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Recently identified a novel neuropeptide manserin colocalize with the TUNEL‐positive cells in the top villi of the rat duodenum
Author(s) -
Yajima Aika,
Narita Naoko,
Narita Masaaki
Publication year - 2008
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.991
Subject(s) - colocalization , tunel assay , biology , duodenum , apoptosis , immunostaining , enteroendocrine cell , microbiology and biotechnology , terminal deoxynucleotidyl transferase , neuropeptide , immunohistochemistry , endocrinology , medicine , biochemistry , immunology , endocrine system , receptor , hormone
We recently isolated a novel 40 amino acid neuropeptide designated manserin from the rat brain. Manserin is derived from secretogranin II, a member of granin acidic secretory protein family by proteolytic processing, as previously reported secretoneurin and EM66. Manserin peptide are localized in the endocrine cells of the pituitary. In this study, we further investigated the manserin localization in the digestive system by immunohistochemical analysis using antimanserin antibody. In the duodenum, manserin immunostaining was exclusively observed in the nuclei of top villi instead of cytosol as observed in neurons in our previous study. Interestingly, manserin‐positive cells in the duodenum are colocalized with terminal deoxynucleotidyl transferase‐mediated dUTP nick‐end labeling (TUNEL) positive cells, the cells whose DNA was damaged. Since the top villi of duodenum epithelial cells are known to undergo spontaneous apoptosis during epithelial cell turn over, and since other peptides such as secretoneurin and EM66 derived from SgII have been reported to be cancer‐related, these results indicated that manserin peptide may have a role in apoptosis and/or cancer pathogenesis in the digestive organ. Copyright © 2008 European Peptide Society and John Wiley & Sons, Ltd.