Crystallin belongs to a small heat shock

protein family with chaperone functions that prevent heat-induced and oxidative stress-induced aggregation proteins [15]. In an inflammation-activated mouse model, crystallin pretreatment reduced tumor necrosis factor-α (TNF-α) and nitric oxide (NO) production in lipopolysaccharide (LPS)-activated astrocytes [16]. This suggested the ability to prevent the inflammation-triggered neurotoxicity by crystallin. Recently, as a class of heat shock protein, Selleck INCB024360 crystallin exhibits protective function in LPS-induced proinflammation release and therapeutic role in neurodegenerative diseases, including Parkinson’s disease, Alzheimer’s disease and

multiple sclerosis [17], [18] and [19]. The role of crystallin in vitro in relation to the function of macrophage activation during nodavirus-infected grouper is not clear. In this report, the focus was on the well-characterized nodavirus-mediated neuropathogenesis of grouper, aiming to reveal any association between nodavirus infection an oxidative damage to brain area. Nodavirus infection was associated with increased production of ROS. Dityrosine, a useful marker for protein oxidation, was involved in amino acid hydroxylation of brain and eye tissue during nodavirus infection in groupers. Injury mediated by free radicals, particularly by ROS, is an important common

pathway of such varied pathological KU-57788 purchase processes as inflammatory damage [20] and neurodegenerative diseases [21]. These previous and present observations indicate tuclazepam that recombinant crystallin is capable of activation of macrophages [22], which is accompanied by production of nitric oxide (NO). A crystallin cDNA from orange-spotted grouper Epinephelus coioides was cloned and its expression was characterized. Grouper crystallin possessed chaperone functions that prevented heat-induced and oxidative stress-induced aggregation proteins. Collectively, these observations indicate that crystallin has the potential to act as an anti-inflammatory agent in neuroprotective processes. The grouper cell line GF-1 [23] was grown at 28 °C in Leibovitz’s L-15 medium (GibcoBRL, Gaithersburg, MD, USA) supplemented with 5% fetal bovine serum (FBS). GF-1 grouper cells, which are susceptible to nodavirus infection and replication, were obtained from the Taiwan Bioresources Collection and Research Center. Transient transfections were performed by introducing 1–2 μg of plasmid encoding grouper crystallin into cells using Lipofectamine (Invitrogen, Carlsbad, CA, USA). After transfection, cells were grown for 24–30 h. Intracellular localization of crystallin proteins was examined using a model IX70 microscope (Olympus, Tokyo, Japan).