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Differential Expression of HSPA1 and HSPA2 Proteins in Human Tissues; Tissue Microarray-based Immunohistochemical Study

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Publisher Springer
Date 2011 Mar 5
PMID 21373891
Citations 25
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Abstract

In the present study we determined the expression pattern of HSPA1 and HSPA2 proteins in various normal human tissues by tissue-microarray based immunohistochemical analysis. Both proteins belong to the HSPA (HSP70) family of heat shock proteins. The HSPA2 is encoded by the gene originally defined as testis-specific, while HSPA1 is encoded by the stress-inducible genes (HSPA1A and HSPA1B). Our study revealed that both proteins are expressed only in some tissues from the 24 ones examined. HSPA2 was detected in adrenal gland, bronchus, cerebellum, cerebrum, colon, esophagus, kidney, skin, small intestine, stomach and testis, but not in adipose tissue, bladder, breast, cardiac muscle, diaphragm, liver, lung, lymph node, pancreas, prostate, skeletal muscle, spleen, thyroid. Expression of HSPA1 was detected in adrenal gland, bladder, breast, bronchus, cardiac muscle, esophagus, kidney, prostate, skin, but not in other tissues examined. Moreover, HSPA2 and HSPA1 proteins were found to be expressed in a cell-type-specific manner. The most pronounced cell-type expression pattern was found for HSPA2 protein. In the case of stratified squamous epithelia of the skin and esophagus, as well as in ciliated pseudostratified columnar epithelium lining respiratory tract, the HSPA2 positive cells were located in the basal layer. In the colon, small intestine and bronchus epithelia HSPA2 was detected in goblet cells. In adrenal gland cortex HSPA2 expression was limited to cells of zona reticularis. The presented results clearly show that certain human tissues constitutively express varying levels of HSPA1 and HSPA2 proteins in a highly differentiated way. Thus, our study can help designing experimental models suitable for cell- and tissue-type-specific functional differences between HSPA2 and HSPA1 proteins in human tissues.

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References
1.
Lebret T, Watson R, Molinie V, ONeill A, Gabriel C, Fitzpatrick J . Heat shock proteins HSP27, HSP60, HSP70, and HSP90: expression in bladder carcinoma. Cancer. 2003; 98(5):970-7. DOI: 10.1002/cncr.11594. View

2.
Otaka M, Odashima M, Tamaki K, Watanabe S . Expression and function of stress (heat shock) proteins in gastrointestinal tract. Int J Hyperthermia. 2009; 25(8):634-40. DOI: 10.3109/02656730903315815. View

3.
Hu S, Ciancio M, Lahav M, Fujiya M, Lichtenstein L, Anant S . Translational inhibition of colonic epithelial heat shock proteins by IFN-gamma and TNF-alpha in intestinal inflammation. Gastroenterology. 2007; 133(6):1893-904. PMC: 2180161. DOI: 10.1053/j.gastro.2007.09.026. View

4.
Rosario M, Perkins S, OBrien D, Allen R, Eddy E . Identification of the gene for the developmentally expressed 70 kDa heat-shock protein (P70) of mouse spermatogenic cells. Dev Biol. 1992; 150(1):1-11. DOI: 10.1016/0012-1606(92)90002-x. View

5.
Su A, Wiltshire T, Batalov S, Lapp H, Ching K, Block D . A gene atlas of the mouse and human protein-encoding transcriptomes. Proc Natl Acad Sci U S A. 2004; 101(16):6062-7. PMC: 395923. DOI: 10.1073/pnas.0400782101. View