Isolation and structural organization of the human preproenkephalin Bgene

Saburo Horikawa; Toshiyuki Takai; Mitsuyoshi Toyosato; Hideo Takahashi; Masaharu Noda; Hitoshi Kakidani; Tai Kubo; Tadaaki Hirose; Seiichi Inayama; Hidenori Hayashida; Takashi Miyata; Shosaku Numa

doi:10.1038/306611a0

Isolation and structural organization of the human preproenkephalin Bgene

Saburo Horikawa, Toshiyuki Takai, Mitsuyoshi Toyosato, Hideo Takahashi, Masaharu Noda, Hitoshi Kakidani, Tai Kubo, Tadaaki Hirose, Seiichi Inayama, Hidenori Hayashida, Takashi Miyata, Shosaku Numa

Division of Aging Science

Research output: Contribution to journal › Article › peer-review

167 Citations (Scopus)

Abstract

The primary structure of porcine preproenkephalin B has been elucidated by cloning and sequencing cDNA¹: it contains neoendorphin^2,3, dynorphin^4,5 and leumorphin^1,6,7 (containing rimorphin as its ammo-terminus)^8,9. These opioid peptides, each having a leucine-enkephalin structure¹⁰, act on the κ-receptor ^7,11-14. We have now cloned a human genomic DNA segment containing the preproenkephalin B gene. The structural organization of this gene resembles those of the genes encoding the other opioid peptide precursors, that is, preproenkephalin A¹⁵ and the corticotropin-β-lipotropin precursor^16-21 (ACTH-β-LPH precursor). The primary structure of human preproenkephalin B has been deduced from the gene sequence. The amino acid sequence homology observed between preproenkephalin B and preproenkephalin A, together with the similarity between their gene organizations, suggests that the two genes have been generated from a common ancestor by gene duplication.

Original language	English
Pages (from-to)	611-614
Number of pages	4
Journal	Nature
Volume	306
Issue number	5943
DOIs	https://doi.org/10.1038/306611a0
Publication status	Published - 1983

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Isolation and structural organization of the human preproenkephalin Bgene. / Horikawa, Saburo; Takai, Toshiyuki; Toyosato, Mitsuyoshi; Takahashi, Hideo; Noda, Masaharu; Kakidani, Hitoshi; Kubo, Tai; Hirose, Tadaaki; Inayama, Seiichi; Hayashida, Hidenori; Miyata, Takashi; Numa, Shosaku.

In: Nature, Vol. 306, No. 5943, 1983, p. 611-614.

Research output: Contribution to journal › Article › peer-review

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title = "Isolation and structural organization of the human preproenkephalin Bgene",

abstract = "The primary structure of porcine preproenkephalin B has been elucidated by cloning and sequencing cDNA1: it contains neoendorphin2,3, dynorphin4,5 and leumorphin1,6,7 (containing rimorphin as its ammo-terminus)8,9. These opioid peptides, each having a leucine-enkephalin structure10, act on the κ-receptor 7,11-14. We have now cloned a human genomic DNA segment containing the preproenkephalin B gene. The structural organization of this gene resembles those of the genes encoding the other opioid peptide precursors, that is, preproenkephalin A15 and the corticotropin-β-lipotropin precursor16-21 (ACTH-β-LPH precursor). The primary structure of human preproenkephalin B has been deduced from the gene sequence. The amino acid sequence homology observed between preproenkephalin B and preproenkephalin A, together with the similarity between their gene organizations, suggests that the two genes have been generated from a common ancestor by gene duplication.",

author = "Saburo Horikawa and Toshiyuki Takai and Mitsuyoshi Toyosato and Hideo Takahashi and Masaharu Noda and Hitoshi Kakidani and Tai Kubo and Tadaaki Hirose and Seiichi Inayama and Hidenori Hayashida and Takashi Miyata and Shosaku Numa",

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T1 - Isolation and structural organization of the human preproenkephalin Bgene

AU - Horikawa, Saburo

AU - Takai, Toshiyuki

AU - Toyosato, Mitsuyoshi

AU - Takahashi, Hideo

AU - Noda, Masaharu

AU - Kakidani, Hitoshi

AU - Kubo, Tai

AU - Hirose, Tadaaki

AU - Inayama, Seiichi

AU - Hayashida, Hidenori

AU - Miyata, Takashi

AU - Numa, Shosaku

PY - 1983

Y1 - 1983

N2 - The primary structure of porcine preproenkephalin B has been elucidated by cloning and sequencing cDNA1: it contains neoendorphin2,3, dynorphin4,5 and leumorphin1,6,7 (containing rimorphin as its ammo-terminus)8,9. These opioid peptides, each having a leucine-enkephalin structure10, act on the κ-receptor 7,11-14. We have now cloned a human genomic DNA segment containing the preproenkephalin B gene. The structural organization of this gene resembles those of the genes encoding the other opioid peptide precursors, that is, preproenkephalin A15 and the corticotropin-β-lipotropin precursor16-21 (ACTH-β-LPH precursor). The primary structure of human preproenkephalin B has been deduced from the gene sequence. The amino acid sequence homology observed between preproenkephalin B and preproenkephalin A, together with the similarity between their gene organizations, suggests that the two genes have been generated from a common ancestor by gene duplication.

AB - The primary structure of porcine preproenkephalin B has been elucidated by cloning and sequencing cDNA1: it contains neoendorphin2,3, dynorphin4,5 and leumorphin1,6,7 (containing rimorphin as its ammo-terminus)8,9. These opioid peptides, each having a leucine-enkephalin structure10, act on the κ-receptor 7,11-14. We have now cloned a human genomic DNA segment containing the preproenkephalin B gene. The structural organization of this gene resembles those of the genes encoding the other opioid peptide precursors, that is, preproenkephalin A15 and the corticotropin-β-lipotropin precursor16-21 (ACTH-β-LPH precursor). The primary structure of human preproenkephalin B has been deduced from the gene sequence. The amino acid sequence homology observed between preproenkephalin B and preproenkephalin A, together with the similarity between their gene organizations, suggests that the two genes have been generated from a common ancestor by gene duplication.

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