Sulphated CCK-8-like peptides in the neural ganglion of the protochordate Ciona intestinalis

J. M. Conlon, T. W. Schwartz, J. F. Rehfeld

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Immunochemical studies were carried out on extracts of the neural ganglion from the ascidian Ciona intestinalis in order to the characterize the peptide(s), which react with antibodies against the C-terminal sequence common for the mammalian hormones, cholecystokinin (CCK) and gastrin. Radioimmunoassays specific for the sulphotyrosyl-containing N-terminus of CCK-8, for the common α-carboxyamidated C-terminus and for gastrin were used to monitor gel chromatography and reverse-phase HPLC of the extracts. Only neutral extracts contained immunoreactive material (634 (524-785) pmol eqv.CCK-8/g) (mean and range, n = 4)). HPLC revealed a small peak eluting almost like CCK-8 and a larger peak eluting earlier. By subsequent gel chromatography the larger peak eluted in the same position as sulphated CCK-8. The material was recognized almost equally by the N- and C-terminal CCK radioimmunoassays, whereas the specific C-terminal gastrin radioimmunoassay did not measure the peptides. Treatment with arylsulphatase removed the binding to the antiserum specific for the sulphotyrosyl-containing sequence of CCK. The results indicate that the ganglion of Ciona intestinalis contains a tyrosyl-sulphated peptide resembling mammalian CCK-8.

Original languageEnglish
Pages (from-to)241-250
Number of pages10
JournalRegulatory Peptides
Issue number3
Publication statusPublished (in print/issue) - Mar 1988


  • Cholecystokinin (CCK)
  • Gastrin
  • Neural ganglion
  • Protochordate
  • Sequence-specific radioimmunoassay


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