Isolation of Leu-Pro-Pro-Gly-Pro-Leu-Pro-Arg-Pro-NH2 (Antho-RPamide), an N-terminally protected, biologically active neuropeptide from sea anemones.
Using a radioimmunoassay against the C-terminal sequence Arg-Pro-NH2 (RPamide), we have isolated the peptide Leu-Pro-Pro-Gly-Pro-Leu-Pro-Arg-Pro-NH2 (Antho-RPamide) from an extract of the sea anemone Anthopleura elegantissima. Antho-RPamide is located in neurons of sea anemones. Application of low concentrations of Antho-RPamide to tentacle preparations of sea anemones strongly increased the frequency and duration of spontaneous contractions, suggesting that this peptide is involved in neurotransmission. Antho-RPamide has a free N-terminus, yet its X-Pro-Pro sequence makes it relatively resistant to degradation by nonspecific aminopeptidases. Thus, we have discovered another strategy by which sea anemones protect the N-termini of their bioactive neuropeptides.
Carstensen
K
K
Center for Molecular Neurobiology (ZMNH), University of Hamburg, Germany.
Rinehart
K L
KL
McFarlane
I D
ID
Grimmelikhuijzen
C J
CJ
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004355:Drug Stability; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000737:chemistry / Q000302:isolation & purification* / Q000502:physiology; D012615:Sea Anemones / Q000737:chemistry* / Q000502:physiology; D017386:Sequence Homology, Amino Acid
D009479:Neuropeptides; C079066:leucyl-prolyl-prolyl-glycyl-prolyl-leucyl-prolyl-arginyl-prolinamide