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Isolation, identification, and synthesis of a disulfated sulfakinin from the central nervous system of an arthropod, the white shrimp Litopenaeus vannamei
Torfs, P.; Baggerman, G.; Meeusen, T.; Nieto, J.; Nachman, R.J.; Calderon, J.; De Loof, A.; Schoofs, L. (2002). Isolation, identification, and synthesis of a disulfated sulfakinin from the central nervous system of an arthropod, the white shrimp Litopenaeus vannamei. Biochem. Biophys. Res. Commun. 299(2): 312-320. dx.doi.org/10.1016/S0006-291X(02)02624-4
In: Biochemical and Biophysical Research Communications. ACADEMIC PRESS INC ELSEVIER SCIENCE: San Diego etc.. ISSN 0006-291X, more
Peer reviewed article  

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Keywords
    Crustacea [WoRMS]; Litopenaeus vannamei (Boone, 1931) [WoRMS]; Marine
Author keywords
    mass spectrometry; cholecystokinin; gastrin/CCK; FaRP; crustacea;Litopenaeus rannamei; neuropeptide

Authors  Top 
  • Torfs, P.
  • Baggerman, G.
  • Meeusen, T.
  • Nieto, J.
  • Nachman, R.J.
  • Calderon, J.
  • De Loof, A.
  • Schoofs, L.

Abstract
    Two myotropic peptides displaying tyrosyl sulfation have been isolated from an extract of central nervous systems (brain, suboesophageal ganglion, thoracic ganglia, and ventral nerve cord) of the white shrimp Litopenaeus vannamei. Both peptides were identified by mass spectrometry and belong to the sulfakinin family of neuropeptides, which are characterized by the C-terminal hexapeptide Y(SO3H)GHMRF-NH2 preceded by two acidic amino acid residues. Pev-SK 1 (AGGSGGVGGEY(SO3H)DDY(SO3H)GH(L/I) RF-NH2) has two sulfated tyrosyl residues and a unique (L/I) for M substitution in the C-terminal sequence. Pev-SK 2 (pQFDEY(SO3H)GHMRF-NH2) fully complies with the typical sulfakinin core sequence and is blocked by a pyroglutamyl residue. Synthetic analogs (sulfated and unsulfated) were synthesized and the tyrosyl sulfations were confirmed by myotropic activity studies and co-elution with the native fractions. Pev-SK 1 is the first disulfated neuropeptide elucidated in the phylum of the arthropoda, with the only other reported disulfated neuropeptide, called cionin, found in a protochordate. The similarities in amino acid sequence and posttranslational modifications of the crustacean sulfakinins and protochordate cionin provide further evidence for the hypothesis stating that gastrin/CCK, cionin, and sulfakinins originate from a common ancestral gastrin/CCK-like peptide.

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