Expression of heat shock proteins HSPA1A, HSPA1B and TP53 in vulval lichen planus and vulval lichen sclerosus.

Abstract

Objectives: Heat shock proteins (HSPs) are proteins involved in protein folding and maturation. HSP expression is induced by heat shock or other stressors including cellular damage and hypoxia. The major groups, which are classified based on their molecular weight, include HSP27, HSP40, HSP60, HSP70, HSP90, and large HSP (HSP110 and glucose-regulated protein 170). The comparison of heat shock proteins and TP53 expression is yet not well studied in both vulval lichen sclerosus and lichen planus. Our aim was to assess the HSP and TP53 gene expression in women suffering from LS or LP and compare it within these groups and also healthy controls.

Material and methods: The inclusion criteria were willingness to donate vulval biopsies, not currently or in the prior two weeks received any local nor systemic treatment for vulval disorder, age > 18 years old. The exclusion criteria were lack of consent, current vaginal infection confirmed with microbiological studies, current local or systemic treatment for vulval disease. 45 consecutive women were recruited into the study. All appropriate vulval samples were process by genetic analysis.

Results: The mean expression (± SD) of HPSA1A for controls was 5.52 ± 3.18, for LS was 7.44 ± 2.16 and for LP was 7.89 ± 2.48. The mean expression (± SD) of HPSA1B for controls was 6.54 ± 3.41, for LS was 9.94 ± 6.88 and for LP was 9.43 ± 2.31. The mean expression (± SD) of TP53 for controls was 9.11 ± 1.14, for LS was 9.94 ± 1.27 and for LP was 10.41 ± 2.00. HSPA1A expression was 3,8 higher in women with lichen sclerosus than in control group.

Conclusions: Heat shock protein-70 is more often expressed in LS than in healthy controls. HSP-70 not only supports tumor growth and metastasis, but on the other hand mat help to develop immune-driven treatment strategies.