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Presence of three acyl-CoA oxidases in rat liver peroxisomes. An inducible fatty acyl-CoA oxidase, a noninducible fatty acyl-CoA oxidase, and a noninducible trihydroxycoprostanoyl-CoA oxidase.
J Biol Chem. 1990 Mar 25; 265(9):5242-6.JB

Abstract

Mammalian liver peroxisomes are capable of beta-oxidizing a variety of substrates including very long chain fatty acids and the side chains of the bile acid intermediates di- and trihydroxycoprostanic acid. The first enzyme of peroxisomal beta-oxidation is acyl-CoA oxidase. It remains unknown whether peroxisomes possess one or several acyl-CoA oxidases. Peroxisomal oxidases from rat liver were partially purified by (NH4)2SO4 precipitation and heat treatment, and the preparation was subjected to chromatofocusing, chromatography on hydroxylapatite and dye affinity matrices, and gel filtration. The column eluates were assayed for palmitoyl-CoA and trihydroxycoprostanoyl-CoA oxidase activities and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The results revealed the presence of three acyl-CoA oxidases: 1) a fatty acyl-CoA oxidase with a pI of 8.3 and an apparent molecular mass of 145 kDa. The enzyme consisted mainly of 52- and 22.5-kDa subunits and could be induced by clofibrate treatment; 2) a noninducible fatty acyl-CoA oxidase with a pI of 7.1 and an apparent molecular mass of 427 kDa. It consisted mainly, if not exclusively, of one polypeptide component of 71 kDa; and 3) a noninducile trihydroxycoprostanoyl-CoA oxidase with a pI of 7.1 and an apparent molecular mass of 139 kDa. It consisted mainly, if not exclusively, of one polypeptide component of 69 kDa. Our findings are probably related to the recent discovery of two species of acyl-CoA oxidase mRNA in rat liver (Miyazawa, S., Hayashi, H., Hijikata, M., Ishii, N., Furata, S., Kagamiyama, H., Osumi, T., and Hashimoto, T. (1987) J. Biol. Chem. 262, 8131-8137) and they probably also explain why in human peroxisomal beta-oxidation defects an accumulation of very long chain fatty acids is not always accompanied by an excretion of bile acid intermediates and vice versa.

Authors+Show Affiliations

Katholieke Universiteit Leuven, Afdeling Farmacologie, Belgium.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

2156865

Citation

Schepers, L, et al. "Presence of Three acyl-CoA Oxidases in Rat Liver Peroxisomes. an Inducible Fatty acyl-CoA Oxidase, a Noninducible Fatty acyl-CoA Oxidase, and a Noninducible trihydroxycoprostanoyl-CoA Oxidase." The Journal of Biological Chemistry, vol. 265, no. 9, 1990, pp. 5242-6.
Schepers L, Van Veldhoven PP, Casteels M, et al. Presence of three acyl-CoA oxidases in rat liver peroxisomes. An inducible fatty acyl-CoA oxidase, a noninducible fatty acyl-CoA oxidase, and a noninducible trihydroxycoprostanoyl-CoA oxidase. J Biol Chem. 1990;265(9):5242-6.
Schepers, L., Van Veldhoven, P. P., Casteels, M., Eyssen, H. J., & Mannaerts, G. P. (1990). Presence of three acyl-CoA oxidases in rat liver peroxisomes. An inducible fatty acyl-CoA oxidase, a noninducible fatty acyl-CoA oxidase, and a noninducible trihydroxycoprostanoyl-CoA oxidase. The Journal of Biological Chemistry, 265(9), 5242-6.
Schepers L, et al. Presence of Three acyl-CoA Oxidases in Rat Liver Peroxisomes. an Inducible Fatty acyl-CoA Oxidase, a Noninducible Fatty acyl-CoA Oxidase, and a Noninducible trihydroxycoprostanoyl-CoA Oxidase. J Biol Chem. 1990 Mar 25;265(9):5242-6. PubMed PMID: 2156865.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Presence of three acyl-CoA oxidases in rat liver peroxisomes. An inducible fatty acyl-CoA oxidase, a noninducible fatty acyl-CoA oxidase, and a noninducible trihydroxycoprostanoyl-CoA oxidase. AU - Schepers,L, AU - Van Veldhoven,P P, AU - Casteels,M, AU - Eyssen,H J, AU - Mannaerts,G P, PY - 1990/3/25/pubmed PY - 1990/3/25/medline PY - 1990/3/25/entrez SP - 5242 EP - 6 JF - The Journal of biological chemistry JO - J Biol Chem VL - 265 IS - 9 N2 - Mammalian liver peroxisomes are capable of beta-oxidizing a variety of substrates including very long chain fatty acids and the side chains of the bile acid intermediates di- and trihydroxycoprostanic acid. The first enzyme of peroxisomal beta-oxidation is acyl-CoA oxidase. It remains unknown whether peroxisomes possess one or several acyl-CoA oxidases. Peroxisomal oxidases from rat liver were partially purified by (NH4)2SO4 precipitation and heat treatment, and the preparation was subjected to chromatofocusing, chromatography on hydroxylapatite and dye affinity matrices, and gel filtration. The column eluates were assayed for palmitoyl-CoA and trihydroxycoprostanoyl-CoA oxidase activities and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The results revealed the presence of three acyl-CoA oxidases: 1) a fatty acyl-CoA oxidase with a pI of 8.3 and an apparent molecular mass of 145 kDa. The enzyme consisted mainly of 52- and 22.5-kDa subunits and could be induced by clofibrate treatment; 2) a noninducible fatty acyl-CoA oxidase with a pI of 7.1 and an apparent molecular mass of 427 kDa. It consisted mainly, if not exclusively, of one polypeptide component of 71 kDa; and 3) a noninducile trihydroxycoprostanoyl-CoA oxidase with a pI of 7.1 and an apparent molecular mass of 139 kDa. It consisted mainly, if not exclusively, of one polypeptide component of 69 kDa. Our findings are probably related to the recent discovery of two species of acyl-CoA oxidase mRNA in rat liver (Miyazawa, S., Hayashi, H., Hijikata, M., Ishii, N., Furata, S., Kagamiyama, H., Osumi, T., and Hashimoto, T. (1987) J. Biol. Chem. 262, 8131-8137) and they probably also explain why in human peroxisomal beta-oxidation defects an accumulation of very long chain fatty acids is not always accompanied by an excretion of bile acid intermediates and vice versa. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/2156865/Presence_of_three_acyl_CoA_oxidases_in_rat_liver_peroxisomes__An_inducible_fatty_acyl_CoA_oxidase_a_noninducible_fatty_acyl_CoA_oxidase_and_a_noninducible_trihydroxycoprostanoyl_CoA_oxidase_ DB - PRIME DP - Unbound Medicine ER -