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 |
|---|---|
| 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 |
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Keywords
- Aging
- Fibroblasts
- Heat response
- HSP47 expression
- Procollagen
ASJC Scopus subject areas
- Ageing
- Developmental Biology
- Biochemistry
- Developmental Neuroscience
Cite this
Age-related attenuation of HSP47 heat response in fibroblasts. / Miyaishi, Osamu; Ito, Yoshitake; Kozaki, Ken ichi; Sato, Tuneko; Takechi, Hajime; Nagata, Kazuhiro; Saga, Shinsuke.
In: Mechanisms of Ageing and Development, Vol. 77, No. 3, 13.01.1995, p. 213-226.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Age-related attenuation of HSP47 heat response in fibroblasts
AU - Miyaishi, Osamu
AU - Ito, Yoshitake
AU - Kozaki, Ken ichi
AU - Sato, Tuneko
AU - Takechi, Hajime
AU - Nagata, Kazuhiro
AU - Saga, Shinsuke
PY - 1995/1/13
Y1 - 1995/1/13
N2 - 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.
AB - 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.
KW - Aging
KW - Fibroblasts
KW - Heat response
KW - HSP47 expression
KW - Procollagen
UR - http://www.scopus.com/inward/record.url?scp=0028861387&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028861387&partnerID=8YFLogxK
U2 - 10.1016/0047-6374(94)01517-P
DO - 10.1016/0047-6374(94)01517-P
M3 - Article
C2 - 7739268
AN - SCOPUS:0028861387
VL - 77
SP - 213
EP - 226
JO - Mechanisms of Ageing and Development
JF - Mechanisms of Ageing and Development
SN - 0047-6374
IS - 3
ER -