Binding of the Stress Protein B-crystallin to Cardiac Myofibrils Correlates with the Degree of Myocardial Damage During Ischemia/Reperfusion in vivo

Author： Golenhofen N.   Htun P.   Ness W.   Koob R.   Schaper W.   Drenckhahn D.  

Publisher： Academic Press

ISSN： 0022-2828

Source： Journal of Molecular and Cellular Cardiology, Vol.31, Iss.3, 1999-03, pp. : 569-580

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Abstract

Stress proteins are assumed to protect cells against various kinds of stresses including ischemia. In this study, we focused on the behaviour of the most abundant myocardial stress protein, B-crystallin, during ischemia and reperfusion of the pig heart in vivo . B-crystallin constitutes 1–2% of the soluble protein pool and underwent, during severe but reversibly damaging ischemia (25 min), complete translocation to the Z-line area of myofibrils. Irreversibly damaging ischemia (60 min) was accompanied by extreme stretching of the majority of myofibrils, and by concomitant extension of B-crystallin localization from the Z-line area to I-bands. This I-band shift correlated with displacement of the T12epitope of titin from the vicinity of Z-lines into I-bands, indicating that the primary binding sites for B-crystallin might also be located in juxtaposition to Z-lines and move into the I-bands during extreme sarcomeric stretching. During reperfusion after 25 min of ischemia, B-crystallin disappeared rapidly from myofibrils; whereas reperfusion after irreversibly damaging ischemia (60 min) resulted in dissociation of B-crystallin only from those myofibrils and myocardiocytes that were still able to contract, and B-crystallin remained bound to the overstretched, damaged myofibrils no longer capable of contraction. The time course of translocation of B-crystallin to myofibrils during ischemia correlated with phosphorylation of approximately 20% of the entire B-crystallin pool. However, disappearance of B-crystallin from myofibrils during reperfusion was not accompanied by dephosphorylation, indicating that phosphorylation alone does not explain myofibrillar binding of B-crystallin. Ischemia-induced myofibrillar targeting of B-crystallin probably requires additional structural and posttranslational modifications of myofibrillar components in juxtaposition to I-bands.

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