Induction and intracellular localization of HSP-72 after renal ischemia

Why, Scott K. Van; Hildebrandt, Friedhelm; Ardito, Thomas; Mann, A. S.; Siegel, Norman J.; Kashgarian, Michael

doi:10.1152/ajprenal.1992.263.5.f769

Cited by 59 publications

(62 citation statements)

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“…An increasing body of indirect evidence suggests that interaction between HSP72 and NKA occurs in both in vitro and in vivo renal ischemic injury. Van Why et al (19) detected a similar localization and granulation pattern between HSP72 and the NKA ␣ 1 -subunit in postischemic kidneys. Ischemic preconditioning with HSP72 overexpression prevented NKA ␣ 1 -subunit dissociation after repeated ischemic insult (1).…”

Section: Discussionmentioning

confidence: 80%

Sex differences in heat shock protein 72 expression and localization in rats following renal ischemia-reperfusion injury

Fekete¹,

Vannay²,

Vér³

et al. 2006

American Journal of Physiology-Renal Physiology

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Fekete, Andrea, Á dám Vannay, Á gota Vér, Krisztina Rusai, Veronika Mü ller, György Reusz, Tivadar Tulassay, and Attila J. Szabó. Sex differences in heat shock protein 72 expression and localization in rats following renal ischemia-reperfusion injury. Am J Physiol Renal Physiol 291: F806 -F811, 2006. First published April 11, 2006 doi:10.1152/ajprenal.00080.2006.-Previously, we demonstrated gender differences in Na-K-ATPase (NKA) expression and function after renal ischemia-reperfusion (I/R) injury (Sex differences in the alterations of Na ϩ , K ϩ -ATPase following ischemia-reperfusion injury in the rat kidney. J Physiol 555: [471][472][473][474][475][476][477][478][479][480] 2004). Postischemic membrane destruction causes inhibition of NKA, whereas heat shock protein (HSP) 72 helps to preserve it. We tested the sex differences in postischemic expression of HSP72 and colocalization with NKA. The left renal pedicle of uninephrectomized female (F) and male (M) Wistar rats was clamped for 55 min followed by 2 (T2), 16 (T16), and 24 h (T24) of reperfusion. Uninephrectomized, sham-operated F and M rats served as controls. Postischemic blood urea nitrogen (BUN), serum creatinine, and renal histology were analyzed. HSP72 mRNA expression was detected by RT-PCR, protein levels by Western blot analysis. Fluorescent immunohistochemistry was performed to evaluate the localization of HSP72 and NKA ␣ 1-subunit. Postischemic BUN and creatinine were higher, and renal histology showed more rapid progression in M vs. F (P Ͻ 0.05). HSP72 mRNA expression was higher in F vs. M in control and in all I/R groups (P Ͻ 0.05). Similar changes were observed in HSP72 protein levels (F vs. M, P Ͻ 0.05, control, T2, T16, T24, respectively). Immunohistochemical localization of HSP72 and NKA ␣ 1 was similar in control F and M. In postischemic F kidneys, the majority of NKA ␣ 1 and HSP72 was colocalized on the basolateral membrane of tubular cells, whereas in M prominent staining was observed in the cytosol and apical domain. This study indicates that in female kidneys the higher basal and postischemic levels of HSP72 and different colocalization with NKA might contribute to the gender differences in renal I/R injury.

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Section: Discussionmentioning

confidence: 80%

Sex differences in heat shock protein 72 expression and localization in rats following renal ischemia-reperfusion injury

Fekete¹,

Vannay²,

Vér³

et al. 2006

American Journal of Physiology-Renal Physiology

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“…Vicencio et al (8) have demonstrated a temporal correlation between a peak of HSP72 protein expression and a consequent protection of immature animals against hypoxic renal injury. In experimental ARF, renal ischemia has been shown to induce HSP72 synthesis during recovery of the proximal tubular cells (15), and low levels of HSP72 have been considered as detrimental for renal recovery (16,17).…”

Section: Discussionmentioning

confidence: 99%

Association between Heat Shock Protein 72 Gene Polymorphism and Acute Renal Failure in Premature Neonates

et al. 2003

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Heat shock protein (HSP)70 plays an important role in the ischemic tolerance of fetal and neonatal kidney. We have investigated the association of genetic polymorphisms of the constitutive HSP70 (HSP73) and the inducible HSP70 (HSP72) encoding genes with the risk of acute renal failure (ARF) in very low birth weight (VLBW) neonates. Thirty-seven VLBW neonates with ARF and 93 VLBW neonates without ARF were enrolled in the study. The presence of HSP72 (1267)AG and HSP73 (190)GC polymorphism was analyzed from dried blood samples by PCR and restriction length fragment polymorphism. Allelic prevalence was related to reference values obtained in 131 healthy adults. Stepwise binary logistic regression was applied to determine the independent effect of the established risk factors to the development of ARF. Sixteen of 37 VLBW neonates with ARF and 18 of 93 VLBW neonates without ARF were homozygous for HSP72 (1267)G allele (p Յ 0.01). The association between HSP72 (1267)GG genotype and ARF remained at the level of significance (p ϭ 0.05) when it was adjusted for established risk factors of neonatal ARF. Prevalence of HSP72 (1267)GG was also higher in VLBW neonates than in the reference population (p Ͻ 0.05) and in VLBW neonates with infant respiratory distress syndrome than in those without (p Ͻ 0.001). We found that in VLBW neonates carrying HSP72 (1267)GG genetic variation, which is associated with low inducibility of HSP72, the risk of ARF was increased. Therefore, VLBW neonates with (1267)GG might express less HSP72 and might be less protected against ARF. ARF is a severe complication of immaturity, affecting up to 40% of VLBW neonates born with a birth weight Ͻ1500 g (1). Despite evident progression in clinical therapy, ARF still remains a leading risk factor of perinatal morbidity (2). Pathologic conditions that are associated with disturbed renal hemodynamics (e.g. fetal distress, sepsis, cardiac failure, NEC, and IRDS) all predispose to ARF in preterm neonates (3).HSPs, particularly the HSP70 family, are ideal candidates for cytoprotective substances against ARF. They act by refolding of disrupted proteins, thereby limiting tubular injury, restoring renal function and accelerating renal recovery (4). HSP70 family includes HSP73, which is expressed constitutively, whereas HSP72 is inducible by various cell stressors, such as hyperthermia, hypoxia, inflammation, and toxic agents (5). The significance of adequate HSP72 production has been extensively investigated in renal pathology of the fetus and neonate in animal models (6). Immature rat kidneys were previously demonstrated to exhibit a rapid HSP72 expression after heat stress and anoxia (7). Recent studies described that tolerance to renal ischemia of the neonatal rat kidney was associated with increased expression of HSP72 (8).Besides environmental factors, genetic polymorphisms were also suggested to influence the production of HSP70s. Decreased HSP72 expression was measured in homozygous carriers of G variants at the 1267 site of the coding region of

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“…The functional significance of this upregulation, however, remains unknown. Interestingly, the endogenous cellular injury signals that can activate TLR2, such as heat shock proteins (6), and the contents of necrotic cells (7) are known to accumulate upon renal ischemic tissue injury (8,9).…”

Section: Introductionmentioning

confidence: 99%

Renal-associated TLR2 mediates ischemia/reperfusion injury in the kidney

Leemans¹,

Stokman²,

Claessen³

et al. 2005

J. Clin. Invest.

508

465

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TLRs are conserved pattern recognition receptors that detect motifs of pathogens and host material released during injury. For unknown reasons, renal TLR2 mRNA is mainly expressed by tubular cells and is enhanced upon renal ischemia/reperfusion (I/R) injury. We evaluated the role of TLR2 in I/R injury using TLR2 -/-and TLR2 +/+ mice, TLR2 antisense oligonucleotides, and chimeric mice deficient in leukocyte or renal TLR2. Tubular cells needed TLR2 to produce significant cytokine and chemokine amounts upon ischemia in vitro. TLR2 played a proinflammatory and detrimental role in vivo after I/R injury, as reflected by a reduction in the amount of local cytokines and chemokines, leukocytes, and the level of renal injury and dysfunction in TLR2 -/-mice compared with controls. Analysis of chimeric mice suggested that TLR2 expressed on renal parenchyma plays a crucial role in the induction of inflammation and injury. TLR2-antisense treatment protected mice from renal dysfunction, neutrophil influx, and tubular apoptosis after I/R injury compared with nonsense treatment. In summary, we identified renal-associated TLR2 as an important initiator of inflammatory responses leading to renal injury and dysfunction in I/R injury. These data imply that TLR2 blockade could provide a basis for therapeutic strategies to treat or prevent renal ischemic injury.

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Induction and intracellular localization of HSP-72 after renal ischemia

Cited by 59 publications

References 0 publications

Sex differences in heat shock protein 72 expression and localization in rats following renal ischemia-reperfusion injury

Sex differences in heat shock protein 72 expression and localization in rats following renal ischemia-reperfusion injury

Association between Heat Shock Protein 72 Gene Polymorphism and Acute Renal Failure in Premature Neonates

Renal-associated TLR2 mediates ischemia/reperfusion injury in the kidney

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