Extracellular Heat Shock Proteins in Cell Signaling and Immunity

Calderwood, Stuart K.; Mambula, Salamatu S.; Gray, Phillip J.

doi:10.1196/annals.1391.019

Cited by 205 publications

(188 citation statements)

References 66 publications

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“…Hsp60, including probably the mitochondrial Cpn60, can be elevated in a number of human tumors (Czarnecka et al, 2006;Cappello et al, 2007;2008) and in the extracellular milieu, which can cause activation of an antitumor immune response (Calderwood et al, 2007). Whether and when mitochondrial and cytosolic Hsp60 have pro-or anti-apoptotic roles is still unclear, since there is evidence supporting both possibilities (Samali et al, 1999;Xanthoudakis et al, 1999;Gupta et al, 2005;Veereshwarayya et al, 2006;Chandra et al, 2007).…”

confidence: 99%

Upon oxidative stress, the antiapoptotic Hsp60/procaspase-3 complex persists in mucoepidermoid carcinoma cells

Campanella¹,

Bucchieri²,

Ardizzone³

et al. 2009

Eur J Histochem

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Hsp60, a mitochondrial chaperonin highly conserved during evolution, has been found elevated in the cytosol of cancer cells, both in vivo and in vitro, but its role in determining apoptosis during oxidative stress (OS) has not yet been fully elucidated. The aim of the present work was to study the effects of OS on Hsp60 levels and its interactions with procaspase- 3 (p-C3) and p53 in tumor cells. NCI-H292 (mucoepidermoid carcinoma) cells were exposed to various concentrations of hydrogen peroxide (H2O2) for 24 hours. Cell viability was determined by Trypan blue and MTT assays. DNA damage was assessed by the Comet assay, and apoptosis was measured by the AnnexinV cytofluorimetric test. Exposure to increasing concentrations of H2O2 resulted in a reduction of cell viability, DNA damage, and early apoptotic phenomena. Hsp60, p-C3, p53, and p21 were assessed by Western blotting and immunocytochemistry before and after OS. Hsp60 and p-C3 were present before and after OS induction. Immunoprecipitation experiments showed an Hsp60/p-C3 complex before OS that persisted after it, while an Hsp60/p53 complex was not detected in either condition. The presence of wild type (wt) p53 was confirmed by RT-PCR, and p21 detection suggested p53 activation after OS. We postulate that, although OS may induce early apoptosis in NCI-H292 cells, Hsp60 exerts an anti-apoptotic effect in these cells and, by extension, it may do so in other cancer cells

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confidence: 99%

Upon oxidative stress, the antiapoptotic Hsp60/procaspase-3 complex persists in mucoepidermoid carcinoma cells

Campanella¹,

Bucchieri²,

Ardizzone³

et al. 2009

Eur J Histochem

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“…[1,2] A growing body of evidence has expanded the role of HSP, which have been regarded as intracellular chaperones beyond their cytoprotective function. The main goal of the chaperones discussed extensively in the recent reviews [3,4] is to preserve cell survival by controlling the three -dimensional structure of the synthesized proteins, preventing misfolding or degradation. Therefore, HSP regulates the response to any detrimental factors such as temperature, radiation, hypoxia, toxins or infectious agents.…”

Section: Introductionmentioning

confidence: 99%

The role of heat shock proteins in kidney disease

Rao

2016

Journal of Translational Internal Medicine

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Heat Shock Proteins (HSP) belong to the family of intracellular proteins that are constitutively expressed and are upregulated by various stressors including heat, oxidative and chemical stress. HSP helps in reparative processes, including the refolding of damaged proteins and the removal of irreparably damaged proteins that would initiate cellular death or apoptosis. A growing body of evidence has expanded the role of HSP and defined their role in diseases such as neurodegenerative disorders, cancer, ischemic heart disease and kidney diseases. The protective role of HSP in ischemic renal injury has been described and HSP impairment has been noted in other forms of kidney injuries including post-transplant situation. Further research into the role of HSP in prevention of kidney injury is crucial if translation from the laboratory to patient bedside has to occur. This article aims to be a review of heat shock protein, and its relevance to kidney diseases.

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“…15 At molecular level, plants tackle heat stress through the action of a set of molecular chaperones known as HSPs, which are emerging extracellular mediators in cell signaling in response to stress. 16 Therefore, it is also plausible to hypothesize that the HSPs secreted by the stigma may modulate temperaturedependent reproductive events in this tissue.…”

Section: The Plant Stigma Exudatementioning

confidence: 99%

The plant stigma exudate

Rejón

Delalande

Schaeffer-Reiss

et al. 2014

Plant Signaling & Behavior

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D uring sexual reproduction, pollenperformance is greatly influenced by the female tissues. The stigma exudate, i.e., the extracellular secretion that covers the stigma outermost surface, has been usually regarded as a reservoir of water, secondary metabolites, cell wall precursors and compounds that serve as energy supply for rapid pollen tube growth. In an attempt to identify the proteins present in the stigma secretome, we performed a large-scale analysis in two species (Lilium longiflorum and Olea europaea) following a proteomicbased approach. The resulting data strongly suggest that the stigma exudate is not a mere storage site but also a biochemically active environment with a markedly catabolic nature. Thus, this secretion may modulate early pollen tube growth and contribute to the senescence of stigma after pollination. In addition, a putative cross-talk between genetic programs that regulate stress/defense and pollination responses in the stigma is also suggested. The stigma exudate might also functionally diverge between species on the basis on their ecology and the biochemical, morphological and anatomical features of their stigmas. Unexpectedly, we identified in both exudates some intracellular proteins, suggesting that a mechanism other than the canonical ER-Golgi exocytic pathway may exist in the stigma and contribute to exudate secretion.During sexual reproduction, pollen performance is greatly influenced by the biochemical, morphological and anatomical features of the female counterpart (i.e., the pistil). In some plants, the stigma outermost surface is coated by a secretion that is released by specialized cells called papillae. This extracellular fluid, the so-called stigma exudate, mostly contains water, sugars, lipids and proteins, 1 but other compounds such as phenols, amino acids, ROS/ RNS and Ca 2+ ions are also present in measurable amounts. [2][3][4][5] The picture of the stigma secretome remains fragmentary and only a few proteins have been identified and characterized so far. [6][7][8] In a recent publication, we performed a largescale protein profiling study of the stigma exudate in two plant species, namely Eastern lily (Lilium longiflorum) and olive (Olea europaea), that substantially differ in their taxonomical position, pistil morphology and anatomy, ecology and cultivation purposes. 9 Following a proteomic-based strategy, we identified 51 and 57 unique proteins in lily and olive, respectively, most of which are first described in this secretion. The resulting data shows that the complexity of the stigma exudate, in terms of protein diversity, is higher than initially expected. 10 Under a functional perspective, this secretion has often been regarded as a mere source of water for pollen hydration, and storage compounds for sustaining

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Extracellular Heat Shock Proteins in Cell Signaling and Immunity

Cited by 205 publications

References 66 publications

Upon oxidative stress, the antiapoptotic Hsp60/procaspase-3 complex persists in mucoepidermoid carcinoma cells

Upon oxidative stress, the antiapoptotic Hsp60/procaspase-3 complex persists in mucoepidermoid carcinoma cells

The role of heat shock proteins in kidney disease

The plant stigma exudate

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