Abstract
The collagen-binding heat shock protein of molecular weight 47 000 (HSP47), resident in the endoplasmic reticulum (ER), is assumed to play a specific role as a molecular chaperon in the processing of procollagen molecules. The present investigation of age-related alteration in the HSP47 heat response in cultured murine and human fibroblasts revealed expression in cells with a low population doubling level (PDL) derived from young mice and people more inducible by heat treatment than those from older mice and people. On the other hand, cells with a high PDL showed a very low heat response in terms of HSP47 expression regardless of the donor age. Northern blot analysis of HSP47 m-RNA indicated that the age related attenuation of HSP47 expression was regulated by transcriptional mechanisms. Furthermore, immunofluorescent analysis using a monoclonal antibody against the carboxylterminal propeptide of type I procollagen revealed far greater retention of procollagen molecules in the ER lumen of cells from old persons than in those from young persons. This was particularly prominent in heat-treated cells from old persons, indicating the possibility that the observed decrease in HSP47 heat response might cause blockage of procollagen transport to the Golgi and therefore secretion.
Original language | English |
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Pages (from-to) | 213-226 |
Number of pages | 14 |
Journal | Mechanisms of Ageing and Development |
Volume | 77 |
Issue number | 3 |
DOIs | |
Publication status | Published - Jan 13 1995 |
Externally published | Yes |
Keywords
- Aging
- Fibroblasts
- HSP47 expression
- Heat response
- Procollagen
ASJC Scopus subject areas
- Ageing
- Developmental Biology