Literature DB >> 3070182

Decline in protease activities with age in the nematode Caenorhabditis elegans.

G J Sarkis1, J D Ashcom, J M Hawdon, L A Jacobson.   

Abstract

The activities of 3 lysosomal proteases in the nematode Caenorhabditis elegans are markedly lower in older animals. The aspartyl protease cathepsin D declines about 10-fold from day 3 (early adulthood) to day 11 (near the mean lifespan); this reflects a net decline in the amount of cathepsin D antigen. The specific activity of the thiol protease cathepsin Ce1 declines about 2.5-fold over the same period, and the specific activity of the thiol protease cathepsin Ce2 declines about 8-fold. The activity of a new non-lysosomal protease, designated cathepsin CeX, is invariant with age. The data are consistent with the hypothesis that reduced protease activity in older animals may cause a decline in the rate of protein turnover with age, but do not prove this hypothesis.

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Year:  1988        PMID: 3070182     DOI: 10.1016/0047-6374(88)90001-2

Source DB:  PubMed          Journal:  Mech Ageing Dev        ISSN: 0047-6374            Impact factor:   5.432


  23 in total

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3.  Evidence for lysosomal processing of amyloid beta-protein precursor in cultured cells.

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8.  Expression and characterization of aspartic protease gene in eggs and larvae stage of Ancylostoma caninum.

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Journal:  Parasitol Res       Date:  2009-01-24       Impact factor: 2.289

Review 9.  Autophagy as a promoter of longevity: insights from model organisms.

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Journal:  Nat Rev Mol Cell Biol       Date:  2018-09       Impact factor: 94.444

Review 10.  Molecular and cellular pathways contributing to brain aging.

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