Salusins: newly identified bioactive peptides with hemodynamic and mitogenic activities

Author:  ["Masayoshi Shichiri","Shinya Ishimaru","Toshio Ota","Tetsuo Nishikawa","Takao Isogai","Yukio Hirata"]

Publication:  Nature Medicine

CITE.CC academic search helps you expand the influence of your papers.

Tags:     Medicine

Abstract

The discovery of endogenous bioactive peptides has typically required a lengthy identification process. Computer-assisted analysis of cDNA and genomic DNA sequence information can markedly shorten the process. A bioinformatic analysis of full-length, enriched human cDNA libraries searching for previously unidentified bioactive peptides resulted in the identification and characterization of two related peptides of 28 and 20 amino acids, which we designated salusin-α and salusin-β. Salusins are translated from an alternatively spliced mRNA of TOR2A, a gene encoding a protein of the torsion dystonia family. Intravenous administration of salusin-α or salusin-β to rats causes rapid, profound hypotension and bradycardia. Salusins increase intracellular Ca2+, upregulate a variety of genes and induce cell mitogenesis. Salusin-β stimulates the release of arginine-vasopressin from rat pituitary. Expression of TOR2A mRNA and its splicing into preprosalusin are ubiquitous, and immunoreactive salusin-α and salusin-β are detected in many human tissues, plasma and urine, suggesting that salusins are endocrine and/or paracrine factors.

Cite this article

Shichiri, M., Ishimaru, S., Ota, T. et al. Salusins: newly identified bioactive peptides with hemodynamic and mitogenic activities. Nat Med 9, 1166–1172 (2003). https://doi.org/10.1038/nm913

View full text

>> Full Text:   Salusins: newly identified bioactive peptides with hemodynamic and mitogenic activities

Bone marrow as a priming site for T-cell responses to blood-borne antigen

Cyclophilin A modulates the sensitivity of HIV-1 to host restriction factors