Identification of one tachykinin- and two kinin-related peptides in the brain of the white shrimp, Penaeus vannamei

Biochem Biophys Res Commun. 1998 Jul 20;248(2):406-11. doi: 10.1006/bbrc.1998.8964.


This paper reports the purification of three myotropic neuropeptides from the white shrimp Penaeus vannamei. The central nervous systems of 3500 shrimps were extracted in an acidified solvent, after which four to five HPLC column systems were used to obtain pure peptides. A cockroach hindgut muscle contraction bioassay was used to monitor all collected fractions. The pure peptides were submitted to Edman degradation based automated microsequencing. Mass spectrometry and chemical synthesis confirmed the sequences. Ala-Pro-Ser-Gly-Phe-Leu-Gly-Met-Arg-NH2 (Pev-tachykinin, 934.1 Da) belongs to the tachykinin family with identified members in all vertebrate classes and some invertebrate classes: arthropods, annelids and molluscs. A very specific Pev-tachykinin antiserum was developed, which labels 4 neurosecretory cells in the brain. Ala-Ser-Phe-Ser-Pro-Trp-Gly-NH2 (Pev-kinin 1, 749.8 Da) and Asp-Phe-Ser-Ala-Trp-Ala-NH2 (Pev-kinin 2, 694.7 Da) are the first crustacean kinins. Pev-kinin 2 is the first kinin with a Trp-Ala-NH2 instead of a kinin-typical Trp-Gly-NH2 carboxyterminus.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Autacoids
  • Brain / cytology
  • Brain Chemistry / physiology
  • Cockroaches
  • Diuretics / chemistry
  • Kinins / chemistry
  • Muscle Contraction / drug effects
  • Neuropeptides / chemistry*
  • Penaeidae
  • Sequence Analysis
  • Sequence Homology, Amino Acid
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Tachykinins / chemistry*


  • Autacoids
  • Diuretics
  • Kinins
  • Neuropeptides
  • Tachykinins