Isolation of L-3-phenyllactyl-Phe-Lys-Ala-NH2 (Antho-KAamide), a novel neuropeptide from sea anemones.
We have isolated and sequenced the neuropeptide L-3-phenyllactyl-Phe-Lys-Ala-NH2 from the sea anemone Anthopleura elegantissima. This neuropeptide (named Antho-KAamide) has the unusual N-terminal L-3-phenyllactyl blocking group which has recently also been discovered in 2 other neuropeptides from sea anemones. We propose that the L-3-phenyllactyl residue renders Antho-KAamide resistant to nonspecific aminopeptidases, thereby increasing the stability of the neuropeptide after neuronal release. The existence of the L-3-phenyllactyl residue in 3 neuropeptides isolated so far suggests that this blocking group is more generally occurring.
Nothacker
H P
HP
Centre for Molecular Neurobiology (ZMNH), University of Hamburg, FRG.
Rinehart
K L
KL
Grimmelikhuijzen
C J
CJ
D000595:Amino Acid Sequence; D000818:Animals; D003063:Cnidaria; D007150:Immunohistochemistry; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000737:chemistry / Q000302:isolation & purification*; D011863:Radioimmunoassay; D012615:Sea Anemones; D012689:Sequence Homology, Nucleic Acid; D016339:Spectrometry, Mass, Fast Atom Bombardment
D009479:Neuropeptides; C071055:3-phenyllactyl-phenylalanyl-lysyl-alaninamide