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<p>Humoral factors regulating cardiac myocytes have not yet been fully elucidated. Using mass spectrometry, we analyzed peptides released from primary neonatal rat cardiac fibroblasts to identify a 24-amino-acid peptide with an intramolecular disulfide bond. It is derived from the C-terminal end of integral membrane protein 2A (ITM2A), a single-pass type II membrane protein; the peptide sequence is identical between humans and rodents and N-terminally flanked by conserved dibasic residues KR. The ITM2A peptide stimulated secretion of atrial natriuretic peptide (ANP), the predominant hormone produced by cardiac myocytes, in a Langendorff rat heart perfusion system as well as a primary culture of neonatal rat ventricular myocytes. These ANP secretion changes were not accompanied by an alteration in the beating rate, a key determinant of ANP secretion. In a mouse cardiac infarction model, both plasma ANP concentration and ITM2A gene expression in heart tissue reached a peak level on day 7 after operation. Our findings provide new insight into cardiac cell-to-cell communication that regulates ANP secretion.</p>

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Carboxy-terminal 24-amino-acid peptide of integral membrane protein 2A is produced in the heart and stimulates atrial natriuretic peptide release

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年3月16日

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  • Tsukasa Osaki,
  • Akikazu Mochiduki,
  • Mitsuhiro Nishigori,
  • Ken Shinmura,
  • Takahiro Miyazaki,
  • Emi Mishiro-Sato,
  • Tetsuya Kadonosono,
  • Kayoko Tamaki,
  • Nobuaki Okumura,
  • Toshifumi Takao,
  • Kazuki Sasaki,
  • Naoto Minamino

摘要

Humoral factors regulating cardiac myocytes have not yet been fully elucidated. Using mass spectrometry, we analyzed peptides released from primary neonatal rat cardiac fibroblasts to identify a 24-amino-acid peptide with an intramolecular disulfide bond. It is derived from the C-terminal end of integral membrane protein 2A (ITM2A), a single-pass type II membrane protein; the peptide sequence is identical between humans and rodents and N-terminally flanked by conserved dibasic residues KR. The ITM2A peptide stimulated secretion of atrial natriuretic peptide (ANP), the predominant hormone produced by cardiac myocytes, in a Langendorff rat heart perfusion system as well as a primary culture of neonatal rat ventricular myocytes. These ANP secretion changes were not accompanied by an alteration in the beating rate, a key determinant of ANP secretion. In a mouse cardiac infarction model, both plasma ANP concentration and ITM2A gene expression in heart tissue reached a peak level on day 7 after operation. Our findings provide new insight into cardiac cell-to-cell communication that regulates ANP secretion.