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Front Endocrinol (Lausanne)

Title:		The Arginine Residue within the C-Terminal Active Core of Bombyx mori Pheromone Biosynthesis-Activating Neuropeptide is Essential for Receptor Binding and Activation
Author(s):		Kawai T; Lee JM; Nagata K; Matsumoto S; Tanokura M; Nagasawa H;
Address:		"Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo Tokyo, Japan"
Journal Title:		Front Endocrinol (Lausanne)
Year:		2012
Volume:		20120320
Issue:
Page Number:		42 -
DOI:		10.3389/fendo.2012.00042
ISSN/ISBN:		1664-2392 (Electronic) 1664-2392 (Linking)
Abstract:		"In most lepidopteran insects, the biosynthesis of sex pheromones is regulated by pheromone biosynthesis-activating neuropeptide (PBAN). Bombyx mori PBAN (BomPBAN) consists of 33 amino acid residues and contains a C-terminus FSPRLamide motif as the active core. Among neuropeptides containing the FXPRLamide motif, the arginine (Arg, R) residue at the second position from the C-terminus is highly conserved across several neuropeptides, which can be designated as RXamide peptides. The purpose of this study was to clarify the role of the Arg residue in the BomPBAN active core. We synthesized 10-residue peptides corresponding to the C-terminal part of BomPBAN with a series of replacements at the second position from the C-terminus, termed the C2 position, and measured their efficacy in stimulating Ca(2+) influx in insect cells expressing a fluorescent PBAN receptor chimera (PBANR-EGFP) using the fluorescent Ca(2+) indicator, Fura Red-AM. The PBAN analogs with the C2 position replaced with alanine (Ala, A), aspartic acid (Asp, D), serine (Ser, S), or l-2-aminooctanoic acid (Aoc) decreased PBAN-like activity. R(C2)A (SKTRYFSPALamide) and R(C2)D (SKTRYFSPDLamide) had the lowest activity and could not inhibit the activity of PBAN C10 (SKTRYFSPRLamide). We also prepared Rhodamine Red-labeled peptides of the PBAN analogs and examined their ability to bind PBANR. In contrast to Rhodamine Red-PBAN C10 at 100 nM, none of the synthetic analogs exhibited PBANR binding at the same concentration. Taken together, our results demonstrate that the C2 Arg residue in BomPBAN is essential for PBANR binding and activation"
Keywords:		FXPRLamide peptides Gpcr Lepidoptera Pban Pbanr neuropeptide sex pheromone silkmoth;
Notes:		"PubMed-not-MEDLINEKawai, Takeshi Lee, Jae Min Nagata, Koji Matsumoto, Shogo Tanokura, Masaru Nagasawa, Hiromichi eng Switzerland 2012/06/02 Front Endocrinol (Lausanne). 2012 Mar 20; 3:42. doi: 10.3389/fendo.2012.00042. eCollection 2012"