Identification of proctolin in the central nervous system of the horseshoe crab, Limulus polyphemus

Abstract

A proctolin-like peptide was isolated from the prosomal CNS of the chelicerate arthropod, Limulus, and purified using size exclusion, ion exchange and high performance liquid chromatography. Coincident bioassay (cockroach hindgut) and radioimmunoassay were employed to identify fractions which contained proctolin-like material. Proctolin-like activity coeluted with synthetic proctolin with all three chromatographic techniques employed. When applied to either the Limulus heart or hindgut preparations, purified Limulusproctolin produced excitatory responses which were indistinguishable from those produced by the synthetic peptide. Purified samples of the Limulus proctolin-like peptide were subjected to Edman degradation and tandem mass spectrometry and the amino acid sequence of the Limulus peptide was determined to be identical to that of cockroach proctolin (H-Arg-Tyr-Leu-Pro-Thr-OH). The presence of proctolin in the LimulusCNS and its biological action on the isolated heart and hindgut suggest a physiological role for this peptide in the regulation of cardiac output and hindgut motility.

Department

Molecular, Cellular and Biomedical Sciences

Publication Date

3-1-1990

Journal Title

Peptides

Publisher

Elsevier

Digital Object Identifier (DOI)

10.1016/0196-9781(90)90072-D

Document Type

Article

Rights

Copyright © 1990, Elsevier

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