The DOI matches its Crossref record; 145 of the 148 references it cites were found in a registry or an index.
Releasing signals, secretory pathways, and immune function of endogenous extracellular heat shock protein 72
Abstract
Heat shock proteins (Hsp) were first characterized as intracellular proteins, which function to limit protein aggregation, facilitate protein refolding, and chaperone proteins. During times of cellular stress, intracellular Hsp levels increase to provide cellular protection. Recently, it has been recognized that Hsp, particularly Hsp72, are also found extracellularly (eHsp72), where they exhibit potent immunomodulatory effects on innate and acquired immunity. Circulating eHsp72 levels also greatly increase during times of stress (i.e., when an organism is exposed to a physical/psychological stressor or suffers from various pathological conditions). It has been proposed that elevated eHsp72 serves a protective role by facilitating immunological responses during times of increased risk of pathogenic challenge and/or tissue damage. This review focuses on the in vivo releasing signals and immunomodulatory function(s) of endogenous eHsp72. In addition, we present data that emphasize the importance of caution when conducting in vitro immunological tests of Hsp72 function.
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“the release of Hsp72 (a possible DAMP) after tailshock is dependent on α-adrenergic, but not βor glucocorticoid, receptor signaling (Johnson et al, 2005;Johnson and Fleshner, 2006).”
From Danger Signals and Inflammasomes: Stress-Evoked Sterile Inflammation in Mood Disorders (2017) · cites this paper as Johnson and Fleshner, 2006
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Goodman & Gilman's The Pharmacological Basis of Therapeutics
Brunton, L. L. (1985) · Cited by 7,321
Goodman and Gilman's the Pharmacological Basis of Therapeutics
Stigelman, W. H., & Pharm, D. (1986) · Military Medicine · doi:10.1093/milmed/151.1.386 · Cited by 6,796
Lindquist, S., & Craig, E. A. (1988) · Annual Review of Genetics · doi:10.1146/annurev.ge.22.120188.003215 · Cited by 5,304
Toll-like receptors: critical proteins linking innate and acquired immunity
Akira, S., Takeda, K., & Kaisho, T. (2001) · Nature Immunology · doi:10.1038/90609 · Cited by 4,777
Molecular chaperones in cellular protein folding
Hartl, F. U. (1996) · Nature · doi:10.1038/381571a0 · Cited by 3,584
Zitvogel, L., Régnault, A., Lozier, A., Wolfers, J., Flament, C., Tenza, D., Ricciardi‐Castagnoli, P., Raposo, G., & Amigorena, S. (1998) · Nature Medicine · doi:10.1038/nm0598-594 · Cited by 2,266
A new puffing pattern induced by temperature shock and DNP in drosophila
Ritossa, F. (1962) · Cellular and Molecular Life Sciences · doi:10.1007/bf02172188 · Cited by 2,146
Asea, A. A. A., Kraeft, S., Kurt‐Jones, E. A., Stevenson, M. A., Chen, L. B., Finberg, R. W., Koo, G. C., & Calderwood, S. K. (2000) · Nature Medicine · doi:10.1038/74697 · Cited by 1,642
Natural adjuvants: Endogenous activators of dendritic cells
Gallucci, S., Lolkema, M. P., & Matzinger, P. (1999) · Nature Medicine · doi:10.1038/15200 · Cited by 1,601
Novel Signal Transduction Pathway Utilized by Extracellular HSP70
Asea, A., Rehli, M., Kabingu, E., Boch, J. A., Baré, O., Auron, P. E., Stevenson, M. A., & Calderwood, S. K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200497200 · Cited by 1,510
Research works printed but not linked: 1
- Gao, 2003, Endotoxin contamination in recombinant human heat shock protein 70 (Hsp70) preparation is responsible for the induction of tumor necrosis factor α release by murine macrophages, J. Biol. Chem., 278, 174, 10.1074/jbc.M208742200 · DOI · Paper page
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Metadata
- Authors
- Johnson, J. D., & Fleshner, M.
- Affiliations
- University of Colorado Boulder (US)
- Corresponding author
- Fleshner, Monika
- ORCID
- Fleshner, Monika
- Venue
- Journal of Leukocyte Biology
- Publisher
- Oxford University Press (OUP)
- Published
- 2005-12-30
- Volume
- 79
- Issue
- 3
- Pages
- 425-434
- ISSN
- 0741-5400 (ISSN-L)
- 1938-3673
- OpenAlex
- W2165218249
- Cited by
- 251
- References
- 148
- Citations by year
- 2026: 5 · 2025: 2 · 2024: 2 · 2023: 8 · 2022: 7 · 2021: 6 · 2020: 8 · 2019: 8 · 2018: 12 · 2017: 13 · 2016: 12 · 2015: 21 · 2014: 18 · 2013: 18 · 2012: 20
- FWCI
- 1.02
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Leukocyte Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › S100 Proteins and Annexins
- Keywords
- HSP72, secretory pathway, immunomodulation, innate immunity, adaptive immunity, stress response, molecular chaperones
- MeSH terms
- Animals, Cell Membrane, Humans, Immunity, Cellular, Immunity, Innate, Immunologic Factors, Receptors, Adrenergic, alpha, Stress, Physiological, Signal Transduction, Up-Regulation, Extracellular Fluid, HSP72 Heat-Shock Proteins
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