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, Diagnosis an-&& of Shrimp Diseases - Central Institute of ...

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cells. It has been shown that possibly some c<strong>an</strong>cers may originate as a result <strong>of</strong> faulty repair<strong>of</strong> DNA damage produced by free radicals.Lipid peroxidation, (LPO) in biological membr<strong>an</strong>es causes alterations in fluidity, fallin membr<strong>an</strong>e potential, increased permeability to H+ <strong>an</strong>d other ions <strong>an</strong>d eventual ruptureleading to release <strong>of</strong> cell <strong>an</strong>d org<strong>an</strong>elle contents such as lysosomal hydrolytic enzymes.Earlier it was shown that the disrupted or damaged tissues undergo lipid peroxidation at afaster rate th<strong>an</strong> their healthy counterparts. Hence the sequence <strong>of</strong> events may be conjured upas:Disease or Toxin + cell damage or death + increased LPO which will well expIainthe elevated lipid peroxidation products in disease <strong>an</strong>d toxicology.Cellular Defense by Antioxid<strong>an</strong>t Enzymes <strong>an</strong>d free Radical ScavengersAvoid<strong>an</strong>ce <strong>of</strong> free radical formationPotentially injurious effects <strong>of</strong> oxid<strong>an</strong>ts <strong>an</strong>d free radicals on the living org<strong>an</strong>ism areprevented by a well-org<strong>an</strong>ised defense system <strong>an</strong>d they function at four levels. The first <strong>an</strong>dbest effort is avoid<strong>an</strong>ce. This is achieved by cytochrome oxidase <strong>an</strong>d other metalloenzymes. They help the cells in carrying out the tetravalent reduction <strong>of</strong> oxygen to waterwithout releasing the toxic intermediates in a free state. Further, metal ions, which couldparticipate in the oxid<strong>an</strong>t producing reactions, are generally carried or sequestered by proteinslike tr<strong>an</strong>sferrin <strong>an</strong>d ferritin, so as to minimise the amount <strong>of</strong> free iron in the cells. Similarlycopper is bound to ceruloplasmin <strong>an</strong>d the ionic form is not generally available in the freestate. Albumin binds copper tightly <strong>an</strong>d iron weakly. Haptoglobin/hemopexin binds freehemoglobinlheme. Hemoglobin <strong>an</strong>d methemoglobin are powerful peroxides <strong>an</strong>d c<strong>an</strong>accelerate lipid peroxidation while haptoglobin inhibits the reaction by binding tohaemoglobin. The <strong>an</strong>tioxid<strong>an</strong>f role <strong>of</strong> urate is due to its ability to tightly bind iron <strong>an</strong>d copperions.Prevention <strong>of</strong> free radicals (FRs) acting on the cellThe second line <strong>of</strong> defense is prevention, by providing a continuous supply <strong>of</strong> GSH.The oxidised <strong>an</strong>d reduced glutathiones are interconvertible <strong>an</strong>d the cell maintains the bulk inthe active (reduced) form. This reaction-is catalysed by the enzyme glutathione reductase.GlutathioneGSSG + NADPH2GSH + NADPreductase

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