dc.contributor.author | Bahmani, P | |
dc.contributor.author | Halabian, R | |
dc.contributor.author | Rouhbakhsh, M | |
dc.contributor.author | Roushandeh, AM | |
dc.contributor.author | Masroori, N | |
dc.contributor.author | Ebrahimi, M | |
dc.contributor.author | Samadikuchaksaraei, A | |
dc.contributor.author | Shokrgozar, MA | |
dc.contributor.author | Roudkenar, MH | |
dc.date.accessioned | 2018-08-26T09:31:19Z | |
dc.date.available | 2018-08-26T09:31:19Z | |
dc.date.issued | 2010 | |
dc.identifier.uri | http://dspace.tbzmed.ac.ir:8080/xmlui/handle/123456789/56999 | |
dc.description.abstract | Lipocalin-2 (Lcn2, NGAL) is a member of the lipocalin super family with diverse function such as the induction of apoptosis, the suppression of bacterial growth, and modulation of inflammatory response. Much interest has recently been focused on the physiological/pathological role of the lipocalin-2 that is considered to be a novel protective factor against oxidative stress. However, its precise biological roles in this protection are not fully understood. In this report we intended to test the effect of lipocalin-2 on the expression of heme oxygenase (1, 2) and superoxide dismutase (1, 2) which are two strong antioxidants. NGAL was cloned to pcDNA3.1 plasmid by using genetic engineering method. The recombinant vector was transfected to CHO and HEK293T to establish stable cell expressing NGAL and the expression of HO-1, 2 and SOD1, 2 were compared with appropriate controls byRT-PCR and western blot. On the other hand, expression of NGAL was suppressed by siRNA transfection in order to study the effect of lipocalin-2 on mentioned genes/proteins. The results showed that the expression of HO-1 and SOD 1, 2 enzymes were higher in cells expressing recombinant lipocalin-2 compared with the control cells. Although the expression of HO-1 was lower in NGAL silencing cells, the expression of SOD1 and SOD2 were higher. Our data suggest that NGAL is a potent inducer of HO-1 and somewhat SOD1 and SOD2 and it appears that part of antioxidant property of NGAL could be attributed to the induction of HO-1and SOD 1, 2. © Cell Stress Society International 2009. | |
dc.language.iso | English | |
dc.relation.ispartof | Cell Stress and Chaperones | |
dc.subject | copper zinc superoxide dismutase | |
dc.subject | heme oxygenase 1 | |
dc.subject | heme oxygenase 2 | |
dc.subject | manganese superoxide dismutase | |
dc.subject | neutrophil gelatinase associated lipocalin | |
dc.subject | plasmid DNA | |
dc.subject | recombinant protein | |
dc.subject | small interfering RNA | |
dc.subject | acute phase protein | |
dc.subject | copper zinc superoxide dismutase | |
dc.subject | heme oxygenase 1 | |
dc.subject | LCN2 protein, human | |
dc.subject | lipocalin | |
dc.subject | manganese superoxide dismutase | |
dc.subject | oncoprotein | |
dc.subject | superoxide dismutase | |
dc.subject | animal cell | |
dc.subject | article | |
dc.subject | cell strain HEK293 | |
dc.subject | cell strain HepG2 | |
dc.subject | CHO cell | |
dc.subject | controlled study | |
dc.subject | down regulation | |
dc.subject | gene silencing | |
dc.subject | genetic engineering | |
dc.subject | genetic transfection | |
dc.subject | human | |
dc.subject | human cell | |
dc.subject | molecular cloning | |
dc.subject | nonhuman | |
dc.subject | plasmid | |
dc.subject | priority journal | |
dc.subject | protein expression | |
dc.subject | reverse transcription polymerase chain reaction | |
dc.subject | Western blotting | |
dc.subject | animal | |
dc.subject | cell line | |
dc.subject | CHO cell line | |
dc.subject | Cricetulus | |
dc.subject | genetics | |
dc.subject | hamster | |
dc.subject | metabolism | |
dc.subject | oxidative stress | |
dc.subject | RNA interference | |
dc.subject | Acute-Phase Proteins | |
dc.subject | Animals | |
dc.subject | Cell Line | |
dc.subject | CHO Cells | |
dc.subject | Cricetinae | |
dc.subject | Cricetulus | |
dc.subject | Heme Oxygenase-1 | |
dc.subject | Humans | |
dc.subject | Lipocalins | |
dc.subject | Oxidative Stress | |
dc.subject | Proto-Oncogene Proteins | |
dc.subject | RNA Interference | |
dc.subject | RNA, Small Interfering | |
dc.subject | Superoxide Dismutase | |
dc.subject | Transfection | |
dc.subject | Bacteria (microorganisms) | |
dc.subject | Acute-Phase Proteins | |
dc.subject | Animals | |
dc.subject | Cell Line | |
dc.subject | CHO Cells | |
dc.subject | Cricetinae | |
dc.subject | Cricetulus | |
dc.subject | Heme Oxygenase-1 | |
dc.subject | Humans | |
dc.subject | Lipocalins | |
dc.subject | Oxidative Stress | |
dc.subject | Proto-Oncogene Proteins | |
dc.subject | RNA Interference | |
dc.subject | RNA, Small Interfering | |
dc.subject | Superoxide Dismutase | |
dc.subject | Transfection | |
dc.title | Neutrophil Gelatinase-Associated Lipocalin induces the expression of heme oxygenase-1 and superoxide dismutase 1, 2 | |
dc.type | Article | |
dc.citation.volume | 15 | |
dc.citation.issue | 4 | |
dc.citation.spage | 395 | |
dc.citation.epage | 403 | |
dc.citation.index | Scopus | |
dc.identifier.DOI | https://doi.org/10.1007/s12192-009-0154-5 | |