The effect of aging on the chaperone concentrations in the hepatic, endoplasmic reticulum of male rats: the possible role of protein misfolding due to the loss of chaperones in the decline in physiological function seen with age
| Autor: | Jordan L. Holtzman, Lisa M. Dunning, Richard R. Erickson |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Male
Aging Protein Folding Calnexin Immunoblotting Endoplasmic Reticulum Sensitivity and Specificity Rats Sprague-Dawley Reference Values Animals Probability Physiological function biology Endoplasmic reticulum Body Weight Cell biology Rats Survival Rate Disease Models Animal Secretory protein Membrane protein Liver Chaperone (protein) biology.protein Protein folding Geriatrics and Gerontology Calreticulin Biomarkers Molecular Chaperones |
| Zdroj: | The journals of gerontology. Series A, Biological sciences and medical sciences. 61(5) |
| ISSN: | 1079-5006 |
| Popis: | The endoplasmic reticulum (ER) chaperones are highly conserved proteins that catalyze the posttranslational processing of all secretory and membrane proteins. Our studies suggest that chaperone declines are one of the two central defects in Alzheimer's disease. We propose that similar declines in other organ systems underlie the physiological deficits of aging. Rats were maintained in a colony from age 21 days to death. Animals were killed at regular intervals, and hepatic, ER chaperone contents were determined by immunoblotting. ERp55, ERp57, ERp72, BiP, and calnexin constitutive levels declined 30%-50% with age. Calreticulin was unaffected. BiP (also known as GRP78), ERp55, and ERp57 showed marked swings with peaks occurring in midwinter and midsummer. This cyclics declined 73% with age. Considering the role of the ER chaperones in membrane and secretory protein posttranslational processing, these data support the concept that their loss could lead to many of the physiological declines associated with aging. |
| Databáze: | OpenAIRE |
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