Aging at the Molecular Level - download pdf or read online

By Nicolle Sitte, Thomas von Zglinicki (auth.), Thomas von Zglinicki (eds.)

ISBN-10: 9048164826

ISBN-13: 9789048164820

ISBN-10: 9401706670

ISBN-13: 9789401706674

During the final forty years, the examine of the organic foundation of getting older has improved significantly, and it has now turn into an autonomous and first rate box of analysis and examine. the fundamental explanation for getting older is molecular harm that slowly overwhelms mobile and organismic protection, fix and upkeep structures. lately, a wealth of hugely refined study has remodeled this concept from a reputable speculation not just to a tremendous concept, yet primarily to permitted wisdom. getting older on the Molecular point examines the foremost parts during this transformation.
Bringing jointly contributions from a global staff of authors, this quantity might be of curiosity to graduates and postgraduates within the fields of drugs and nursing, researchers of alternative features of biogerontology and people within the pharmaceutical, cosmeceutical, nutraceutical and health-care industry.

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Several studies have verified that irreversible oxidation of protein sulfhydryls is more extensive in aged tissue samples. If these damaged proteins are not sufficiently removed by proteolysis, aged cells may accumulate increased amounts of protein containing damaged sulfhydryls. An adequate pool of glutathione as a protectant is essential to prevent this increase in sulfhydryl oxidation. However, changes in the glutathione redox status during the aging process indicate that there is only a limited potential for regeneration of oxidized protein sulfhydryls left [reviewed in ref.

Examples for specific oxidation ofaromatic amino acid residues (see Table 1) are the conversion of phenylalanine to a-tyrosine, m-tyrosine and 3-nitrophenylalanine, respectively (Figure 4). Another amino acid residue present in proteins that is susceptible to oxidation is the indole moiety of tryptophan. The reducing potential is considerably less than that of cysteine and methionine, so oxidation of tryptophanyl residues usually does not occur until all exposed thiol residues are oxidized. Tryptophan residues are the only chromophoric moieties in proteins which can be photooxidized to tryptophanyl radicals by UV radiation [14].

Thus, exposure of old houseflies to X-irradiation led to greater increase in the protein carbonyl content and to greater loss of glucose-6-phosphate dehydrogenase activity compared to young flies [52]. The age-related accumulation of oxidized proteins may result from an increase in protein oxidation or a decline in the degradation of oxidized proteins. It was suggested that both processes actually contribute to an age-related accumulation of oxidized compounds. There is a strong indication that protein turnover in cells and tissues tends to decline with age, and we now have good evidence demonstrating an actual decrease in the activity of the major cytosolic protease - the proteasomal system [reviewed in ref.

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Aging at the Molecular Level by Nicolle Sitte, Thomas von Zglinicki (auth.), Thomas von Zglinicki (eds.)


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