02357nas a2200277   4500008004100000022001400041245015900055210006900214260009000283300001200373490000700385520127400392653002401666653002801690653002901718653003401747100002001781700002401801700002001825700002401845700001901869700002001888700002301908700002001931856012801951       2008                        eng d  a1071-576200aAnalysis of reactive oxygen species and antioxidant defenses in complex I deficient patients revealed a specific increase in superoxide dismutase activity0 aAnalysis of reactive oxygen species and antioxidant defenses in   aTELEPHONE HOUSE, 69-77 PAUL STREET, LONDON EC2A 4LQ, ENGLANDbINFORMA HEALTHCAREcMAY  a415-4270 v423 a<p>The mechanism of free radical production by complex I deficiency is ill-defined, although it is of significant contemporary interest. This study studied the ROS production and antioxidant defenses in children with mitochondrial NADH dehydrogenase deficiency. ROS production has remained significantly elevated in patients compared to controls. The expression of all antioxidant enzymes significantly increased at mRNA level. However, the enzyme activities did not correlate with high mRNA or protein expression. Only the activity of superoxide dismutase (SOD) was found to correlate with higher mRNA expression in patient derived cell lines. The activities of the enzymes such as glutathione peroxidase (GPx), Catalase (CAT) and glutathione-S-transferase (GST) were significantly reduced in patients (p &lt; 0.05 or p &lt; 0.01). Glutathione reductase (GR) activity and intracellular glutathione (GSH) levels were not changed. Decreased enzyme activities could be due to post-translational or oxidative modification of ROS scavenging enzymes. The information on the status of ROS and marking the alteration of ROS scavenging enzymes in peripheral lymphocytes or lymphoblast cell lines will provide a better way to design antioxidant therapies for such disorders.</p>10aantioxidant enzymes10amitochondrial complex I10amitochondrial myopathies10aReactive Oxygen Species (ROS)1 aWani, Aijaz, A.1 aRangrez, Ashraf, Y.1 aKumar, Himanshu1 aBapat, Sharmila, A.1 aSuresh, C., G.1 aBarnabas, Shama1 aPatole, Milind, S.1 aShouche, Yogesh  uhttps://library.ncl.res.in/content/analysis-reactive-oxygen-species-and-antioxidant-defenses-complex-i-deficient-patients-001704nas a2200205   4500008004100000022001400041245009100055210006900146260000800215300001600223490000700239520100400246100002301250700002001273700002701293700002101320700002001341700002101361856011601382       2022                        eng d  a2041-652000aBQ-AurIPr: a redox-active anticancer Au(i) complex that induces immunogenic cell death0 aBQAurIPr a redoxactive anticancer Aui complex that induces immun  cSEP  a10779-107850 v133 a<p>
	Immunogenic Cell Death (ICD) is a unique cell death mechanism that kills cancer cells while rejuvenating the anticancer immunosurveillance, thereby benefiting the clinical outcomes of various immuno-chemotherapeutic regimens. Herein, we report development of a library of benzo[a]quinolizinium-based Au(i) complexes through an intramolecular amino-auration reaction of pyridino-alkynes. We tested 40 candidates and successfully identified BQ-AurIPr as a novel redox-active Au(i) complex with potent anticancer properties. BQ-AurIPr efficiently triggered generation of DAMPs - the hallmarks of ICD - and was superior in terms of efficiency compared to FDA-approved drugs known to induce ICD. BQ-AurIPr significantly increased immunogenicity of cancer cells enhancing their phagocytosis when co-cultured with immune cells. Our investigation reveals that BQ-AurIPr induces oxidative stress inside mitochondria leading to mitophagy, as the mechanism for immunogenic cell death in A549 cells.</p>
1 aMule, Ravindra, D.1 aKumar, Akhilesh1 aSancheti, Shashank, P.1 aSenthilkumar, B.1 aKumar, Himanshu1 aPatil, Nitin, T.  uhttps://library.ncl.res.in/content/bq-auripr-redox-active-anticancer-aui-complex-induces-immunogenic-cell-death