{"refrec":{"BRefID":281048,"RR":"<b>Torfs, P.; Baggerman, G.; Meeusen, T.; Nieto, J.; Nachman, R.J.; Calderon, J.; De Loof, A.; Schoofs, L.</b> (2002). Isolation, identification, and synthesis of a disulfated sulfakinin from the central nervous system of an arthropod, the white shrimp <i>Litopenaeus vannamei</i>. <i>Biochem. Biophys. Res. Commun. 299(2)</i>: 312-320. <a href=\"https://dx.doi.org/10.1016/S0006-291X(02)02624-4\" target=\"_blank\">https://dx.doi.org/10.1016/S0006-291X(02)02624-4</a>","BEntID":273067,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>Biochem. Biophys. Res. Commun. 299(2)</i>: 312-320. <a href=\"https://dx.doi.org/10.1016/S0006-291X(02)02624-4\" target=\"_blank\">https://dx.doi.org/10.1016/S0006-291X(02)02624-4</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Torfs, P.; Baggerman, G.; Meeusen, T.; Nieto, J.; Nachman, R.J.; Calderon, J.; De Loof, A.; Schoofs, L.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Torfs, P. <i>et al.</i>","Englishabstract":"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 <i>Litopenaeus vannamei</i>. Both peptides were identified by mass spectrometry and belong to the sulfakinin family of neuropeptides, which are characterized by the C-terminal hexapeptide Y(SO<sub>3</sub>H)GHMRF-NH<sub>2</sub> preceded by two acidic amino acid residues. Pev-SK 1 (AGGSGGVGGEY(SO<sub>3</sub>H)DDY(SO<sub>3</sub>H)GH(L/I) RF-NH<sub>2</sub>) has two sulfated tyrosyl residues and a unique (L/I) for M substitution in the C-terminal sequence. Pev-SK 2 (pQFDEY(SO<sub>3</sub>H)GHMRF-NH<sub>2</sub>) 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.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Isolation, identification, and synthesis of a disulfated sulfakinin from the central nervous system of an arthropod, the white shrimp <i>Litopenaeus vannamei</i>","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2026-06-14 01:31:38.065109","timezone_type":1,"timezone":"+02:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"mass spectrometry; cholecystokinin; gastrin/CCK; FaRP; crustacea;Litopenaeus rannamei; neuropeptide","OtherDescriptors":null,"Notes":null,"AnaPub":2002,"MonPub":null,"DateUpdate":"2022-07-13","DateCreate":"2016-10-09","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000179515900025","VABBcode":null,"OpenAcc":0,"DOI":"10.1016/S0006-291X(02)02624-4"},"refs":null,"anarec":{"AnaID":281048,"PubliDate":2002,"Pagination":"312-320","XtraPublOfAnaID":null,"ISBN":null,"Volume":"299","Issue":"2","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":42249,"SerRR":"Biochemical and Biophysical Research Communications. 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