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. 1987 Jan;84(2):575–579. doi: 10.1073/pnas.84.2.575

Unusual cardioactive peptide (CCAP) from pericardial organs of the shore crab Carcinus maenas

J Stangier *, C Hilbich †, K Beyreuther †, R Keller *
PMCID: PMC304253  PMID: 16593803

Abstract

An unusual crustacean cardioactive peptide (CCAP) from the pericardial organs of the shore crab Carcinus maenas has been purified to homogeneity by a two-step reversed-phase HPLC procedure. Manual microsequencing using the 4-(N,N-dimethylamino)azobenzene 4′-isothiocyanate/phenylisothiocyanate double-coupling technique and automated gas-phase sequencing of the oxidized peptide revealed that CCAP is a nonapeptide (Mr 957) of the sequence Pro-Phe-[unk]Cys-Asn-Ala-Phe-Thr-Gly-Cys-NH2. We have confirmed the sequence by chemical synthesis of the C-terminally amidated and nonamidated forms of the peptide. The presence of the amide group was indicated by lack of susceptibility to carboxypeptidase A and Y treatment and was confirmed by the observation that the native CCAP comigrated with the amidated synthetic peptide on HPLC. Native and synthetic CCAP displayed high accelerating activity on a semi-isolated crab heart preparation, whereas the nonamidated synthetic peptide was of much lower potency. The effect of CCAP was both inoand chronotropic. The two pericardial organs of one animal yielded 30-40 pmol of extractable CCAP. Its sequence does not resemble that of any known neuropeptide. However, a “mirror-image” similarity to vasopressin is conspicuous.

Keywords: crustacean neuropeptide, amino acid sequence, cardioactive neurohormone, neurosecretion

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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