Author: Yamazaki Shota Uchiumi Asato Katagata Yohtaro
Publisher: Spandidos Publications
ISSN: 1107-3756
Source: International Journal of Molecular Medicine, Vol.29, Iss.2, 2012-02, pp. : 165-168
Disclaimer: Any content in publications that violate the sovereignty, the constitution or regulations of the PRC is not accepted or approved by CNPIEC.
Abstract
Keratins represent important structural components of intermediate filament proteins. Their expression profiles are remarkably tissue-specific. Recent data have shown that keratins associate with many proteins including heat shock proteins (HSP). We recently identified cell-specific keratin and HSP expression. We aimed to gain further insight into the regulation of keratins by specific inhibition through knockdown of Hsp40 in human keratinocyte cells. Keratin-HSP interaction in HaCaT cell lysate was evaluated by immunoprecipitation followed by Western blotting. Immunofluorescence, was used to examine the co-localization of keratins and Hsp40. Hsp40 depletion led to an increase in the levels of keratin proteins (K5, K14, K10) and a decrease in keratin ubiquitination without influencing keratin gene expression. Our results demonstrate direct or indirectly association of Hsp40 and imply that expressed keratin proteins were regulated by Hsp40 depending on the ubiquitin-proteasome pathway in HaCaT. Furthermore, the K10 differentiation marker was increased by knockdown of Hsp40. The results presented in this study indicate that Hsp40 is related to the differentiation exchange of keratin pairs.
Related content
Ubiquitin-Proteasome Pathway and Prostate Cancer
Oncology Research and Treatment, Vol. 36, Iss. 10, 2013-09 ,pp. :
Respiration, Vol. 74, Iss. 4, 2007-03 ,pp. :
The Longevity of Cultured Human Cells*
JOURNAL OF AMERICAN GERIATRICS SOCIETY, Vol. 22, Iss. 1, 1974-01 ,pp. :
Human Metapneumovirus Impairs Apoptosis of Nasal Epithelial Cells in Asthma via HSP70
Journal of Innate Immunity, Vol. 9, Iss. 1, 2016-10 ,pp. :