Objective: Heat shock proteins (HSPs) are molecular chaperones which are es
sential for cell survival. Heat shock and hypoxia markedly increase the exp
ression of several HSPs in various tissues, i.e. heart. In our in vitro stu
dy, we investigated whether HSPs are inducible in human vessels which are u
sed as coronary artery bypass grafts. Methods: We used remnants of the saph
enous vein and the internal mammary artery from 34 patients undergoing coro
nary artery bypass surgery. Each vessel was divided into segments, one for
control conditions at 37 degreesC (5% CO2-95% air), the remaining ones for
thermal (30 min at 42 degreesC) or hypoxic treatment (6 h oxygen deprivatio
n with nitrogen). The expression of Hsp60, Hsp72 and Hsp73 was investigated
by immunohistochemistry and Western-blot analysis. Results: Compared to co
ntrols, segments of the saphenous vein undergoing heat treatment showed sig
nificantly increased expression of Hsp72 in the intima (P=0.035) and Hsp73
in the media (P=0.003). In the internal mammary artery, Hsp72 and Hsp73 wer
e expressed in the intima at significantly higher levels (P=0.042 each). A
6 h oxygen deprivation with nitrogen resulted in elevated levels of Hsp60 (
media: P=0.048), of Hsp72 (intima: P<0.001 and media: P=0.003) and of Hsp73
(intima: P=0.029) in the saphenous vein. In the internal mammary artery, H
sp73 expression was significantly enhanced (intima: P=0.048 and media: P=0.
017). The results were confirmed by Western-blot analysis in representative
veins. Conclusions: These findings demonstrate the common cellular defense
mechanism of HSP expression in response to stress in coronary artery bypas
s grafts. Hypoxia and heat treatment strongly induce Hsp72 and Hsp73 expres
sion in human coronary artery bypass grafts. (C) 2001 Published by Elsevier
Science B.V.