ArticleThe Journal of biological chemistry2012
Degradation of an old human protein: age-dependent cleavage of γS-crystallin generates a peptide that binds to cell membranes.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 20 citations in OpenAlex.
- Article
- Article
- New insights into the mechanisms of age-related protein-protein crosslinking in the human lens.Experimental eye research · 2021Review
- Tau Is Truncated in Five Regions of the Normal Adult Human Brain.International journal of molecular sciences · 2021Article
- Spatiotemporal changes in the human lens proteome: Critical insights into long-lived proteins.Progress in retinal and eye research · 2020Review
- Molecular Processes Implicated in Human Age-Related Nuclear Cataract.Investigative ophthalmology & visual science · 2019Review
- Spontaneous cross-linking of proteins at aspartate and asparagine residues is mediated via a succinimide intermediate.The Biochemical journal · 2018Article
- DehydroalanylGly, a new post translational modification resulting from the breakdown of glutathione.Biochimica et biophysica acta. General subjects · 2018Article
- Article
- The etiology of human age-related cataract. Proteins don't last forever.Biochimica et biophysica acta · 2016Review
- Biophysical chemistry of the ageing eye lens.Biophysical reviews · 2015Review
- Effects of photobleaching on selected advanced glycation end products in the human lens.BMC research notes · 2015Article
- The OPEP protein model: from single molecules, amyloid formation, crowding and hydrodynamics to DNA/RNA systems.Chemical Society reviews · 2014Review
- Lens crystallin modifications and cataract in transgenic mice overexpressing acylpeptide hydrolase.The Journal of biological chemistry · 2014Article
- Tyrosine/cysteine cluster sensitizing human γD-crystallin to ultraviolet radiation-induced photoaggregation in vitro.Biochemistry · 2014Article
- The αA66-80 peptide interacts with soluble α-crystallin and induces its aggregation and precipitation: a contribution to age-related cataract formation.Biochemistry · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Long-lived proteins exist in a number of tissues in the human body; however, little is known about the reactions involved in their degradation over time. Lens proteins, which do not turn over, provide a useful system to examine such processes. Using a combination of Western blotting and proteomic methodology, age-related changes to a major protein, γS-crystallin, were studied. By teenage years, insoluble intact γS-crystallin was detected, indicative of protein denaturation. This was not the only change, however, because blots revealed evidence of significant cross-linking as well as cleavage of γS-crystallin in all adult lenses. Cleavage at a serine residue near the C terminus was a major reaction that caused the release of a 12-residue peptide, SPAVQSFRRIVE, which bound tightly to lens cell membranes. Several other crystallin-derived peptides with double basic residues also lodged in the cell membrane fraction. Model studies showed that once cleaved from γS-crystallin, SPAVQSFRRIVE adopts a markedly different shape from that in the intact protein. Further, the acquired helical conformation may explain why the peptide seems to affect water permeability. This observation may help explain the changes to cell membranes known to be associated with aging in human lenses. Age-related cleavage of long-lived proteins may therefore yield peptides with untoward biological activity.
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