The Role of Heat Shock Proteins in Pathogenesis of Oral Squamous Cell Carcinoma

Cell in the distress situation, denaturation of proteins may occur, and may also respond by expressing stress proteins. however, such homeostasis effort does not always succeed and even may lead to disease, including cancer. in distress situation also ensue much protein misfolding. objective; this research were to explain the role of heat shock protein 40 (hsp40) and hsp70 in pathogenesis of occurred oral squamous cell carcinoma (ossc) patient which realized human papilloma virus (hpv) infection. material and method; tissue biopsy frozen section were taken from bosc and oscc patients was cut into three part. parrafin blocks were made from cutting i, which was subsequently stains with he to ascertain the type of neoplasm. cutting ii was subjected to dna isolation. the dna isolation results were subjected to pcr to amplify li-hpv gene for fixed the hpv stressor. protein isolation was treated from cutting iii, followed with blottdot test by using antibody monoclonal anti hsp40 and hsp70 and continued with measurement using densitometer to find the concentration of hsp40 and hsp70. the collected data were analyzed with f test (manova) and discriminant analysis. result; this experiment showed the differences in concentration of hsp40 (p<=0,070) and hsp70 (p<=0,006) between benign oral squamous cell (bosc) and oscc patients which realized hpv infection. conclusion; this experiment proved that oscc patients which realized hpv infection indicated an up regulated of hsp70 concentration, so that there was occurs misfolding of the proteins cell. the misfolding was ensue obstacle of apoptosis and to raise cell proliferation which to storm carcinogenesis. an up regulated of hsp40 was role as co-chaperone.