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Am J Physiol Cell Physiol 275: C711-C731, 1998;
0363-6143/98 $5.00
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Vol. 275, Issue 3, C711-C731, September 1998

Polarity, integrin, and extracellular matrix dynamics in the postischemic rat kidney

Anna Zuk1,2, Joseph V. Bonventre1,2,3, Dennis Brown1,4, and Karl S. Matlin1,2

1 Renal Unit, Massachusetts General Hospital, Charlestown 02129; Departments of 2 Medicine and 4 Pathology, Harvard Medical School, Boston 02115; and 3 Division of Health Sciences and Technology, Harvard Medical School- Massachusetts Institute of Technology, Cambridge, Massachusetts 02139

Acute renal failure (ARF) as a consequence of ischemic injury is a common disease affecting 5% of the hospitalized population. Despite the fact that mortality from ARF is high, there has been little improvement in survival rates over the last 40 years. The pathogenesis of ARF may be related to substantial changes in cell-cell and cell-extracellular matrix interactions mediated by beta 1-integrins. On the basis of in vitro and in vivo studies, reorganization of beta 1-integrins from basal to apical surfaces of injured tubular epithelia has been suggested to facilitate epithelial detachment, contributing to tubular obstruction and backleak of glomerular filtrate. In this study, we examine integrin and extracellular matrix dynamics during epithelial injury and repair using an in vivo rat model of unilateral ischemia. We find that, soon after reperfusion, beta 1-integrins newly appear on lateral borders in epithelial cells of the S3 segment but are not on the apical surface. At later times, as further injury and regeneration coordinately occur, epithelia adherent to the basement membrane localize beta 1 predominantly to basal surfaces even while the polarity of other marker proteins is lost. At the same time, amorphous material consisting of depolarized exfoliated cells fills the luminal space. Notably, beta 1-integrins are not detected on exfoliated cells. A novel finding is the presence of fibronectin, a glycoprotein of plasma and the renal interstitium, in tubular spaces of the distal nephron and to a lesser extent S3 segments. These results indicate that beta 1-integrins dramatically change their distribution during ischemic injury and epithelial repair, possibly contributing to cell exfoliation initially and to epithelial regeneration at later stages. Together with the appearance of large amounts of fibronectin in tubular lumens, these alterations may play a significant role in the pathophysiology of ARF.

beta 1-integrin; epithelial polarity; fibronectin; acute renal failure


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