Purification and characterization of Contractin A from the pedicellarial venom of sea urchin, Toxopneustes pileolus☆
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Cited by (19)
Molecular cloning and characterization of the two putative toxins expressed in the venom of the devil stinger Inimicus japonicus
2021, ToxiconCitation Excerpt :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).
Non-peptide molecules in the pedicellariae of Toxopneustes roseus
2020, ToxiconCitation Excerpt :The pedicellaria of T. roseus is considered mildly venomous to human and can deliver a painful sting if touched, causing local inflammation, burning rash, and a local anesthetic effect at the punctured area (personal observation). Although little is known about its chemical composition, other studies in venomous Toxopneustidae species (i.e., Toxopneustes pileolus and Tripneustes gratilla) have documented the presence of several protein compounds in their pedicellariae, including: two D-galactose-specific lectins (SUL-I and SUL-II) (Hatakeyama et al., 2015a; Nakagawa et al., 1996); a heparin-binding lectin (TGL-I) (Nakagawa et al., 1999); a mannose-containing glycoprotein lectin (Contractin A) (Hatakeyama et al., 2015b; Nakagawa et al., 1991, 2003); an acidic protein (UT841), similar in sequence to Contractin A (Zhang et al., 2001); and the Peditoxin, a protein toxin whose prosthetic group (pedoxin) alone is sufficient, even at low doses, to cause anaphylaxis-like shock and death (Kuwabara, 1994). Unfortunately, a large proportion of these works have focused on the study of protein compounds, since they are based on protein purification protocols or cDNA cloning, leaving aside the study of non-peptide active compounds.
CDNA cloning and expression of Contractin A, a phospholipase A<inf>2</inf>-like protein from the globiferous pedicellariae of the venomous sea urchin Toxopneustes pileolus
2015, ToxiconCitation Excerpt :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.
A sea urchin lectin, SUL-1, from the Toxopneustid sea urchin induces DC maturation from human monocyte and drives Th1 polarization in vitro
2006, Toxicology and Applied Pharmacology
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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.