Abstract
Evidence that membrane-bound and extracellular heat shock proteins (HSPs) with molecular weights of 70 and 90 kDa are potent stimulators of the immune responses has accumulated over the last decade. In this review, we discuss the modulation of Hsp70 expression, a major stress-inducible member of the HSP70 family, in the cytoplasm and on the plasma membrane of tumor cells by clinically applied interventions such as radio- and chemotherapy.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Amino Acid Sequence
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Animals
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Anti-Inflammatory Agents, Non-Steroidal / pharmacology
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Anti-Inflammatory Agents, Non-Steroidal / therapeutic use
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Antineoplastic Agents / pharmacology
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Antineoplastic Agents / therapeutic use*
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Cell Differentiation / drug effects
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Gene Expression Regulation, Neoplastic / drug effects
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Gene Expression Regulation, Neoplastic / radiation effects
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HSP70 Heat-Shock Proteins / biosynthesis
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HSP70 Heat-Shock Proteins / drug effects*
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HSP70 Heat-Shock Proteins / immunology
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HSP70 Heat-Shock Proteins / physiology
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Humans
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Membrane Proteins / drug effects
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Membrane Proteins / physiology
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Mice
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Mice, Mutant Strains
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Mice, SCID
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Molecular Sequence Data
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Multigene Family
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Neoplasm Proteins / biosynthesis
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Neoplasm Proteins / drug effects*
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Neoplasm Proteins / immunology
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Neoplasm Proteins / physiology
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Neoplasms / drug therapy
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Neoplasms / immunology
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Neoplasms / radiotherapy
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Neoplasms / therapy*
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Peptide Fragments / pharmacology
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Peptide Fragments / therapeutic use
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Stress, Physiological / drug effects
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Tretinoin / pharmacology
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Tretinoin / therapeutic use
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Xenograft Model Antitumor Assays
Substances
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Anti-Inflammatory Agents, Non-Steroidal
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Antineoplastic Agents
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HSP70 Heat-Shock Proteins
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Membrane Proteins
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Neoplasm Proteins
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Peptide Fragments
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Tretinoin