Age-related attenuation of HSP47 heat response in fibroblasts

Osamu Miyaishi, Yoshitake Ito, Ken ichi Kozaki, Tuneko Sato, Hajime Takechi, Kazuhiro Nagata, Shinsuke Saga

Research output: Contribution to journalArticle

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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 languageEnglish
Pages (from-to)213-226
Number of pages14
JournalMechanisms of Ageing and Development
Volume77
Issue number3
DOIs
Publication statusPublished - 13-01-1995

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Heat-Shock Proteins
Fibroblasts
Hot Temperature
Molecular Weight
Procollagen
Endoplasmic Reticulum
Molecular Chaperones
Collagen Type I
Northern Blotting
Population
Carrier Proteins
Collagen
Monoclonal Antibodies
RNA

All Science Journal Classification (ASJC) codes

  • Ageing
  • Developmental Biology

Cite this

Miyaishi, Osamu ; Ito, Yoshitake ; Kozaki, Ken ichi ; Sato, Tuneko ; Takechi, Hajime ; Nagata, Kazuhiro ; Saga, Shinsuke. / Age-related attenuation of HSP47 heat response in fibroblasts. In: Mechanisms of Ageing and Development. 1995 ; Vol. 77, No. 3. pp. 213-226.
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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.",
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Miyaishi, O, Ito, Y, Kozaki, KI, Sato, T, Takechi, H, Nagata, K & Saga, S 1995, 'Age-related attenuation of HSP47 heat response in fibroblasts', Mechanisms of Ageing and Development, vol. 77, no. 3, pp. 213-226. https://doi.org/10.1016/0047-6374(94)01517-P

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 journalArticle

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AU - Miyaishi, Osamu

AU - Ito, Yoshitake

AU - Kozaki, Ken ichi

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AU - Takechi, Hajime

AU - Nagata, Kazuhiro

AU - Saga, Shinsuke

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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.

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