Related Experiment Video
Updated: Apr 21, 2026
Multi-Faceted Mass Spectrometric Investigation of Neuropeptides in Callinectes sapidus
Published on: May 31, 2022
Purification and charcterization of a neuropeptide (AN peptide) from starfish, Asterias amurensis
Mi Jeong Jo1, Hye-Jin Go2, Nam Gyu Park3
1Department of Microbiology, Pukyong National University, Busan 48513, South Korea; Research Center for Marine-Integrated Bionics Technology, Pukyong National University, Busan 48513, South Korea; Marine integrated Biomedical Technology center, The National Key Research Institutes in Universities, Pukyong National University, Busan 48513, South Korea.
Abstract:
Although neuropeptides have been extensively studied in marine invertebrates, their diversity and physiological roles remain incompletely understood. Starfish is marine echinoderm with a unique water structure, and lives in seas around the world. In this study, neuropeptide was purified from starfish Asterias amurensis and their properties were analyzed. ANP is a muscle-contracting peptide composed of 18 amino acids purified from starfish tube feet. As a result of full-length cDNA analysis, a total of 5 isotypes were identified through post-translational conversion by dibasic cleavage site (KR) and monobasic cleavage site (K). To investigate the potential physiological role of ANP, tissue-specific expression profiles of ANP transcript were checked and it was found to be highly expressed in the nerve cord. In vitro pharmacological assay confirmed that ANP caused contraction in the apical muscle of A. amurensis. Additionally, the effect of in vivo injection on starfish motility revealed that starfish motility was significantly reduced by ANP. These findings suggest that ANP is a neuropeptide involved in the regulation of muscle contraction and locomotor behavior in starfish, providing new insights into the physiological roles of neuropeptides in echinoderms.
