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B-crystallin to Z lines of myocardium
1 Institute of Anatomy,
It is becoming clear that stress proteins play
a role in various aspects of postischemic myocardial recovery and that
the cytoskeleton of cardiac myocytes is an important determinant for cellular survival during ischemia and energy depletion. In the present study, we addressed the question of whether the
cytoskeleton-binding stress protein 
B-crystallin may be involved in
early cellular responses of rat and porcine myocardium to
ischemia. Immunostaining and subcellular fractionation revealed
a rapid ischemia-induced redistribution of B-crystallin from
a cytosolic pool to intercalated disks and Z lines of the myofibrils.
This striking translocation of B-crystallin from the cytosol to
sites of the myofibrillar system that are known to be sensitive to
ischemiareperfusion injury was accompanied by a rapid shift
of a fraction of B-crystallin to a more acidic isoelectric point.
This shift is caused by B-crystallin phosphorylation, as identified
by its augmentation in the presence of phosphatase inhibitors
(vanadate, fluoride) and comigration of the acidic B-crystallin form
with the phosphorylated B1 form of
lenticular B-crystallin. In view of the chaperone-like function of
B-crystallin in conjunction with its high level of constitutive expression in the myocardium (1-2% of soluble protein content), we consider B-crystallin an excellent candidate to play a role in
early aspects of the protection of the myocardial contractile apparatus
against ischemia-reperfusion injury.
cardiomyocyte; myofibril; cytoskeleton; heat shock protein
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