Polymorphism in the regulatory sequence of the human hsp70-1 gene does notaffect heat shock factor binding or heat shock protein synthesis

Citation
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
Citations number
39
Categorie Soggetti
Cell & Developmental Biology
Journal title
CELLULAR AND MOLECULAR LIFE SCIENCES
ISSN journal
1420682X → ACNP
Volume
56
Issue
7-8
Year of publication
1999
Pages
701 - 708
Database
ISI
SICI code
1420-682X(19991115)56:7-8<701:PITRSO>2.0.ZU;2-F
Abstract
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.