Chlamydia trachomatis heat shock proteins 60 and 10 induce apoptosis in endocervical epithelial cells.

AIM AND OBJECTIVE

The potential role of chlamydial heat shock proteins (cHSP) 60 and cHSP10 in apoptosis of primary cervical epithelial cells was investigated.

METHODS

Primary cervical epithelial cells were stimulated with cHSP60 and cHSP10 for 4 h. Quantitative measurements of apoptosis were made using cytofluorometry, and apoptosis-related genes were analyzed by microarray, real-time PCR and western blotting. Further, levels of proinflammatory cytokines (IL-18 and IL-1β) were determined by semi-quantitative RT-PCR.

RESULTS

After a 4-h incubation in the presence of recombinant cHSP60 or cHSP10, the number of cells exhibiting annexin V binding activity increased 6- and 5-fold, respectively (P < 0.05). A DNA microarray study showed significant (P < 0.05) upregulation of interleukin (IL)-1 β-convertase, and caspase-3, -8 and -9 genes in cHSP60- and cHSP10-stimulated than in control cells as confirmed by real-time RT-PCR and western blotting. Transcript levels of IL-1β and IL-18 in cells treated with cHSP60 and cHSP10 were found to be significantly (P < 0.05) higher in stimulated than in control cells.

CONCLUSION

cHSP60- and cHSP10-induced caspase expression, proinflammatory cytokine production and apoptosis of primary cervical epithelial cells might play a role in the pathogenesis of infertility in women with persistent chlamydial infection.