Expression of heat shock protein 90 at the cell surface in human neuroblastoma cells

Cid, Cristina; Regidor, Ignacio; Poveda, Pedro D.; Alcázar, Alberto

doi:10.1007/s12192-008-0076-7

Cited by 24 publications

(15 citation statements)

References 19 publications

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“…The 70-kDa class of heat shock protein genes is associated with the folding and translocation of proteins across membranes and also with cell division and developmental stage progression, among various other functions . Cytosolic Hsp90, an essential and highly conserved molecular chaperone that promote cancer cell growth, differentiation, and apoptosis in humans, is also involved in the activation of many key signal transducers in fungi (Cid et al 2009;Cowen 2009;LaFayette et al 2010;Mittelman et al 2010;Shapiro et al 2009;Solit and Chiosis 2008). The amount of the hsp30 transcript induced upon heating for 2 h was greatly reduced in the palA + background at alkaline pH, an effect not Fig.…”

Section: Resultsmentioning

confidence: 99%

Transcription of the Hsp30, Hsp70, and Hsp90 heat shock protein genes is modulated by the PalA protein in response to acid pH-sensing in the fungus Aspergillus nidulans

Freitas

Silva

Leal

et al. 2011

Cell Stress and Chaperones

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Heat shock proteins are molecular chaperones linked to a myriad of physiological functions in both prokaryotes and eukaryotes. In this study, we show that the Aspergillus nidulans hsp30 (ANID_03555.1), hsp70 (ANID_05129.1), and hsp90 (ANID_08269.1) genes are preferentially expressed in an acidic milieu, whose expression is dependent on the palA + background under optimal temperature for fungal growth. Heat shock induction of these three hsp genes showed different patterns in response to extracellular pH changes in the palA + background. However, their accumulation upon heating for 2 h was almost unaffected by ambient pH changes in the palA − background. The PalA protein is a member of a conserved signaling cascade that is involved in the pH-mediated regulation of gene expression. Moreover, we identified several genes whose expression at pH 5.0 is also dependent on the palA + background. These results reveal novel aspects of the heat-and pH-sensing networks of A. nidulans.

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Section: Resultsmentioning

confidence: 99%

Transcription of the Hsp30, Hsp70, and Hsp90 heat shock protein genes is modulated by the PalA protein in response to acid pH-sensing in the fungus Aspergillus nidulans

Freitas

Silva

Leal

et al. 2011

Cell Stress and Chaperones

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“…Both CRT and HSPs are ER chaperones capable of assisting peptide loading and correct folding of MHC molecules (2,6,35,36). HSPs on the membrane surface of various types of cells (e.g., activated lymphoid cells and tumor cells) exert strong immunobiological functions (37)(38)(39)(40)(41)(42). Similar to CRT, HSP60, HSP70, HSP90, and gp96 are able to directly activate immune cells in vitro (35,36).…”

Section: Discussionmentioning

confidence: 99%

Functional Analysis of Recombinant Calreticulin Fragment 39–272: Implications for Immunobiological Activities of Calreticulin in Health and Disease

Cheng

Qiu

et al. 2010

The Journal of Immunology

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Although calreticulin (CRT) is a major Ca2+-binding luminal resident protein, it can also appear on the surface of various types of cells and it functions as an immunopotentiating molecule. However, molecular mechanisms underlying the potent immunobiological activity of cell surface CRT are still unclear. In the present study, a recombinant fragment (rCRT/39–272) covering the lectin-like N domain and partial P domain of murine CRT has been expressed in Escherichia coli. The affinity-purified rCRT/39–272 assembles into homodimers and oligomers in solution and exhibits high binding affinity to various glycans, including carrageenan, alginic acids, and hyaluronic acids. Functionally, rCRT/39–272 is capable of driving the activation and maturation of B cells and cytokine production by macrophages in a TLR-4–dependent manner in vitro. It specifically binds recombinant mouse CD14, but not BAFFR and CD40. It is also able to trigger Ig class switching by B cells in the absence of T cell help both in vitro and in vivo. Furthermore, this fragment of CRT exhibits strong adjuvanticity when conjugated to polysaccharides or expressed as part of a fusion protein. Soluble CRT can be detected in the sera of patients with rheumatoid arthritis or systemic lupus erythematosus, but not in healthy subjects. We argue that CRT, either on the membrane surface of cells or in soluble form, is a potent stimulatory molecule to B cells and macrophages via the TLR-4/CD14 pathway and plays important roles in the pathogenisis of autoimmune diseases.

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“…The mitochondria Hsp60 has been reported on the surface of human T cell-lines (54), endothelial cells (55, 56), as well as in the liver and spleen of mice (57). Hsp90 was initially detected on the cell surface of tumor cells (58) and subsequently in multipotential mesenchymal precursor cells (59), human neuroblastoma cells (60, 61), human monocytes, (62). Grp94 was observed on the plasma membrane of sarcoma cells (63).…”

Section: The Export Of Hspmentioning

confidence: 99%

Extracellular Heat Shock Proteins

Maio¹,

Vázquez

2013

Shock

151

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The expression of heat shock proteins (hsp) is a basic and well conserved cellular response to an array of stresses. These proteins are involved in the repair of cellular damage induced by the stress, which is necessary for the salutary resolution from the insult. Moreover, they confer protection from subsequent insults, which has been coined stress tolerance. Since these proteins are expressed in subcellular compartments, it was thought that their function during stress conditions was circumscribed to the intracellular environment. However, it is now well established that hsp can also be present outside cells where they appear to display a function different than the well understood chaperone role. Extracellular hsp act as alert stress signals priming other cells, particularly of the immune system, to avoid the propagation of the insult and favor resolution. Since the majority of hsp do not possess a secretory peptide signal, they are likely be exported by a non-classical secretory pathway. Different mechanisms have been proposed to explain the export of hsp, including translocation across the plasma membrane and release associated with lipid vesicles, as well as the passive release after cell death by necrosis. Extracellular hsp appear in various flavors, including membrane-bound and membrane-free forms. All of these variants of extracellular hsp suggest that their interactions with cells may be quite diverse, both in target cell types and the activation signaling pathways. This review addresses some of our current knowledge about the release and relevance of extracellular hsp.

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Expression of heat shock protein 90 at the cell surface in human neuroblastoma cells

Cited by 24 publications

References 19 publications

Transcription of the Hsp30, Hsp70, and Hsp90 heat shock protein genes is modulated by the PalA protein in response to acid pH-sensing in the fungus Aspergillus nidulans

Transcription of the Hsp30, Hsp70, and Hsp90 heat shock protein genes is modulated by the PalA protein in response to acid pH-sensing in the fungus Aspergillus nidulans

Functional Analysis of Recombinant Calreticulin Fragment 39–272: Implications for Immunobiological Activities of Calreticulin in Health and Disease

Extracellular Heat Shock Proteins

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