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Journal of Histochemistry and Cytochemistry, Vol. 51, 1279-1284, October 2003, Copyright © 2003, The Histochemical Society, Inc.

ARTICLE

Distribution of the Serine Protease HtrA1 in Normal Human Tissues

Antonio De Lucaa, Maria De Falcob, Anna Severinoc, Mara Campionic, Daniele Santinid, Feliciano Baldie, Marco G. Paggic, and Alfonso Baldic,e
a Department of Medicine and Public Health, Section of Clinical Anatomy, Second University of Naples, Naples, Italy
b Department of Evolutive and Comparative Biology, University of Naples "Federico II", Naples, Italy
c Center for Experimental Research, Regina Elena Cancer Institute, Rome, Italy
d Service of Oncology, Campus BioMedico University, Rome, Italy
e Department of Biochemistry and Biophysics "F. Cedrangolo," Section of Pathologic Anatomy, Second University of Naples, Naples, Italy

Correspondence to: Alfonso Baldi, Center for Experimental Research, Regina Elena Cancer Institute, Via delle Messi d'Oro, 156, 00158 Rome, Italy. E-mail: baldi@ifo.it

The human HtrA family of proteases consists of three members: HtrA1, HtrA2, and HtrA3. In bacteria, the chief role of HtrA is recognition and degradation of misfolded proteins in the periplasm, combining a dual activity of chaperone and protease. In humans, the three HtrA homologues appear to be involved in diverse functions such as cell growth, apoptosis, allergic reactions, fertilization, control of blood pressure, and blood clotting. Previous studies using RNA blot hybridization have shown that the expression of HtrA1 is ubiquitous in normal human tissues. Here we show by immunohistochemistry (IHC) that HtrA1 is widely expressed, although different tissue distributions and/or levels of expression were detected in the different tissues examined. In particular, high to medium HtrA1 expression was detected in mature layers of epidermis, in secretory breast epithelium, in liver, and in kidney tubules of cortex, in concordance with its secretory properties. Furthermore, we show a higher protein expression level in the epithelium of proliferative endometrium, in contrast to epithelium of secretory endometrium, which is almost completely negative for this protein. This suggests a possible role for HtrA1 in the modulation of tissue activity in this organ. The various expression levels in human tissues indicate several possible roles for HtrA1 in different cell types. (J Histochem Cytochem 51:1279–1284, 2003)

Key Words: HtrA1, human tissues, immunohistochemistry, endometrium


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