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ANGT_HUMAN[448-462], an Anorexigenic Peptide Identified Using Plasma Peptidomics.

ABSTRACT: The discovery of bioactive peptides is an important research target that enables the elucidation of the pathophysiology of human diseases and provides seeds for drug discovery. Using a large number of native peptides previously identified using plasma peptidomics technology, we sequentially synthesized selected sequences and subjected them to functional screening using human cultured cells. A 15-amino-acid residue proangiotensinogen-derived peptide, designated ANGT_HUMAN[448-462], elicited cellular responses and bound to cultured human cells. Synthetic fluorescent-labeled and biotinylated ANGT_HUMAN[448-462] peptides were rendered to bind to cell- and tissue-derived proteins and peptide-cell protein complexes were retrieved and analyzed using liquid chromatography-tandem mass spectrometry, revealing the β-subunit of ATP synthase as its cell-surface binding protein. Because ATP synthase mediates the effects of anorexigenic peptides, the ability of ANGT_HUMAN[448-462] to modulate eating behavior in mice was investigated. Both intraperitoneal and intracerebroventricular injections of low doses of ANGT_HUMAN[448-462] suppressed spontaneous food and water intake throughout the dark phase of the diurnal cycle without affecting locomotor activity. Immunoreactive ANGT_HUMAN[448-462], distributed throughout human tissues and in human-derived cells, is mostly co-localized with angiotensin II and is occasionally present separately from angiotensin II. In this study, an anorexigenic peptide, ANGT_HUMAN[448-462], was identified by exploring cell surface target proteins of the human native peptides identified using plasma peptidomics.

SUBMITTER: Sasaki S

PROVIDER: S-EPMC9184509 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature

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ANGT_HUMAN[448-462], an Anorexigenic Peptide Identified Using Plasma Peptidomics.

Sasaki Sayaka S Oba Kazuhito K Kodera Yoshio Y Itakura Makoto M Shichiri Masayoshi M

Journal of the Endocrine Society 20220519 7

The discovery of bioactive peptides is an important research target that enables the elucidation of the pathophysiology of human diseases and provides seeds for drug discovery. Using a large number of native peptides previously identified using plasma peptidomics technology, we sequentially synthesized selected sequences and subjected them to functional screening using human cultured cells. A 15-amino-acid residue proangiotensinogen-derived peptide, designated ANGT_HUMAN[448-462], elicited cellu ...[more]

PMID: 35702602

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Dataset Information

ANGT_HUMAN[448-462], an Anorexigenic Peptide Identified Using Plasma Peptidomics.

Publications

ANGT_HUMAN[448-462], an Anorexigenic Peptide Identified Using Plasma Peptidomics.

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