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Autoantibody to Heat Shock Protein Hsp40 in Sera of Lung Cancer Patients

Heat shock protein Hsp40 is a stress protein with chaperone activity and has a cooperative function with Hsp70 in mammalian cells. We examined the possible expression of Hsp40 in lung tumor tissues using immunoblotting and immunohistochemistry, and established an enzyme‐linked immuno‐sorbent assay (...

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Detalles Bibliográficos
Autores principales: Oka, Mikio, Sato, Sho‐ichi, Soda, Hiroshi, Fukuda, Minoru, Kawabata, Shigeru, Nakatomi, Katsumi, Shiozawa, Ken, Nakamura, Yo‐ichi, Ohtsuka, Kenzo, Kohno, Shigeru
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Blackwell Publishing Ltd 2001
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5926706/
https://www.ncbi.nlm.nih.gov/pubmed/11267942
http://dx.doi.org/10.1111/j.1349-7006.2001.tb01097.x
Descripción
Sumario:Heat shock protein Hsp40 is a stress protein with chaperone activity and has a cooperative function with Hsp70 in mammalian cells. We examined the possible expression of Hsp40 in lung tumor tissues using immunoblotting and immunohistochemistry, and established an enzyme‐linked immuno‐sorbent assay (ELISA) method to detect IgG antibody to Hsp40 in the serum using purified human Hsp40. Sera were obtained from 130 normal subjects and 50 patients with lung cancer. Lung tumor tissues and cells specifically overexpressed Hsp40, and no such expression was detected in normal lung tissues. Compared with normal sera, significantly higher levels of auto‐antibody to Hsp40 were present in patients with lung cancer. The present study is the first to demonstrate overexpression of Hsp40 in human tumor tissue and the associated presence of autoantibody to Hsp40 in the serum. These results suggest that overexpression of Hsp40 in tumor cells may be recognized as a self‐antigen.