Inducible heat shock protein 70 kD and inducible nitric oxide synthase in hemorrhage/resuscitation-induced injury
Open accessAbstract
Inducible head shock protein 70 kD (HSP-70i) has been shown to protect cells, tissues, and organs from harmful assaults in vivo and in vitro experimental models. Hemorrhagic shock followed by resuscitation is the principal cause of death among trauma patients and soldiers in the battlefield. Although the underlying mechanisms are still not fully understood, it has been shown that nitric oxide (NO) overproduction and inducible nitric oxide synthase (iNOS) overexpression play important roles in producing injury caused by hemorrhagic shock including increases in polymorphonuclear neutrophils (PMN) infiltration to injured tissues and leukotriene B(4) (LTB(4)) generation. Moreover, transcription factors responsible for iNOS expression are also altered by hemorrhage and resuscitation. It has been evident that either up-regulation of HSP-70i or down-regulation of iNOS can limit tissue injury caused by ischemia/reperfusion or hemorrhage/resuscitation. In our laboratory, geldanamycin, a member of ansamycin family, has been shown to induce HSP- 70i overexpression and then subsequently to inhibit iNOS expression, to reduce cellular caspase-3 activity, and to preserve cellular ATP levels. HSP-70i is found to couple to iNOS and its transcription factor. Therefore, the complex formation between HSP-70i and iNOS may be a novel mechanism for protection from hemorrhage/resuscitation-induced injury.
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HSPA8 was significantly co-expressed with integrin alpha V, annexin I and other ECM components.
“Also, the heat shock protein 8 (HSPA8), a surface marker for the undifferentiated cellular state expressed on the surface of human embryonic stem cells [39], performs an important role in the repair processes following harmful tissular assaults (for example, hemorrhage or local ischemia) [40], and was found to be significantly co-expressed with integrin alpha V, annexin I and other ECM components.”
From Adipose tissue transcriptomic signature highlights the pathological relevance of extracellular matrix in human obesity (2008) · cites this paper as [40]
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- Authors
- KIANG, J. G.
- Affiliations
- Uniformed Services University of the Health Sciences (US)
- Corresponding author
- KIANG, Juliann G
- ORCID
- KIANG, Juliann G
- Venue
- Cell Research
- Published
- 2004-12
- Volume
- 14
- Issue
- 6
- Pages
- 450-459
- ISSN
- 1001-0602 (ISSN-L)
- 1748-7838
- OpenAlex
- W2049047452
- Cited by
- 63
- References
- 75
- Citations by year
- 2025: 2 · 2022: 1 · 2020: 1 · 2019: 2 · 2018: 2 · 2017: 5 · 2016: 2 · 2015: 6 · 2014: 5 · 2013: 4 · 2012: 3
- FWCI
- 0.43
- Type
- journal article
- Language
- en
- Open access
- green
- zenodo.org
- Licence
- public-domain
- www.springer.com/tdm (tdm)
- Locations
- Cell Research (publishedVersion)
- PubMed (publishedVersion)
- Zenodo (CERN European Organization for Nuclear Research) (submittedVersion, public-domain)
- Funders
- U.S. Department of Defense
- Uniformed Services University of the Health Sciences
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Health Sciences › Medicine › Critical Care and Intensive Care Medicine › Trauma, Hemostasis, Coagulopathy, Resuscitation
- Health Sciences › Medicine › Emergency Medicine › Cardiac Arrest and Resuscitation
- Keywords
- HSP70, inducible nitric oxide synthase, hemorrhagic shock, resuscitation, nitric oxide, ischemia-reperfusion injury, geldanamycin, ansamycins, caspase-3, neutrophil infiltration, leukotriene B4, transcription factors, trauma (physical injury)
- MeSH terms
- Animals, Enzyme Activation, Humans, Nitric Oxide, Resuscitation, Shock, Hemorrhagic, Wounds and Injuries, HSP70 Heat-Shock Proteins, Nitric Oxide Synthase, Nitric Oxide Synthase Type II
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