title: 116 kDa glycoprotein isolated from Ulmus davidiana Nakai (UDN) inhibits glucose/glucose oxidase (G/GO)-induced apoptosis in BNL CL.2 cells.
abstract: Ulmus davidiana Nakai (UDN) has been used in folk medicine for its anti-inflammatory activity. In the present study, we investigated the antiapoptotic effect of UDN glycoprotein in glucose/glucose oxidase (G/GO)-induced BNL CL.2 cells. To evaluate the antiapoptotic effect of UDN glycoprotein, experiments were carried out using Western blot analysis for nuclear factor-kappa B (NF-kappaB), caspase-3, and poly(ADP-ribose) polymerase (PARP). We also examined nitric oxide (NO) production and nuclear staining. When BNL CL.2 cells were treated with G/GO (50 mU/ml), viability of the cells was 54.1%. However, the number of living cells after the addition of UDN glycoprotein in the presence of G/GO increased. UDN glycoprotein protected from cell damage caused by G/GO. Interestingly, UDN glycoprotein decreased NF-kappaB activation and stimulated NO production in G/GO-induced BNL CL.2 cells. In apoptotic parameters, UDN glycoprotein inhibited activations of caspase-3 and PARP cleavage in G/GO-induced BNL CL.2 cells. The results of nuclear staining indicated that UDN glycoprotein (50 microg/ml) has a protective ability from apoptotic cell death caused G/GO (50 mU/ml). In conclusion, UDN glycoprotein has a protective effect on apoptosis induced by G/GO through the inhibition of NF-kappaB, caspase-3, and PARP activity, and the stimulation of NO production in BNL CL.2 cells.
authors.affiliation: Molecular Biochemistry Laboratory and Biodefensive Substances Group, Institute of Biotechnology, Chonnam National University, Kwangju, Yongbong-Dong 500-757, South Korea.
authors.forename: Jeong-Hyeon
authors.initials: JH
authors.lastname: Ko
authors.forename: Sei-Jung
authors.initials: SJ
authors.lastname: Lee
authors.forename: Kye-Taek
authors.initials: KT
authors.lastname: Lim
mesh_terms: D000818:Animals; D017209:Apoptosis / Q000187:drug effects*; D015153:Blotting, Western; D053148:Caspase 3; D061945:Caspase Inhibitors; D002374:Catalase / Q000037:antagonists & inhibitors; D002460:Cell Line; D002467:Cell Nucleus / Q000187:drug effects / Q000201:enzymology; D004354:Drug Screening Assays, Antitumor; D004791:Enzyme Inhibitors / Q000302:isolation & purification / Q000494:pharmacology*; D005947:Glucose / Q000037:antagonists & inhibitors* / Q000494:pharmacology*; D005949:Glucose Oxidase / Q000037:antagonists & inhibitors* / Q000494:pharmacology; D006023:Glycoproteins / Q000302:isolation & purification / Q000494:pharmacology*; D051379:Mice; D016328:NF-kappa B / Q000187:drug effects; D009569:Nitric Oxide / Q000037:antagonists & inhibitors / Q000096:biosynthesis; D000067856:Poly(ADP-ribose) Polymerase Inhibitors; D013778:Tetrazolium Salts; D013844:Thiazoles; D034403:Ulmus / Q000737:chemistry*
chemical_list: D061945:Caspase Inhibitors; D004791:Enzyme Inhibitors; D006023:Glycoproteins; D016328:NF-kappa B; D000067856:Poly(ADP-ribose) Polymerase Inhibitors; D013778:Tetrazolium Salts; D013844:Thiazoles; D009569:Nitric Oxide; D005949:Glucose Oxidase; D002374:Catalase; C505409:Casp3 protein, mouse; D053148:Caspase 3; C022616:thiazolyl blue; D005947:Glucose