Purification and characterization of Contractin A from the pedicellarial venom of sea urchin, Toxopneustes pileolus

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Abstract

A component that causes contraction of the isolated guinea pig tracheal smooth muscle was isolated in homogeneous form from the venom of the pedicellaria of the sea urchin, Toxopneustes pileolus. It is named Contractin A. Contractin A has 18,000 Da with a total residue of 138 amino acids. The molecular weight is about 17,700. The N-terminal amino acid is serine. The partial amino acid sequence was determined up to 37 residues. Direct comparison of sea urchin Contractin A does not show any similarity in amino acid sequence to toxins isolated from other marine toxin producers such as sea snakes, sea anemones, or marine worms. Contractin A caused contraction of the tracheal smooth muscle in a dose-dependent manner. Furthermore, Contractin A relaxed the contraction induced by histamine. The contraction and relaxation activity of Contractin A on the tracheal smooth muscle is reduced by a cyclooxygenase inhibitor such as indomethacin. The contraction induced by Contractin A is also inhibited by a phospholipase C inhibitor but not by a phospholipase A2 inhibitor. These results suggest that in the isolated guinea pig tracheal smooth muscle, the response to Contractin A may be effected through activated phospholipase C.

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    For example, several toxins have been isolated from the globiferous pedicellariae of the sea urchins Toxopneustes pileolus and Tripneustes gratilla (Satoh et al., 2002). One of these toxins, Contractin A, was isolated based on its smooth muscle contraction activity and was found to have similarity in the N-terminal amino acid sequence to phospholipase A2 (Nakagawa et al., 1991; Hatakeyama et al., 2015). In contrast, SUL-I isolated from the same organism is a lectin that binds to galactose and galactose-related carbohydrates and is involved with various processes such as chemotactic activity on guinea pig neutrophils and mitogenic activity on murine splenocytes (Nakagawa et al., 1996; Takei and Nakagawa, 2006).

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    Venom from the globiferous pedicellariae of T. pileolus contains several toxins, which have various biological activities (Nakagawa et al., 2003). One of these toxins, Contractin A, was purified using an assay to measure smooth muscle–contraction activity (Nakagawa et al., 1991). This activity was inhibited by a phospholipase C inhibitor, suggesting that Contractin A has phospholipase C-like activity or can activate cellular phospholipase C to induce its biological effects, although the N-terminal amino acid sequence has some similarity with PLA2.

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This work was supported by NIH Merit Award R37 GM15591 (A.T.T.) and a Senior Faculty Fellowship from the Ministry of Education, Japan (H.N.).

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Present address: Department of Health Science, Integrated Arts and Sciences, University of Tokushima, Tokushima 770, Japan.

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