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*
Department of Pediatrics University of Michigan, Ann Arbor,
Michigan
Department of Medicine, Vanderbilt University, Nashville,
Tennessee
Department of Cell and Developmental Biology, University of Michigan, Ann
Arbor, Michigan
§
Max Delbrück Center for Molecular Medicine,
Berlin-Buch, Germany.
Correspondence to Dr. William E. Smoyer, Pediatric Nephrology, University of Michigan Medical Center, 8220E MSRB III, Box 0646, 1150 W. Medical Center Drive, Ann Arbor, MI 48109. Phone: 734-763-9524; Fax: 734-615-1386; E-mail: wsmoyer{at}umich.edu
B-crystallin and heat shock protein (hsp) 25 are
structurally and functionally related small stress proteins induced by a
variety of insults, including heat and ischemia. Cytoprotection by these two
hsp is thought to result from molecular chaperoning and/or cytoskeletal
stabilization. Because renal ischemia is characterized by disruption of the
renal tubular cell actin cytoskeleton, this study was conducted to determine
the localization and quantify the expression and phosphorylation of both hsp
in renal cortex, isolated glomeruli, outer medulla, and inner medulla of rats
after bilateral renal ischemia. Sham-operated kidneys had similarly small
amounts of hsp25 and
B-crystallin in cortex and glomeruli, with
substantially greater amounts of
B-crystallin versus hsp25 in
outer and inner medulla. Ischemia resulted in significantly increased hsp25
(and hsp70i) but variable
B-crystallin levels in cortex and outer
medulla, and progressively decreased glomerular hsp25 phosphorylation. In
sham-operated kidneys, hsp25 localized to glomeruli, vessels, and collecting
ducts, with
B-crystallin primarily in medullary thin limbs and
collecting ducts. After ischemia, hsp25 accumulated in proximal tubules in
cortex and outer medulla, while
B-crystallin labeling became
nonhomogeneous in outer medulla, and increased in Bowman's capsule. It is
concluded that: (1) There is striking differential expression of
hsp25 and
B-crystallin in various renal compartments; and (2)
Renal ischemia results in differential accumulation of hsp25 and
B-crystallin, with hsp25 part of a generalized stress response in renal
proximal tubular cells, which may play a role in recovery from
ischemia-induced actin filament disruption.
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