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Department of Medicine, Division of Endocrinology and Metabolism, University of California, San Diego, La Jolla, California 92093-0618
The protective effects of heat shock proteins
(HSPs) during myocardial ischemia are now well documented, but
little is known about the mechanisms of protection and the specificity
of different HSPs. Because cytoskeletal injury plays a crucial role in
the pathogenesis of irreversible ischemic damage, we tested whether overexpression of specific HSPs protects the integrity of microtubules during simulated ischemia in rat neonatal cardiac myocytes.
Overexpression of specific HSPs was achieved by adenovirus-mediated
transgene expression. Damage was assessed by comparing control cells to cells that were subjected to a simulated ischemia protocol.
Microtubular integrity was measured by indirect immunofluorescence,
confocal microscopy, and image analysis. Within 14 h of simulated
ischemia, microtubular integrity decreased significantly in
uninfected myocytes (from 24.6 ± 1.2 to 13.2 ± 0.4) and in
myocytes infected with a control virus that expressed no transgene
(from 25.9 ± 1.8 to 13.1 ± 1.4). Microtubular integrity after
ischemia was significantly better preserved in cells
overexpressing constitutive Hsp70 (21.7 ± 1.6) or
B-crystallin (18.0 ± 2.7) but not in cells overexpressing inducible Hsp70 (11.5 ± 0.8) or Hsp27 (14.0 ± 2.2). We conclude that specific HSPs
protect the microtubules during simulated cardiac ischemia.
confocal microscopy; immunofluorescence; image analysis; cytoskeleton; tubulin
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