Analysis of endothelin related peptides in culture supernatant of porcine aortic endothelial cells

Evidence for biosynthetic pathway of endothelin-1

Tatsuya Sawamura, Sadao Kimura, Osamu Shinmi, Yoshiki Sugita, Masashi Yanagisawa, Tomoh Masaki

Research output: Contribution to journalArticle

84 Citations (Scopus)

Abstract

We investigated the molecular forms of endothelin (ET) related peptides in culture supernatant of porcine aortic endothelial cells by high performance liquid chromatography coupled with radioimmunoassays for ET related peptides. We isolated and sequenced a C-terminal peptide (big ET-1(22-39)) of big ET-1(1-39) and its N-terminal truncated form (big ET-1(23-39)) in addition to ET-1(1-21) and its oxidized form, [Met7(O)]ET-1(1-21). The total contents of the two C-terminal peptides of big ET-1(1-39) are approximately equal to those of ET-1(1-21) and its oxidized form on a molar basis in the culture supernatant. Furthermore, we isolated big ET-1(1-39) although its content is approximately 2% of that of ET-1(1-21). These results strongly suggest that ET-1(1-21) and big ET-1(22-39) are generated from big ET-1(1-39) by specific processing between Trp21-Val22.

Original languageEnglish (US)
Pages (from-to)1287-1294
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume162
Issue number3
DOIs
StatePublished - Aug 15 1989

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Endothelins
Biosynthetic Pathways
Endothelial cells
Endothelin-1
Cell culture
Swine
Endothelial Cells
Peptides
High performance liquid chromatography
Radioimmunoassay
High Pressure Liquid Chromatography
endothelin-1 (1-21)
Processing
big-endothelin (1-22)

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Analysis of endothelin related peptides in culture supernatant of porcine aortic endothelial cells : Evidence for biosynthetic pathway of endothelin-1. / Sawamura, Tatsuya; Kimura, Sadao; Shinmi, Osamu; Sugita, Yoshiki; Yanagisawa, Masashi; Masaki, Tomoh.

In: Biochemical and Biophysical Research Communications, Vol. 162, No. 3, 15.08.1989, p. 1287-1294.

Research output: Contribution to journalArticle

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abstract = "We investigated the molecular forms of endothelin (ET) related peptides in culture supernatant of porcine aortic endothelial cells by high performance liquid chromatography coupled with radioimmunoassays for ET related peptides. We isolated and sequenced a C-terminal peptide (big ET-1(22-39)) of big ET-1(1-39) and its N-terminal truncated form (big ET-1(23-39)) in addition to ET-1(1-21) and its oxidized form, [Met7(O)]ET-1(1-21). The total contents of the two C-terminal peptides of big ET-1(1-39) are approximately equal to those of ET-1(1-21) and its oxidized form on a molar basis in the culture supernatant. Furthermore, we isolated big ET-1(1-39) although its content is approximately 2{\%} of that of ET-1(1-21). These results strongly suggest that ET-1(1-21) and big ET-1(22-39) are generated from big ET-1(1-39) by specific processing between Trp21-Val22.",
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