F. Favatier et al., Polymorphism in the regulatory sequence of the human hsp70-1 gene does notaffect heat shock factor binding or heat shock protein synthesis, CELL MOL L, 56(7-8), 1999, pp. 701-708
A bi-allelic polymorphism found in the regulatory region of the human heat
shock (MS) protein (HSP) hsp70-1 gene, which comprises an A --> C transvers
ion, 3 bp upstream of the HS element (HSE), has been associated with extend
ed HLA haplotypes. In view of the chaperoning and protective functions of H
sp70, we investigated whether this hsp70-1 bi-allelic polymorphism could mo
dulate the stress response, which may relate to enhanced resistance or susc
eptibility to certain diseases. We compared the basal and MS-induced HS fac
tor (HSF)-binding activity of the two polymorphic HSEs, hsp70-1 mRNA accumu
lation and HSP expression in two human Epstein-Barr virus (EBV)-transformed
B cell lines typed for hsp70-1 promoter alleles. Our results suggest that
hsp70-1 promoter polymorphism does not influence HSF-binding activity, hsp7
0 mRNA accumulation or synthesis in human EBV-transformed B cell lines.