Characterization of putative tachykinin peptides in Caenorhabditis elegans Journal Article


Authors: Sakai, N.; Ohno, H.; Yoshida, M.; Iwamoto, E.; Kurogi, A.; Jiang, D.; Sato, T.; Miyazato, M.; Kojima, M.; Kato, J.; Ida, T.
Article Title: Characterization of putative tachykinin peptides in Caenorhabditis elegans
Abstract: Tachykinin-like peptides, such as substance P, neurokinin A, and neurokinin B, are among the earliest discovered and best-studied neuropeptide families, and research on them has contributed greatly to our understanding of the endocrine control of many physiological processes. However, there are still many orphan tachykinin receptor homologs for which cognate ligands have not yet been identified, especially in small invertebrates, such as the nematode Caenorhabditis elegans (C. elegans). We here show that the C. elegans nlp-58 gene encodes putative ligands for the orphan G protein-coupled receptor (GPCR) TKR-1, which is a worm ortholog of tachykinin receptors. We first determine, through an unbiased biochemical screen, that a peptide derived from the NLP-58 preprotein stimulates TKR-1. Three mature peptides that are predicted to be generated from NLP-58 show potent agonist activity against TKR-1. We designate these peptides as C. elegans tachykinin (CeTK)-1, −2, and −3. The CeTK peptides contain the C-terminal sequence GLR-amide, which is shared by tachykinin-like peptides in other invertebrate species. nlp-58 exhibits a strongly restricted expression pattern in several neurons, implying that CeTKs behave as neuropeptides. The discovery of CeTKs provides important information to aid our understanding of tachykinin-like peptides and their functional interaction with GPCRs. © 2021 Elsevier Inc.
Keywords: c. elegans; gpcr; tachykinin; novel bioactive peptide
Journal Title: Biochemical and Biophysical Research Communications
Volume: 559
ISSN: 0006-291X
Publisher: Elsevier Science, Inc.  
Date Published: 2021-06-25
Start Page: 197
End Page: 202
Language: English
DOI: 10.1016/j.bbrc.2021.04.063
PROVIDER: scopus
PUBMED: 33945998
DOI/URL:
Notes: Article -- Export Date: 1 June 2021 -- Source: Scopus
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  1. Hayao Ohno
    2 Ohno