Expression of heat shock protein 27 in developing and adult human kidney

Khan, Wasil; McGuirt, Joan P.; Sens, Mary Ann; Sens, Donald A.; Todd, John H.

doi:10.1016/0378-4274(95)03613-x

Cited by 27 publications

(20 citation statements)

References 24 publications

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“…It is an evolutionary highly conserved low molecular weight protein that is phosphorylated and overexpressed in response to thermal and oxidative stress, cytokines and other mediators of inflammation (2). Since its original identification in the human breast cancer cell line MCF-7, Hsp27 has been detected in the oviduct, uterus, cervix, vagina, breast, placenta, platelets, kidney and in the epidermis and adnexal structures (3,4). In unstressed cells, Hsp27 exists predominantly as a large oligomeric unit of up to 800 kDa, usually comprising six tetrameric complexes of the protein located in the cytoplasm near the Golgi complex.…”

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confidence: 99%

Hsp27 Expression Coincides with Epidermal Stratification during Human Epidermal Morphogenesis

Monastirli¹,

Vourekas²,

Badavanis³

et al. 2005

Acta Dermato-Venereologica

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Heat shock protein 27 (Hsp27), apart from its protective function in response to stress, is implicated in the regulation of cell growth, differentiation and apoptosis. Data on the expression of Hsp27 in the developing human epidermis are sparse and partially conflicting. Thus, the purpose of the present study was to investigate Hsp27 expression during the morphogenesis of human epidermis. Skin biopsies and dispase-separated epidermal sheets obtained from 7 human embryos (7 and 8 weeks estimated gestational age, EGA), from 79 human fetuses (9-23 weeks EGA) and from 10 healthy adult volunteers were investigated by immunohistochemistry and Western blotting, respectively. The earliest detection of Hsp27 expression was found by immunohistochemistry at the 12th week EGA (basal and intermediate layer) and by Western blotting at the 9th week EGA. From the 16th to the 23rd week EGA immunoreactivity was not detectable in the basal layer, whereas in the overlying layers it revealed a differentiation-related pattern. The simultaneous onset of epidermal stratification and Hsp27 expression (9th week EGA) and the alterations of the latter in the subsequent stages of development, suggest that this stress protein may be involved in the molecular events underlying human epidermal morphogenesis.

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confidence: 99%

Hsp27 Expression Coincides with Epidermal Stratification during Human Epidermal Morphogenesis

Monastirli¹,

Vourekas²,

Badavanis³

et al. 2005

Acta Dermato-Venereologica

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“…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. RPT cells grown under SHAKE conditions tend to preserve their in vivo characteristics [20] and respond to heat stress through upregulation of HSP70.…”

Section: Discussionmentioning

confidence: 99%

“…Renal cells in vivo are susceptible to injury by a wide variety of physical and chemical agents [7, 8], possibly due to a limited capacity for mounting a cellular stress response. The purpose of this study was to characterize and define the heat stress response of renal cell culture models grown under specific conditions.…”

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%

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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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“…[8][9][10] HSP27 expression can be induced by diverse conditions, including heat shock, oxidative stress (OS) with other stress conditions in addition to nerve injury, and differentiation. 8,11,12 Khan et al showed that elevated intra-renal HSP27 levels are normally expressed in the medulla 13 a kidney region subjected to severe hypoxia 14,15 and osmotic stress 13,16 suggesting that HSP27 plays a defensive role against these two stresses. [17][18][19] Moreover, HSP27 plays an important role in actin cytoskeletal remodeling in proximal tubules 20 as well as modulation of mesangial and smooth muscle cells contractions.…”

Section: Introductionmentioning

confidence: 99%