title: Biochemical and physiological properties of pedicellarial lectins from the toxopneustid sea urchins.
abstract: Pedicellarial lectins (SUL-I, SUL-II, and TGL-I) were purified from the toxopneustid sea urchins, Toxopneustes pileolus and Tripneustes gratilla using gel filtration chromatography, affinity chromatography, and reverse-phase HPLC. SUL-I (Nakagawa et al., 1996) and SUL-II from the large globiferous pedicellariae of T. pileolus are D-galactose-binding lectins with molecular masses of 32 kDa and 23 kDa, respectively; while TGL-I from the globiferous pedicellariae of T. gratilla is a Ca(2+)-independent heparin-binding lectin with a molecular mass of 23 kDa. SUL-I induced mitogenic stimulation on murine splenocytes but TGL-I did not. At higher dose ranges SUL-I exhibited inhibitory effects on the cells. The dual response to SUL-I was effectively inhibited by D-galactose. SUL-I enhanced norepinephrine-induced contraction of isolated rat mesenteric artery with endothelium. When endothelium was removed from the artery, acetylcholine did not relax the norepinephrine-induced contraction. In the same artery the enhancing effect of the contraction by SUL-I was abolished, suggesting that SUL-I acts on the endothelium of mesenteric artery, and may release prostanoids. The present results suggest an extracellular function for SUL-I that may have wide-ranging effects in physiological processes. The primary role of pedicellarial lectins from T. pileolus and T. gratilla might be defense against a foreign body.
authors.affiliation: Department of Life Sciences, University of Tokushima, Japan. sea-hide@ias.tokushima-u.ac.jp
authors.forename: H
authors.initials: H
authors.lastname: Nakagawa
authors.forename: C
authors.initials: C
authors.lastname: Yamaguchi
authors.forename: H
authors.initials: H
authors.lastname: Sakai
authors.forename: K
authors.initials: K
authors.lastname: Kanemaru
authors.forename: H
authors.initials: H
authors.lastname: Hayashi
authors.forename: Y
authors.initials: Y
authors.lastname: Araki
authors.forename: Y
authors.initials: Y
authors.lastname: Tomihara
authors.forename: M
authors.initials: M
authors.lastname: Shinohara
authors.forename: K
authors.initials: K
authors.lastname: Ohura
authors.forename: H
authors.initials: H
authors.lastname: Kitagawa
mesh_terms: D000371:Agglutination; D000818:Animals; D002478:Cells, Cultured; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D004730:Endothelium, Vascular / Q000502:physiology; D004912:Erythrocytes / Q000187:drug effects; D005260:Female; D066298:In Vitro Techniques; D037102:Lectins / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology*; D008214:Lymphocytes / Q000187:drug effects; D008297:Male; D008638:Mesenteric Arteries / Q000187:drug effects / Q000502:physiology; D051379:Mice; D008934:Mitogens / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology; D008970:Molecular Weight; D009119:Muscle Contraction / Q000187:drug effects; D009131:Muscle, Smooth, Vascular / Q000187:drug effects; D011817:Rabbits; D051381:Rats; D017207:Rats, Sprague-Dawley; D012617:Sea Urchins; D013154:Spleen / Q000166:cytology / Q000187:drug effects
chemical_list: D037102:Lectins; D008934:Mitogens