Purification and Characterization of Urotensin II and Parvalbumin from an Elasmobranch Fish, Scyliorhinus canicula (Common Dogfish)

Abstract

The caudal portion of the spinal cord of elasmobranch fish incorporates a diffuse neuroendocrine system. Using an antiserum raised against urotensin II from a teleost fish (goby) to facilitate purification, a peptide structurally related to urotensin II was isolated in pure form from an extract of neuroendocrine tissue from the spinal cord of the European common dogfish, Scyliorhinus canicula. The primary structure of the peptide was established as: Asn-Asn-Phe-Ser-Asp-Cys-Phe-Trp-Lys-Tyr-Cys-Val. The amino acid sequence was confirmed by chemical synthesis. A comparison of this sequence with those of the known teleost urotensin II peptides shows that the cyclic region of the molecule has been fully conserved between species and suggests that the presence of an acidic residue at position 5 and a hydrophobic residue at position 12 are important features for the biological activity of the peptide. The dogfish spinal cord extract also contained a high concentration of the calcium-binding protein, parvalbumin and the amino acid sequence at its NH2 terminus [residues (1–50)] was determined.

Urotensin II in Invertebrates: From Structure to Function in Aplysia californica

“…Among lower vertebrates, UII has been reported in jawless fish such as lamprey [80], which lack a caudal neurosecretory system. Isolation of UII peptides from whole brain extracts of the sea lamprey, Petromyzon marinus , and the river lamprey, Lampetra fluviatilis , which are structurally identical to UII from the dogfish [81] and skate [82], suggests that the primary structure of UII was well-conserved phylogenetically among the ancient vertebrates where it may have functioned as a neurotransmitter/neuromodulator in the CNS, rather than as a neurohormone of the caudal neurosecretory system [80]. Here, we present evidence that the UII prohormone is expressed and can fulfill a signaling function in the protostomian mollusk A. californica.…”

International Union of Basic and Clinical Pharmacology. XCII. Urotensin II, Urotensin II–Related Peptide, and Their Receptor: From Structure to Function

“…The amino acid sequence of UII has been determined in dogfish (Conlon et al, 1992a), flounder (Conlon et al, 1990), frog (Conlon et al, 1992b), and pig (Mori et al, 1999) confirming that the peptide is generated through cleavage at the Arg…”

Biochemical and functional characterization of high‐affinity urotensin II receptors in rat cortical astrocytes

“…1980). UII has been subsequently characterized from the brain and spinal cord of various vertebrate species including dogfish (Conlon et al . 1992a), trout (Waugh and Conlon 1993), frog (Conlon et al .…”

“…Urotensin II (UII) is a cyclic neuropeptide originally isolated from the caudal neurosecretory organ (urophysis) of teleost fish on the basis of its spasmogenic activity (Pearson et al 1980). UII has been subsequently characterized from the brain and spinal cord of various vertebrate species including dogfish (Conlon et al 1992a), trout (Waugh and Conlon 1993), frog (Conlon et al 1992b), mouse (Coulouarn et al 1999), rat (Coulouarn et al 1999), pig (Mori et al 1999) and human (Coulouarn et al 1998;Ames et al 1999). The human UII sequence encompasses 11 residues (Coulouarn et al 1998;Chartrel et al 2004), while the rat and mouse sequences consist of 14 and 17 amino acids, respectively (Coulouarn et al 1999;Elshourbagy et al 2002).…”