Effect of water diuresis and water restriction on expression of HSPs-27, -60 and -70 in rat kidney

Medina, Ruth; Cantley, Lewis C.; Spokes, Katherine; Epstein, Franklin H.

doi:10.1038/ki.1996.427

Cited by 23 publications

(25 citation statements)

References 13 publications

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“…For HSP25, one study of human breast cancer cells (MCF-7) has reported that HSP25 protein can be enhanced by hyperosmolality [16]. Consistent with this finding is the in vivo observation that transcription of HSP25 mRNA in the renal papilla is enhanced [27] during short-term water restriction. However, no data are available for the change of HSP25 protein content under these in vivo conditions.…”

Section: Introductionsupporting

confidence: 50%

“…In our investigations HSP60 was unaffected by the different experimental protocols. Medina et al [27] have observed a slight increase of HSP60 mRNA in rats after 2 days of water restriction. This suggests that HSP60 may participate in the early response to acute osmolar changes, possibly by supporting the enhanced energy supply of medullary cells during adaptive processes.…”

Section: Discussionmentioning

confidence: 98%

“…To gain further insight into the role of HSPs in vivo several investigators have studied the effect of changing medullary osmolality on the expression of HSPs. With respect to HSP72, the literature is inconsistent, with reports of HSP72 being completely unaffected by diuresis or antidiuresis [26,27], but also of induction of HSP72 mRNA and protein [10,42]. For HSP25, one study of human breast cancer cells (MCF-7) has reported that HSP25 protein can be enhanced by hyperosmolality [16].…”

Section: Introductionmentioning

confidence: 96%

“…The cells of the renal medulla, which are exposed to wide variations in extracellular osmolality, respond to increasing extracellular solute concentrations by accumulating organic osmolytes, which are able to compensate these adverse effects [2,11]. In addition to organic osmolytes, recent investigations suggest that heat shock proteins (HSPs) participate in this adaptive response [10,27,29,31]. Under physiological conditions these ubiquitously detectable proteins are considered to function as molecular chaperones in that they transiently bind other proteins and facilitate their folding or intracellular trafficking [12,13].…”

Section: Introductionmentioning

confidence: 99%

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Effects of long-term changes in medullary osmolality on heat shock proteins HSp25, hsp60, HSP72 and HSP73 in the rat kidney

Müller

Neuhofer

Burger‐Kentischer

et al. 1998

Pfl�gers Archiv European Journal of Physiology

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The influence of diuresis and antidiuresis on the expression of heat shock proteins (HSP) 25, 60, 72 and 73 in the renal cortex and outer and inner medulla of Wistar rats was analysed. Medullary osmolality was reduced by long-term diuresis (3% sucrose in the drinking water for 3 weeks) and subsequently enhanced by transition to a concentrating state by giving normal drinking water again in combination with deamino-D-arginine vasopressin (dDAVP) for 5 days. Western blot analyses revealed that neither HSP73 nor HSP60 was influenced by any treatment. The HSP72 level in the medulla was markedly reduced (50%) when osmolality was lowered and increased when tonicity was high. RNAse protection assays showed that the effects on HSP72 are parallelled in general by changes in HSP72 mRNA. While levels of HSP25 were not influenced, isoelectric focusing revealed that the degree of phosphorylation of outer and inner medullary HSP25 increased following both treatments. It thus seems that HSP73 and HSP60 are not directly involved in the long-term adaptation to varying medullary osmolalities. The correlation between changes in osmolality and amounts of the major stress-inducible HSP72 in the medulla implies that medullary hypertonicity is stressful for kidney cells. Furthermore, adaptation to pronounced changes in the osmolality of the environment most likely involves phosphorylation of HSP25.

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Section: Introductionsupporting

confidence: 50%

Section: Discussionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Effects of long-term changes in medullary osmolality on heat shock proteins HSp25, hsp60, HSP72 and HSP73 in the rat kidney

Müller

Neuhofer

Burger‐Kentischer

et al. 1998

Pfl�gers Archiv European Journal of Physiology

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“…This distribution pattern, however, is not observed for other members of the HSP family, such as the constitutively expressed HSP73 (also termed HSC70) and HSP60 [11,13]. In addition, the expression of HSP25 mRNA [14], HSP72 [8,13], and OSP94 mRNA [10] changes appropriately with the diuretic state.…”

mentioning

confidence: 99%

Heat Shock Proteins and the Cellular Response to Osmotic Stress

Beck

Grünbein

Lugmayr

et al. 2000

Cell Physiol Biochem

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In antidiuresis, the intrarenal distribution of HSP25/27, αB-crystallin, HSP72, OSP94 and HSP110 corresponds to the osmotic gradient between cortex and papilla: low amounts in the cortex and high values in the inner medulla and papilla. In addition, medullary HSP72 levels change appropriately with the diuretic state. Studies on MDCK cells suggest that, in the renal medulla in vivo, stressors, such as NaCl and low pH, may act in concert to induce HSP72 expression. Urea, added to the medium at high concentrations (600 mM), causes the majority of MDCK cells to die. Prior exposure of these cells to hypertonic media (NaCl addition), a maneuver that induces HSP72, protects the cells against the deleterious effects of high urea concentrations. Inhibition of HSP72 expression by stable antisense transfection or SB203580 treatment abolishes the beneficial effects of prior hypertonic stress. Conversely, overexpression of HSP72 under isotonic conditions by a dexamethasone-driven vector confers substantial resistance against subsequent exposure to high urea concentrations. Taken together these results suggest that also in the renal inner medulla, NaCl-induced enhancement of HSP72 expression may help counteract the detrimental effects of high urea concentrations.

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