Identification and expression distribution of esophageal carcinoma autoantigens.

e16520 Background: To identify the autoantigen protein molecules with autoserum in the tissues from the esophageal carcinoma (EC) patients, analyze autoantigen expression distribution in EC tissues, so as to provide basis for the molecular pathogenesis and clinical medication of EC. Methods: 69 cases of EC patients tissues and serum and 81 cases of healthy people serum were collected, serological proteome analysis (SERPA) was modified with sequential extraction of subcellular protein fractions to identify esophageal oncopathgensis stages autoantigen with autoserum in the tissues from the EC patients. Another 93 cases of EC patients tissue were collected, immunohistochemical and western blot method were used to detect expression distribution of EC autoantigens in esophageal carcinoma tissue, para-carcinoma tissue and normal tissue. Results: Autoantigens CK13, CK16, CaD, ACTG2, tumor rejection antigen (gp96) 1 variant, heat shock protein gp96 precursor were identified, among wihich, CK16, CaD, ACTG2, tumor rejection antigen (gp96)1 variant, heat shock protein gp96 precursor were firstly reported as EC autoantigens. Expression of autoantigens CK16, CaD, ACTG2 were increased in EC carcinoma tissue than para-carcinoma tissue and normal tissue, while CK13 were decreased. Positive expression level of CK16 in normal tissue, para-carcinoma tissue and cancer tissue of EC patients was 0.0076±0.0033, 0.0158±0.0065, 0.0356±0.0165 respectively, CaD was 0.0085±0.0048, 0.0107±0.0056, 0.0177±0.0103 respectively, ACTG2 was 0.0091±0.0039, 0.0136±0.0043, 0.0214±0.0110 respectively, and CK13 was 0.2053±0.0311, 0.1633±0.0280, 0.0412±0.0239 respectively. Conclusions: 6 EC autoantigens were identified, and 5 were first reported. Autoantigens CK13, CK16, CaD and ACTG2 were expressed in EC patients carcinoma tissue, which can be the potential biomarkers of esophageal carcinoma. This study provides new basis for the EC molecular mechanism and development of molecular drugs.

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Molecular heterogeneity of tumor rejection antigen/heat shock protein GP96

International Journal of Cancer ◽

10.1002/ijc.2910630227 ◽

1995 ◽

Vol 63 (2) ◽

pp. 310-314 ◽

Cited By ~ 34

Author(s):

Anna M. Feldweg ◽

Pramod K. Srivastava

Keyword(s):

Heat Shock ◽

Heat Shock Protein ◽

Tumor Rejection ◽

Molecular Heterogeneity ◽

Heat Shock Protein Gp96 ◽

Tumor Rejection Antigen

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Effects of retinoic acid combined with interferon-gamma on the expression of a tumor rejection antigen (heat shock protein gp96) in human cervical cancer

International Journal of Gynecological Cancer ◽

10.1046/j.1525-1438.1998.09807.x ◽

1998 ◽

Vol 8 (2) ◽

pp. 158-163 ◽

Cited By ~ 2

Author(s):

Santin ◽

Hermonat ◽

Ravaggi ◽

Chiriva-Internati ◽

Pecorelli ◽

...

Keyword(s):

Cervical Cancer ◽

Retinoic Acid ◽

Heat Shock ◽

Heat Shock Protein ◽

Interferon Gamma ◽

Tumor Rejection ◽

Heat Shock Protein Gp96 ◽

Tumor Rejection Antigen ◽

Human Cervical Cancer

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Localization and Significance of Molecular Chaperones, Heat Shock Protein 1, and Tumor Rejection Antigen gp96 in the Male Reproductive Tract and During Capacitation and Acrosome Reaction1

Biology of Reproduction ◽

10.1095/biolreprod.104.034470 ◽

2005 ◽

Vol 72 (2) ◽

pp. 328-337 ◽

Cited By ~ 63

Author(s):

Kelly L. Asquith ◽

Amanda J. Harman ◽

Eileen A. McLaughlin ◽

Brett Nixon ◽

R. John Aitken

Keyword(s):

Heat Shock ◽

Heat Shock Protein ◽

Molecular Chaperones ◽

Reproductive Tract ◽

Tumor Rejection ◽

Male Reproductive Tract ◽

Tumor Rejection Antigen

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Secretory Heat Shock Protein - gp96-Ig Chaperoned Her-2/new Vaccines

10.21236/ada382781 ◽

1999 ◽

Author(s):

Eckhard Podack

Keyword(s):

Heat Shock ◽

Heat Shock Protein ◽

Heat Shock Protein Gp96 ◽

Her 2 ◽

New Vaccines

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Cross-priming of minor histocompatibility antigen-specific cytotoxic T cells upon immunization with the heat shock protein gp96.

Journal of Experimental Medicine ◽

10.1084/jem.182.3.885 ◽

1995 ◽

Vol 182 (3) ◽

pp. 885-889 ◽

Cited By ~ 249

Author(s):

D Arnold ◽

S Faath ◽

H Rammensee ◽

H Schild

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

Heat Shock Protein ◽

Tumor Cells ◽

Mhc Class I ◽

Donor Cell ◽

Class I ◽

Heat Shock Protein Gp96 ◽

Shock Proteins

Vaccination of mice with heat shock proteins isolated from tumor cells induces immunity to subsequent challenge with those tumor cells the heat shock protein was isolated from but not with other tumor cells (Udono, H., and P.K. Srivastava. 1994. J. Immunol. 152:5398-5403). The specificity of this immune response is caused by tumor-derived peptides bound to the heat shock proteins (Udono., H., and P.K. Srivastava. 1993. J. Exp. Med. 178:1391-1396). Our experiments show that a single immunization with the heat shock protein gp96 isolated from beta-galactosidase (beta-gal) expressing P815 cells (of DBA/2 origin) induces cytotoxic T lymphocytes (CTLs) specific for beta-gal, in addition to minor H antigens expressed by these cells. CTLs can be induced in mice that are major histocompatibility complex (MHC) identical to the gp96 donor cells (H-2d) as well as in mice with a different MHC (H-2b). Thus gp96 is able to induce "cross priming" (Matzinger, P., and M.J. Bevan. 1977. Cell. Immunol. 33:92-100), indicating that gp96-associated peptides are not limited to the MHC class I ligands of the gp96 donor cell. Our data confirm the notion that samples of all cellular antigens presentable by MHC class I molecules are represented by peptides associated with gp96 molecules of that cell, even if the fitting MHC molecule is not expressed. In addition, we extend previous reports on the in vivo immunogenicity of peptides associated gp96 molecules to two new groups of antigens, minor H antigens, and proteins expressed in the cytosol.

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