ArticleThe Journal of investigative dermatology2018
Extracellular and Non-Chaperone Function of Heat Shock Protein-90α Is Required for Skin Wound Healing.
Article in The Journal of investigative dermatology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
24 citing papers in PubMed, 38 citations in OpenAlex.
- Targeting eHsp90α/GRP78 signaling-mediated endothelial barrier dysfunction in diabetic atherosclerosis: evidence from clinical and experimental studies.Molecular and cellular biochemistry · 2026Article
- Spatiotemporal acoustic meta-patches for multifactorial wound treatment.Bioactive materials · 2026Article
- The Role of Thermal Immunomodulation in Postoperative Wound Repair with a Focus on Hepatic Surgery.International journal of molecular sciences · 2026Review
- Heat shock protein 90 stabilizes CD93 glycosylation to influence angiogenesis during diabetic wound healing.Cellular & molecular biology letters · 2026Article
- Fractional carbon dioxide laser-induced photothermal activation of mesenchymal stem cell-derived exosomes accelerates diabetic wound healing by enhancing angiogenesis.World journal of diabetes · 2026Article
- Review
- Article
- A novel method for the establishment of autologous skin cell suspensions: characterisation of cellular sub-populations, epidermal stem cell content and wound response-enhancing biological properties.Frontiers in bioengineering and biotechnology · 2024Article
- Organismal Roles of Hsp90.Biomolecules · 2023Review
- Heat shock protein 90 inhibitor RGRN-305 potently attenuates skin inflammation.Frontiers in immunology · 2023Article
- Exosomes from Adipose Stem Cells Promote Diabetic Wound Healing through the eHSP90/LRP1/AKT Axis.Cells · 2022Article
- Cytosolic Hsp90 Isoform-Specific Functions and Clinical Significance.Biomolecules · 2022Review
- Extracellular Heat Shock Protein-90 (eHsp90): Everything You Need to Know.Biomolecules · 2022Review
- The Therapeutic Roles of Recombinant Hsp90α on Cornea Epithelial Injury.Investigative ophthalmology & visual science · 2022Article
- Targeting extracellular Hsp90: A unique frontier against cancer.Frontiers in molecular biosciences · 2022Review
- Correlation of Serum Chemokine (C-C Motif) Ligand 21 and Heat Shock Protein 90 with Preeclampsia.Evidence-based complementary and alternative medicine : eCAM · 2022Article
- Wound Healing Driver Gene and Therapeutic Development: Political and Scientific Hurdles.Advances in wound care · 2021Review
- Combination of lyophilized adipose-derived stem cell concentrated conditioned medium and polysaccharide hydrogel in the inhibition of hypertrophic scarring.Stem cell research & therapy · 2021Article
- Computationally predicted gene regulatory networks in molluscan biomineralization identify extracellular matrix production and ion transportation pathways.Bioinformatics (Oxford, England) · 2020Article
- Heat shock proteins in the physiology and pathophysiology of epidermal keratinocytes.Cell stress & chaperones · 2019Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Despite years of effort and investment, there are few topical or systemic medications for skin wounds. Identifying natural drivers of wound healing could facilitate the development of new and effective treatments. When skin is injured, there is a massive increase of heat shock protein (Hsp) 90α inside the wound bed. The precise role for these Hsp90α proteins, however, was unclear. The availability of a unique mouse model that lacked the intracellular ATPase-driven chaperoning, but spared the extracellular fragment-5-supported pro-motility function of Hsp90α allowed us to test specifically the role of the non-chaperone function of Hsp90α in normal wound closure. We found that the chaperone-defective Hsp90α-Δ mutant mice showed similar wound closure rate as the wild-type Hsp90α mice. We generated recombinant proteins from the mouse cDNAs encoding the Hsp90α-Δ and wild-type Hsp90α. Topical application of Hsp90α-Δ mutant protein promoted wound closure as effectively as the full-length wild-type Hsp90α protein. More importantly, selective inhibition of the extracellular Hsp90α-Δ protein function by a monoclonal antibody targeting the fragment-5 region disrupted normal wound closure in both wild-type Hsp90α and Hsp90α-Δ mice. Thus, this study provides direct support for non-chaperone, extracellular Hsp90α as a potential driver for normal wound closure.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.