Heat Shock Protein 72/73 in Normal and Diseased Kidneys

Venkataseshan, V S; Marquet, E

doi:10.1159/000189108

Cited by 19 publications

(6 citation statements)

References 15 publications

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“…Increased HSP expression is found in patients with various forms of nephritis including minimal change glomerulonephritis, FSGS, membranous nephropathy, and acute interstitial nephritis in the loci of acute interstitial infiltration (Venkataseshan and Marquet 1996). Marzec et al (2009) revealed the decreased HSP72 expression on the surface of peripheral blood monocytes of patients with CKD as compared with the control.…”

Section: Role Of Hsp70 and Hsp60 In The T Cell Regulation Of Chronic mentioning

confidence: 95%

“…In kidneys with the puromycin aminonucleoside induced nephrosis, HSP73 accumulates in the cytoplasm at a level higher than in the nucleus in association with the severity of renal dysfunction and proteinuria (Komatsuda et al 1992). Somewhat different localization of HSP70 expression in normal human kidney was demonstrated by Venkataseshan and Marquet (1996) and Dinda et al (1998). HSP73/72 showed a uniform fine granular cytoplasmic staining of visceral glomerular epithelial cells and epithelia of distal convoluted tubules and collecting ducts without localization in proximal tubules.…”

Section: Hsp73 In Normal Renal Tissuementioning

confidence: 99%

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Heat shock proteins and kidney disease: perspectives of HSP therapy

Chebotareva

Bobkova

Shilov

2017

Cell Stress and Chaperones

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Heat shock proteins (HSPs) mediate a diverse range of cellular functions, prominently including folding and regulatory processes of cellular repair. A major property of these remarkable proteins, dependent on intracellular or extracellular location, is their capacity for immunoregulation that optimizes immune activity while avoiding hyperactivated inflammation. In this review, recent investigations are described, which examine roles of HSPs in protection of kidney tissue from various traumatic influences and demonstrate their potential for clinical management of nephritic disease. The HSP70 class is particularly attractive in this respect due to its multiple protective effects. The review also summarizes current understanding of HSP bioactivity in the pathophysiology of various kidney diseases, including acute kidney injury, diabetic nephropathy, chronic glomerulonephritis, and lupus nephritis-along with other promising strategies for their remediation, such as DNA vaccination.

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Section: Role Of Hsp70 and Hsp60 In The T Cell Regulation Of Chronic mentioning

confidence: 95%

Section: Hsp73 In Normal Renal Tissuementioning

confidence: 99%

Heat shock proteins and kidney disease: perspectives of HSP therapy

Chebotareva

Bobkova

Shilov

2017

Cell Stress and Chaperones

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“…Recent studies suggested that HSP 72/73 expression of renal tubular epithelial cells may be induced not only by focal inflammatory alterations of the cellular environment but also by systemic influences, such as hemodialysis [44, 45]. Particularly during CAPD, repeated exposure to dialysis solutions probably also modulate mesothelial HSP expression.…”

Section: Discussionmentioning

confidence: 99%

Expression of Heat Shock Proteins 72/73 in Human Peritoneal Mesothelial Cells in vivo and in vitro

Lopez-Cotarelo¹,

Sellhaus²,

Baba³

et al. 2000

Nephron

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Leukocyte accumulation during peritonitis leads to an injurious microenvironment which is involved in the host defense reaction but is also thought to cause peritoneal damage. We tested the hypothesis that mesothelial cells (MC) respond to the injurious microenvironment during peritonitis by an increased expression of heat shock proteins (HSP 72/73), a basic way by which cells are protected against injury. Comparison of resting MC and activated MC during peritonitis in vivo by means of immunohistochemistry revealed an increased expression of HSP 72/73. As assessed by Western immunoblotting, incubation of MC in vitro with tumor necrosis factor-α (TNF-α) and interleukin-1β (IL-1β) caused a time-dependent induction of HSP 72/73 expression, which was maximal 6 h after stimulation. We suggest that the increased HSP 72/ 73 expression of MC during peritonitis is in part induced by TNF-α and IL-1β and may exert a cell-protective function, lessening MC damage during peritonitis.

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“…A number of published reports show that HSPs can be elevated in kidneys in vivo, particularly as a result of disease or injury [9, 10, 11, 12, 13]. However, deficient cytoprotection by HSP70 [7] or low HSP levels in kidney relative to other organs [8, 14] could explain the marked sensitivity of RPT cells to various modes of injury.…”

Section: Discussionmentioning

confidence: 99%

“…This stress response is tissue-dependent and may be attenuated, or absent, in some cell types that exhibit a high sensitivity to a variety of stress conditions [3, 4, 5, 6]. In particular, susceptibility of renal proximal tubule (RPT) cells to various toxic agents could be related to a limited capacity for mounting a cellular stress response [7, 8], although the expression of certain HSPs is elevated in numerous renal disease states [9, 10, 11, 12, 13]. Constitutive HSP levels in kidney, however, may be quite low and with the possible exception of HSP70 may be significantly lower than those in liver, for example [14].…”

Section: Introductionmentioning

confidence: 99%

Stress Response in a Leporine Renal Cell Model

Henle

Jethmalani

Nolen

et al. 1997

Nephron

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It is well established that renal proximal tubule (RPT) cells grown under standard in vitro conditions attenuate many of their in vivo properties and functions. Thus, the study of renal stress response mechanisms requires an appropriate cell culture model. In the present study, we compared the heat stress (10 min, 45°C) response of freshly isolated RPT cells with that of RPT cells grown in vitro for 6 days under two different culture conditions: (1) SHAKE conditions, where oxygen levels and physiological functions are maintained via continuous media motion [Nowak G, Schnellmann RG: Am J Physiol 1996;271:C2072–2080] and (2) STILL conditions, involving standard cell culture which leads to partial hypoxia and a marked reduction in physiological functions. The freshly isolated RPT cells progressively synthesized heat shock proteins (HSPs) and stress glycoproteins (SGs) during a 3-hour culture period in vitro. Under these conditions, heat stress did not further increase HSP and SG synthesis. In RPT cells grown under SHAKE conditions, HSP70 synthesis was detected 1 h after heat stress and decreased below detection by 3 h. In contrast, the uptake of radiolabeled mannose into (glycoprotein) GP62 (M_r 62,000), GP50, and GP38 was observed in control SHAKE cultures and was not further increased after heat stress. These results are consistent with immunohistochemistry studies, where similar changes in HSP70 and GP50 expression were noted. RPT cells grown under STILL conditions showed both increased synthesis of HSP70 and increased glycosylation of GP62, GP50, and GP38 as early as 1 h after heat stress, but in contrast to SHAKE conditions, this heat-induced stress response further intensified at 3 h after heat stress. By 7 h after heating, HSP synthesis returned to control levels, while glycosylation of GP62 and GP50 remained elevated. Based on our results, we conclude that freshly isolated RPT cells exhibit a stress response that may be caused by acute cell isolation/culture stress. While this stress response unfolds, freshly isolated RPT cells appear unable to respond to additional heat stress. RPT cells grown under SHAKE and STILL conditions exhibit high rates of SG glycosylation, especially that of GP62, possibly reflecting a ‘stress’ condition associated with growth on plastic substrate. Concurrently, RPT cells from STILL cultures show a higher capacity for responding to acute heat stress than SHAKE cultures, evidenced by the transiently increased HSP synthetic rates. The interpretation of the renal stress response capacity, therefore, must be linked to a specific culture condition.

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Heat Shock Protein 72/73 in Normal and Diseased Kidneys

Cited by 19 publications

References 15 publications

Heat shock proteins and kidney disease: perspectives of HSP therapy

Heat shock proteins and kidney disease: perspectives of HSP therapy

Expression of Heat Shock Proteins 72/73 in Human Peritoneal Mesothelial Cells in vivo and in vitro

Stress Response in a Leporine Renal Cell Model

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