology. (2004) [Pubmed]
  22. Effect of cimetidine on delta-aminolevulinic acid synthase and microsomal heme oxygenase in rat liver. Marcus, D.L., Halbrecht, J.L., Bourque, A.L., Lew, G., Nadel, H., Freedman, M.L. Biochem. Pharmacol. (1984) [Pubmed]
  23. Protective role of heme oxygenase-1 in the intestinal tissue injury in an experimental model of sepsis. Fujii, H., Takahashi, T., Nakahira, K., Uehara, K., Shimizu, H., Matsumi, M., Morita, K., Hirakawa, M., Akagi, R., Sassa, S. Crit. Care Med. (2003) [Pubmed]
  24. Involvement of heme in the transcriptional activation of CYPIIB1/B2 gene by phenobarbitone in rat liver--studies with succinylacetone. Venkateswar, V., Padmanaban, G. Arch. Biochem. Biophys. (1991) [Pubmed]
  25. Acute effect of amitriptyline, phenobarbital or cobaltous chloride on delta-aminolevulinic acid synthetase, heme oxygenase and microsomal heme content and drug metabolism in rat liver. Hoshi, K., Senda, N., Fujino, S. Jpn. J. Pharmacol. (1989) [Pubmed]
  26. Inhibition of delta-aminolevulinate dehydratase in trichloroethylene-exposed rats, and the effects on heme regulation. Fujita, H., Koizumi, A., Yamamoto, M., Kumai, M., Sadamoto, T., Ikeda, M. Biochim. Biophys. Acta (1984) [Pubmed]
  27. Tissue-specific stability of nuclear- and mitochondrially encoded mRNAs. Connor, M.K., Takahashi, M., Hood, D.A. Arch. Biochem. Biophys. (1996) [Pubmed]
  28. Effects of iron overload on bile secretion and hepatic porphyrin metabolism in ethinyl estradiol-treated rats. Cantoni, L., Di Padova, C., Rizzardini, M., Dal Fiume, D., Graziani, A., Rovagnati, P., Tritapepe, R. Toxicology (1986) [Pubmed]
  29. Haem and drug-metabolizing enzymes in regenerating rat liver. Srivastava, R.C., Dwivedi, R.S., Kaur, G., Srivastava, R. British journal of experimental pathology. (1982) [Pubmed]
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