Heat‐Shock Proteins

@article{Li2004HeatShockP,
  title={Heat‐Shock Proteins},
  author={Zihai Li and P. Srivastava},
  journal={Current Protocols in Immunology},
  year={2004},
  volume={58}
}
Heat‐shock proteins (HSPs), or stress proteins, are highly conserved and present in all organisms and in all cells of all organisms. Selected HSPs, also known as chaperones, play crucial roles in folding/unfolding of proteins, assembly of multiprotein complexes, transport/sorting of proteins into correct subcellular compartments, cell‐cycle control and signaling, and protection of cells against stress/apoptosis. More recently, HSPs have been implicated in antigen presentation with the role of… Expand
Dynamics of Heat Shock Proteins in Immunity and Aging
TLDR
This chapter discusses on the existing scientific data about HSP with an effort to highlight the possible future implication of HSP during stress, aging, apoptosis and their status at post-translational and mitochondrial level and the possible drug targets for improving prognosis and treatment of various diseases. Expand
Unfolding the Role of Large Heat Shock Proteins: New Insights and Therapeutic Implications
TLDR
The current advances in understanding these large HSPs as molecular chaperones in proteostasis control and immune modulation as well as their therapeutic implications in treatment of cancer and neurodegeneration are reviewed. Expand
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Activation of natural killer cells by heat shock protein 70
  • G. Multhoff
  • Medicine
  • International journal of hyperthermia : the official journal of European Society for Hyperthermic Oncology, North American Hyperthermia Group
  • 2002
TLDR
In this review, an unusual tumor-selective membrane-localization of non-conserved regions of the 72000Da HSP (Hsp70) has been found to act as a recognition structure for natural killer (NK) cells. Expand
Role of Heat-Shock Proteins in Cellular Function and in the Biology of Fungi
TLDR
Role of Hsps in fungi during morphogenesis and various stress conditions (temperature, pH, and osmotic pressure) and in antifungal drug tolerance is focused on. Expand
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TLDR
The functional involvement of cytosolic and endoplasmic reticulum (ER) HSPs/chaperones in plant immunity is discussed to obtain an integrated understanding of the immune responses in plant cells. Expand
C-terminal modulators of heat shock protein of 90 kDa (HSP90): State of development and modes of action.
TLDR
The current development state of characteristic C-terminal inhibitors is summarized, with an emphasis on their (proposed) molecular modes of action and binding sites. Expand
Heat-Shock Proteins in Neuroinflammation
TLDR
The role of neuroinflammation in acute and chronic pathological conditions affecting the brain is summarized and the existing literature on HSP-mediated inflammatory function within the central nervous system is explored. Expand
Heat Shock Protein 90 in Plants: Molecular Mechanisms and Roles in Stress Responses
The heat shock protein 90 (Hsp90) family mediates stress signal transduction, and plays important roles in the control of normal growth of human cells and in promoting development of tumor cells.Expand
Heat Shock Proteins Regulatory Role in Neurodevelopment
TLDR
This review will examine the regulatory role that individual chaperones may play in neurodevelopment, and will focus specifically on the signaling pathways involved in the maturation of neuronal and glial cells as well as the underlying vascular network. Expand
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References

SHOWING 1-10 OF 57 REFERENCES
Chaperone-mediated protein folding.
  • A. Fink
  • Biology, Medicine
  • Physiological reviews
  • 1999
TLDR
The availability of high-resolution structures has facilitated a more detailed understanding of the complex chaperone machinery and mechanisms, including the ATP-dependent reaction cycles of the GroEL and HSP70 chaperones. Expand
Comparison of tumor-specific immunogenicities of stress-induced proteins gp96, hsp90, and hsp70.
TLDR
It is suggested that the poor immunogenicity of hsp90 results from its lack of a measurable ATPase activity, which has been implicated in the ability of HSPs to transfer peptide to acceptor molecules. Expand
Roles of heat-shock proteins in innate and adaptive immunity
TLDR
The immunological properties of HSPs enable them to be used in new immunotherapies of cancers and infections and make them uniquely suited to an important role in organismal survival by their participation in innate and adaptive immune responses. Expand
Tumor rejection antigen gp96/grp94 is an ATPase: implications for protein folding and antigen presentation.
TLDR
It is demonstrated here that gp96 molecules contain ATP‐binding cassettes, bind ATP and possess an Mg(2+)‐dependent ATPase activity, which are consistent with its proposed roles in chaperoning antigenic peptides and in facilitating MHC class I‐‐peptide assembly in the ER lumen. Expand
PBP74, a new member of the mammalian 70-kDa heat shock protein family, is a mitochondrial protein.
TLDR
The cloning of a cDNA encoding a new member of the highly conserved mammalian 70-kDa heat shock protein (hsp 70) family termed PBP74 is reported, and a variety of immunological and biochemical approaches are used both in vitro and in vivo to demonstrate that it is imported into and resides in mitochondria. Expand
Hsp47: a molecular chaperone that interacts with and stabilizes correctly‐folded procollagen
TLDR
The results indicate that Hsp47 acts as a novel molecular chaperone, potentially stabilizing the correctly folded collagen helix from heat denaturation before its transport from the ER, and is distinct from that of prolyl 4‐hydroxylase. Expand
Calreticulin, a Peptide-binding Chaperone of the Endoplasmic Reticulum, Elicits Tumor- and Peptide-specific Immunity
TLDR
It is shown that CRT molecules can be complexed in vitro to unglycosylated peptides and used to elicit peptide-specific CD8+ T cell response in spite of exogenous administration, and closely resemble those of HSPs gp96, hsp90, and hsp70, although CRT has no apparent structural homologies to them. Expand
Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-kappa B pathway.
TLDR
It is reported here that heat shock proteins (HSP), the most abundant and conserved mammalian molecules, constitute such an internal signal that provides a unified mechanism for response to internal and external stimuli. Expand
CD91: a receptor for heat shock protein gp96
TLDR
The CD91 molecule is shown here to be a cell surface receptor for the heat shock protein gp96, and it is proposed that CD91 acts as a sensor for necrotic cell death. Expand
Heat shock protein 70-associated peptides elicit specific cancer immunity
TLDR
The data indicate that antigenicity of hSp70 preparations derives, not from hsp70 per se, but from associated peptides, which may suggest a novel method of using the peptide-binding property of hSP70 for specific vaccination against cancer and infectious diseases. Expand
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