The Chaperone Function of hsp70 Is Required for Protection against Stress-Induced Apoptosis

No abstract is available for this paper.

• Publication year

  2000

• Venue

  Molecular and Cellular Biology

• Publication date

  2000-10-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1128/MCB.20.19.7146-7159.2000PMID 10982831PMCID PMC86268
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• [Mitochondria and apoptosis].

  2000cited by this paper
• Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome

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  2000cited by this paper
• Use of a micromanipulator for high-efficiency cloning of cells co-expressing fluorescent proteins.

  2000cited by this paper
• The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant

  2000cited by this paper
• The Function of HSP72 in Suppression of c-Jun N-terminal Kinase Activation Can Be Dissociated from Its Role in Prevention of Protein Damage*

  1999cited by this paper
• BCL-2 family members and the mitochondria in apoptosis.

  1999cited by this paper
• Presence of a pre‐apoptotic complex of pro‐caspase‐3, Hsp60 and Hsp10 in the mitochondrial fraction of Jurkat cells

  1999cited by this paper
• The temporal relationship between protein phosphatase, mitochondrial cytochrome c release, and caspase activation in apoptosis.

  1999cited by this paper
• Heat shock proteins delivered with a virus vector can protect cardiac cells against apoptosis as well as against thermal or hypoxic stress.

  1999cited by this paper
• Cytochrome c and dATP-mediated Oligomerization of Apaf-1 Is a Prerequisite for Procaspase-9 Activation*

  1999cited by this paper
• Protein-Damaging Stresses Activate c-Jun N-Terminal Kinase via Inhibition of Its Dephosphorylation: a Novel Pathway Controlled by HSP72

  1999influential reference
• Bcl-2 proteins: regulators of apoptosis or of mitochondrial homeostasis?

  1999cited by this paper
• Hsp60 accelerates the maturation of pro‐caspase‐3 by upstream activator proteases during apoptosis

  1999cited by this paper
• ATPase activity of the heat shock protein Hsp72 is dispensable for its effects on dephosphorylation of stress kinase JNK and on heat‐induced apoptosis

  1999influential reference
• Oncogenic potential of Hsp72

  1999cited by this paper
• Role of Hsp70 in regulation of stress‐kinase JNK: implications in apoptosis and aging

  1998cited by this paper
• Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators.

  1998cited by this paper
• Molecular chaperones as HSF1-specific transcriptional repressors.

  1998cited by this paper
• The Hsp70 and Hsp60 chaperone machines.

  1998cited by this paper
• Hsp70 exerts its anti‐apoptotic function downstream of caspase‐3‐like proteases

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• In vivo heat shock protects rat myocardial mitochondria.

  1998cited by this paper
• Reduced thermotolerance in aged cells results from a loss of an hsp72-mediated control of JNK signaling pathway.

  1998cited by this paper
• The Carboxy-Terminal Domain of Hsc70 Provides Binding Sites for a Distinct Set of Chaperone Cofactors

  1998cited by this paper
• Heat Shock Protein 72 Modulates Pathways of Stress-induced Apoptosis*

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• Expression of heat shock protein 70 blocks thymic differentiation of T cells in transgenic mice

  1998cited by this paper
• Inhibition of cellular proliferation by the Wilms tumor suppressor WT1 requires association with the inducible chaperone Hsp70.

  1998cited by this paper
• The role of inducible 70-kDa heat shock protein in cell cycle control, differentiation, and apoptotic cell death of the human myeloid leukemic HL-60 cells.

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• Mitochondria and apoptosis.

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• The Release of Cytochrome c from Mitochondria: A Primary Site for Bcl-2 Regulation of Apoptosis

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• Stress-signalling kinase Sek1 protects thymocytes from apoptosis mediated by CD95 and CD3

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• Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade.

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• Heat shock proteins and cell proliferation in human breast cancer biopsy samples.

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• Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis

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• Use of a dicistronic expression cassette encoding the green fluorescent protein for the screening and selection of cells expressing inducible gene products.

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• Overexpression of the heat shock protein 70 enhances the TCR/CD3- and Fas/Apo-1/CD95-mediated apoptotic cell death in Jurkat T cells.

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• Hsp70 Prevents Activation of Stress Kinases

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• Prevention of Apoptosis by Bcl-2: Release of Cytochrome c from Mitochondria Blocked

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• The role of c-Jun N-terminal kinase (JNK) in apoptosis induced by ultraviolet C and gamma radiation. Duration of JNK activation may determine cell death and proliferation.

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• Molecular chaperones in cellular protein folding

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• Protein kinase cascades activated by stress and inflammatory cytokines

  1996cited by this paper
• Mitochondria are selective targets for the protective effects of heat shock against oxidative injury.

  1996cited by this paper
• T Cell Lymphoma in Transgenic Mice Expressing the HumanHsp70Gene

  1996cited by this paper
• Requirement for ceramide-initiated SAPK/JNK signalling in stress-induced apoptosis

  1996cited by this paper
• Heat shock proteins increase resistance to apoptosis.

  1996cited by this paper
• Bcl-2 inhibits the mitochondrial release of an apoptogenic protease

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• Inhibition of proliferation and induction of apoptosis by abrogation of heat-shock protein (HSP) 70 expression in tumor cells

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• Transcriptional activation by tetracyclines in mammalian cells.

  1995cited by this paper
• Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: inhibition by overexpression of Bcl-2 and Abl

  1995cited by this paper
• Over‐expression of hsp70 confers tumorigenicity to mouse fibrosarcoma cells

  1995cited by this paper
• Effects of expressing human Hsp70 and its deletion derivatives on heat killing and on RNA and protein synthesis.

  1995cited by this paper
• Heat shock protein hsp70 accelerates the recovery of heat-shocked mammalian cells through its modulation of heat shock transcription factor HSF1.

  1995cited by this paper
• The development of thermotolerance protects blowfly flight muscle mitochondrial function from heat damage

  1995cited by this paper
• Opposing Effects of ERK and JNK-p38 MAP Kinases on Apoptosis

  1995cited by this paper
• Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ‐1.

  1995influential reference
• Molecular chaperones in cellular protein folding.

  1994cited by this paper
• Importance of the ATP-binding domain and nucleolar localization domain of HSP72 in the protection of nuclear proteins against heat-induced aggregation.

  1994cited by this paper
• 1 Progress and Perspectives on the Biology of Heat Shock Proteins and Molecular Chaperones

  1994cited by this paper
• Heat shock protects neuronal cells from programmed cell death by apoptosis.

  1993cited by this paper
• The DNA-binding activity of the human heat shock transcription factor is regulated in vivo by hsp70

  1993cited by this paper
• Major heat shock protein hsp70 protects tumor cells from tumor necrosis factor cytotoxicity.

  1992cited by this paper
• The consequences of expressing hsp70 in Drosophila cells at normal temperatures.

  1992influential reference
• Heat shock protein hsp70 protects cells from thermal stress even after deletion of its ATP-binding domain.

  1992cited by this paper
• Induced thermotolerance to apoptosis in a human T lymphocyte cell line

  1992cited by this paper
• Growth, Metabolic, And Antibody Production Kinetics Of Hybridoma Cell Culture: 1. Analysis Of Data From Controlled Batch Reactors

  1991cited by this paper
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  1991influential reference
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  1989cited by this paper
• Cell cycle-dependent association of HSP70 with specific cellular proteins

  1989cited by this paper
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  1989cited by this paper
• Expression of human HSP70 during the synthetic phase of the cell cycle.

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