ISOLATION OF 2 NOVEL NEUROPEPTIDES FROM SEA-ANEMONES - THE UNUSUAL, BIOLOGICALLY-ACTIVE L-3-PHENYLLACTYL-TYR-ARG-ILE-NH2 AND ITS DES-PHENYLLACTYL FRAGMENT TYR-ARG-ILE-NH2

被引:8
作者
NOTHACKER, HP
RINEHART, KL
MCFARLANE, ID
GRIMMELIKHUIJZEN, CJP
机构
[1] UNIV HAMBURG,CTR MOLEC NEUROBIOL,MARTINISTR 52,W-2000 HAMBURG 20,GERMANY
[2] UNIV ILLINOIS,SCH CHEM SCI,URBANA,IL 61801
[3] UNIV HULL,DEPT APPL BIOL,HULL HU6 7RX,N HUMBERSIDE,ENGLAND
关键词
NEUROTRANSMITTER; NEUROHORMONE; NEUROPEPTIDE BLOCKING GROUP; PEPTIDE STRUCTURE; POSTTRANSLATIONAL MODIFICATION; MASS SPECTROMETRY; COELENTERATE;
D O I
10.1016/0196-9781(91)90190-Z
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Using a radioimmunoassay for the carboxyl-terminal sequence Arg-Val-NH2, two novel peptides were purified from extracts of the sea anemone Anthopleura elegantissima. These peptides were L-3-phenyllactyl-Tyr-Arg-Ile-NH2 (name: Antho-RIamide I) and its des-phenyllactyl fragment Tyr-Arg-Ile-NH2 (Antho-RIamide II). Immunocytochemical staining showed that these peptides were localized in neurons of sea anemones. Application of low concentrations (10(-8) M) of Antho-RIamide I inhibited spontaneous contractions in several muscle groups of sea anemones, whereas Antho-RIamide II was inactive. Antho-RIamide I is the second neuropeptide from sea anemones that bears the unusual, amino-terminal L-3-phenyllactyl blocking group. We suggest that this group renders the peptide resistant against degradation by nonspecific aminopeptidases. In addition, the L-3-phenyllactyl residue might also play a role in receptor binding.
引用
收藏
页码:1165 / 1173
页数:9
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