ISOLATION AND AMINO-ACID-SEQUENCE OF CRUSTACEAN HYPERGLYCEMIC HORMONE PRECURSOR-RELATED PEPTIDES

被引:21
|
作者
TENSEN, CP
VERHOEVEN, AHM
GAUS, G
JANSSEN, KPC
KELLER, R
VANHERP, F
机构
[1] CATHOLIC UNIV NIJMEGEN,FAC SCI,DEPT EXPTL ZOOL,6525 ED NIJMEGEN,NETHERLANDS
[2] UNIV BONN,INST ZOOPHYSIOL,W-5300 BONN 1,GERMANY
关键词
CRUSTACEAN HYPERGLYCEMIC HORMONE PRECURSOR-RELATED PEPTIDES; AMINO ACID SEQUENCES; MONOBASIC PROCESSING SITES; HOMARUS-AMERICANUS; ORCONECTES-LIMOSUS; CARCINUS-MAENAS; CARDISOMA-CARNIFEX;
D O I
10.1016/0196-9781(91)90119-A
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
The crustacean hyperglycemic hormone (CHH) is synthesized as part of a larger preprohormone in which the sequence of CHH is N-terminally flanked by a peptide for which the name CPRP (CHH precursor-related peptide) is proposed. Both CHH and CPRP are present in the sinus gland, the neurohemal organ of neurosecretory cells located in the eyestalk of decapod crustaceans. This paper describes the isolation and sequence analysis of CPRPs isolated from sinus glands of the crab Carcinus maenas, the crayfish Orconectes limosus and the lobster Homarus americanus. The published sequence of "peptide H" isolated from the land crab, Cardisoma carnifex, has now been recognized as a CPRP in this species. Sequence comparison reveals a high level of identity for the N-terminal region (residues 1-13) between all four peptides, while identity in the C-terminal domain is high between lobster and crayfish CPRP on the one hand, and between both crab species on the other. Conserved N-terminal residues include a putative monobasic processing site at position 11, which suggests that CPRP may be a biosynthetic intermediate from which a potentially bioactive decapeptide can be derived.
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页码:673 / 681
页数:9
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