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Cloning of a human cDNA encoding a novel enzyme involved in the elongation of long-chain polyunsaturated fatty acids.
Biochem J 2000; 350 Pt 3:765-70BJ

Abstract

The Saccharomyces cerevisiae protein ELO2p is involved in the elongation of saturated and monounsaturated fatty acids. Among several sequences with limited identity with the S. cerevisiae ELO2 gene, a consensus cDNA sequence was identified from the LifeSeq(R) database of Incyte Pharmaceuticals, Inc. Human liver cDNA was amplified by PCR using oligonucleotides complementary to the 5' and 3' ends of the putative human cDNA sequence. The resulting full-length sequence, termed HELO1, consisted of 897 bp, which encoded 299 amino acids. However, in contrast with the ELO2 gene, expression of this open reading frame in S. cerevisiae demonstrated that the encoded protein was involved in the elongation of long-chain polyunsaturated fatty acids, as determined by the conversion of gamma-linolenic acid (C(18:3, n-6)) into dihomo-gamma-linolenic acid (C(20:3, n-6)), arachidonic acid (C(20:4, n-6)) into adrenic acid (C(22:4, n-6)), stearidonic acid (C(18:4, n-3)) into eicosatetraenoic acid (C(20:4, n-3)), eicosapentaenoic acid (C(20:5, n-3)) into omega3-docosapentaenoic acid (C(22:5, n-3)) and alpha-linolenic acid (C(18:3, n-3)) into omega3-eicosatrienoic acid (C(20:3, n-3)). The predicted amino acid sequence of the open reading frame had only 29% identity with the yeast ELO2 sequence, contained a single histidine-rich domain and had six transmembrane-spanning regions, as suggested by hydropathy analysis. The tissue expression profile revealed that the HELO1 gene is highly expressed in the adrenal gland and testis. Furthermore, the HELO1 gene is located on chromosome 6, best known for encoding the major histocompatibility complex, which is essential to the human immune response.

Authors+Show Affiliations

Department of Strategic Discovery Research, Ross Products Division, Abbott Laboratories, 3300 Stelzer Road, Columbus, OH 43219, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

10970790

Citation

Leonard, A E., et al. "Cloning of a Human cDNA Encoding a Novel Enzyme Involved in the Elongation of Long-chain Polyunsaturated Fatty Acids." The Biochemical Journal, vol. 350 Pt 3, 2000, pp. 765-70.
Leonard AE, Bobik EG, Dorado J, et al. Cloning of a human cDNA encoding a novel enzyme involved in the elongation of long-chain polyunsaturated fatty acids. Biochem J. 2000;350 Pt 3:765-70.
Leonard, A. E., Bobik, E. G., Dorado, J., Kroeger, P. E., Chuang, L. T., Thurmond, J. M., ... Mukerji, P. (2000). Cloning of a human cDNA encoding a novel enzyme involved in the elongation of long-chain polyunsaturated fatty acids. The Biochemical Journal, 350 Pt 3, pp. 765-70.
Leonard AE, et al. Cloning of a Human cDNA Encoding a Novel Enzyme Involved in the Elongation of Long-chain Polyunsaturated Fatty Acids. Biochem J. 2000 Sep 15;350 Pt 3:765-70. PubMed PMID: 10970790.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Cloning of a human cDNA encoding a novel enzyme involved in the elongation of long-chain polyunsaturated fatty acids. AU - Leonard,A E, AU - Bobik,E G, AU - Dorado,J, AU - Kroeger,P E, AU - Chuang,L T, AU - Thurmond,J M, AU - Parker-Barnes,J M, AU - Das,T, AU - Huang,Y S, AU - Mukerji,P, PY - 2000/9/6/pubmed PY - 2001/2/28/medline PY - 2000/9/6/entrez SP - 765 EP - 70 JF - The Biochemical journal JO - Biochem. J. VL - 350 Pt 3 N2 - The Saccharomyces cerevisiae protein ELO2p is involved in the elongation of saturated and monounsaturated fatty acids. Among several sequences with limited identity with the S. cerevisiae ELO2 gene, a consensus cDNA sequence was identified from the LifeSeq(R) database of Incyte Pharmaceuticals, Inc. Human liver cDNA was amplified by PCR using oligonucleotides complementary to the 5' and 3' ends of the putative human cDNA sequence. The resulting full-length sequence, termed HELO1, consisted of 897 bp, which encoded 299 amino acids. However, in contrast with the ELO2 gene, expression of this open reading frame in S. cerevisiae demonstrated that the encoded protein was involved in the elongation of long-chain polyunsaturated fatty acids, as determined by the conversion of gamma-linolenic acid (C(18:3, n-6)) into dihomo-gamma-linolenic acid (C(20:3, n-6)), arachidonic acid (C(20:4, n-6)) into adrenic acid (C(22:4, n-6)), stearidonic acid (C(18:4, n-3)) into eicosatetraenoic acid (C(20:4, n-3)), eicosapentaenoic acid (C(20:5, n-3)) into omega3-docosapentaenoic acid (C(22:5, n-3)) and alpha-linolenic acid (C(18:3, n-3)) into omega3-eicosatrienoic acid (C(20:3, n-3)). The predicted amino acid sequence of the open reading frame had only 29% identity with the yeast ELO2 sequence, contained a single histidine-rich domain and had six transmembrane-spanning regions, as suggested by hydropathy analysis. The tissue expression profile revealed that the HELO1 gene is highly expressed in the adrenal gland and testis. Furthermore, the HELO1 gene is located on chromosome 6, best known for encoding the major histocompatibility complex, which is essential to the human immune response. SN - 0264-6021 UR - https://www.unboundmedicine.com/medline/citation/10970790/Cloning_of_a_human_cDNA_encoding_a_novel_enzyme_involved_in_the_elongation_of_long_chain_polyunsaturated_fatty_acids_ L2 - https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/10970790/ DB - PRIME DP - Unbound Medicine ER -