Article

Expression of Hsp72 protein in chronic kidney disease patients.

Departments of Nephrology, Transplantology and Internal Medicine.
Scandinavian Journal of Urology and Nephrology (Impact Factor: 1.01). 06/2009; DOI: 10.1080/00365590903089489
Source: PubMed

ABSTRACT Objective. Expression of heat shock protein (Hsp) 72 is one of the major mechanisms acting against cellular injury. It displays a plethora of functions, including a considerable impact on inflammation. The aim of this study was to investigate Hsp72 expression in blood monocytes of patients with chronic kidney disease (CKD). Material and methods. Hsp72 protein level was assessed by flow cytometry in blood monocytes of predialysis, haemodialysis (HD) and continuous peritoneal dialysis patients, and controls. It was followed by evaluation of Hsp72 gene expression in the same cohorts by reverse transcription-polymerase chain reaction. Results. The level of Hsp72 protein was significantly lower in the predialysis (359+/-83 AU) and HD groups (293+/-62 AU) than in controls (405+/-51 AU) (p<0.01 and p<0.001, respectively). The amount of mRNA was significantly lower only in the HD group, compared with controls (0.39+/-0.10 vs 0.48+/-0.10, p<0.01). In the predialysis group, there were negative correlations between Hsp72 protein level and serum creatinine concentration, blood urea nitrogen and C-reactive protein. Conclusions. This study demonstrates that uraemic toxicity decreases expression of Hsp72. Attenuation of Hsp 72 expression in uraemia, found in the present study, could contribute to the inflammatory state, a common complication in CKD patients.

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    ABSTRACT: The classic heat shock (stress) response (HSR) was originally attributed to protein denaturation. However, heat shock protein (Hsp) induction occurs in many circumstances where no protein denaturation is observed. Recently considerable evidence has been accumulated to the favour of the "Membrane Sensor Hypothesis" which predicts that the level of Hsps can be changed as a result of alterations to the plasma membrane. This is especially pertinent to mild heat shock, such as occurs in fever. In this condition the sensitivity of many transient receptor potential (TRP) channels is particularly notable. Small temperature stresses can modulate TRP gating significantly and this is influenced by lipids. In addition, stress hormones often modify plasma membrane structure and function and thus initiate a cascade of events, which may affect HSR. The major transactivator heat shock factor-1 integrates the signals originating from the plasma membrane and orchestrates the expression of individual heat shock genes. We describe how these observations can be tested at the molecular level, for example, with the use of membrane perturbers and through computational calculations. An important fact which now starts to be addressed is that membranes are not homogeneous nor do all cells react identically. Lipidomics and cell profiling are beginning to address the above two points. Finally, we observe that a deregulated HSR is found in a large number of important diseases where more detailed knowledge of the molecular mechanisms involved may offer timely opportunities for clinical interventions and new, innovative drug treatments. This article is part of a Special Issue entitled: Membrane structure and function: Relevance in the cell's physiology, pathology and therapy. This article is part of a Special Issue entitled: Membrane structure and function: Relevance in the cell's physiology, pathology and therapy.
    Biochimica et Biophysica Acta 12/2013; · 4.66 Impact Factor

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May 26, 2014