Open AccessIdentification of novel periviscerokinins from single neurohaemal release sites in insects
Author(s) -
Predel Reinhard,
Kellner Roland,
Baggerman Geert,
Steinmetzer Torsten,
Schoofs Liliane
Publication year - 2000
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1327.2000.01425.x
Subject(s) - cockroach , edman degradation , peptide , biology , neuropeptide , electrospray ionization , amino acid , peptide sequence , zoology , anatomy , stereochemistry , biochemistry , chemistry , mass spectrometry , ecology , chromatography , gene , receptor
Three novel members of the periviscerokinin family could be identified directly from extracts of single abdominal perisympathetic organs of blaberoid cockroaches by means of electrospray ionization‐quadrupole time of flight (ESI‐QTOF) MS. Sequences of these periviscerokinins were confirmed by Edman degradation. Their primary structures are GSSGLIPFGRT‐NH 2 (Lem‐PVK‐1), GSSGLISMPRV‐NH 2 (Lem‐PVK‐2), and GSSGMIPFPRV‐NH 2 (Lem‐PVK‐3). Hitherto only known from the American cockroach, this neuropeptide family contains a highly conserved N‐terminus whereas, at the C‐terminus, only the penultimate amino‐acid residue (Arg) has been found in all members of this peptide family. The identified periviscerokinins are the only abundant myoactive peptides in abdominal perisympathetic organs of blaberoid cockroches and they appear to be absent in the retrocerebral complex. Screening of extracts of single abdominal perisympathetic organs (70–90 µm in diameter), from five different species of the suborder Blaberoidea, revealed that they all contain the three neuropeptides which are described here for the first time.