Isolation of L-3-phenyllactyl-Phe-Lys-Ala-NH2 (Antho-KAamide), a novel neuropeptide from sea anemones

H P Nothacker; K L Rinehart; C J Grimmelikhuijzen

Isolation of L-3-phenyllactyl-Phe-Lys-Ala-NH2 (Antho-KAamide), a novel neuropeptide from sea anemones

H P Nothacker, K L Rinehart, C J Grimmelikhuijzen

Cell and Neurobiology

10 Citations (Scopus)

Abstract

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.

Original language	English
Journal	Biochemical and Biophysical Research Communications
Volume	179
Issue number	3
Pages (from-to)	1205-11
Number of pages	7
ISSN	0006-291X
Publication status	Published - 30 Sept 1991

Keywords

Amino Acid Sequence
Animals
Cnidaria
Immunohistochemistry
Molecular Sequence Data
Neuropeptides
Radioimmunoassay
Sea Anemones
Sequence Homology, Nucleic Acid
Spectrometry, Mass, Fast Atom Bombardment

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title = "Isolation of L-3-phenyllactyl-Phe-Lys-Ala-NH2 (Antho-KAamide), a novel neuropeptide from sea anemones",

abstract = "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.",

keywords = "Amino Acid Sequence, Animals, Cnidaria, Immunohistochemistry, Molecular Sequence Data, Neuropeptides, Radioimmunoassay, Sea Anemones, Sequence Homology, Nucleic Acid, Spectrometry, Mass, Fast Atom Bombardment",

author = "Nothacker, {H P} and Rinehart, {K L} and Grimmelikhuijzen, {C J}",

year = "1991",

month = sep,

day = "30",

language = "English",

volume = "179",

pages = "1205--11",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Elsevier",

number = "3",

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TY - JOUR

T1 - Isolation of L-3-phenyllactyl-Phe-Lys-Ala-NH2 (Antho-KAamide), a novel neuropeptide from sea anemones

AU - Nothacker, H P

AU - Rinehart, K L

AU - Grimmelikhuijzen, C J

PY - 1991/9/30

Y1 - 1991/9/30

N2 - 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.

AB - 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.

KW - Amino Acid Sequence

KW - Animals

KW - Cnidaria

KW - Immunohistochemistry

KW - Molecular Sequence Data

KW - Neuropeptides

KW - Radioimmunoassay

KW - Sea Anemones

KW - Sequence Homology, Nucleic Acid

KW - Spectrometry, Mass, Fast Atom Bombardment

M3 - Journal article

C2 - 1681803

SN - 0006-291X

VL - 179

SP - 1205

EP - 1211

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 3

ER -

Isolation of L-3-phenyllactyl-Phe-Lys-Ala-NH2 (Antho-KAamide), a novel neuropeptide from sea anemones

Abstract

Keywords

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