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IJMS
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Molecular Advances in Burn and Wound Healing
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Molecular Advances in Burn and Wound Healing

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Pathology, Diagnostics, and Therapeutics".

Deadline for manuscript submissions: 20 June 2025 | Viewed by 568

Special Issue Editor

Prof. Dr. Alisha R. Oropallo

E-Mail Website
Guest Editor
Zucker School of Medicine, Hofstra University/Northwell, New Hyde Park, NY 11042, USA
Interests: translational research; tissue regeneration

Special Issue Information

Dear Colleagues,

Burn and wound healing is a complex process orchestrated by intricate molecular cascades. Despite significant progress in clinical management, the complete molecular landscape of burn and wound healing still needs to be fully elucidated. This Special Issue will gather cutting-edge research exploring novel molecular mechanisms underlying burn and wound healing, ranging from the initial inflammatory response to tissue regeneration and scar formation. We invite original research articles, reviews, and perspectives that delve into the molecular aspects of cell signaling, growth factors, cytokines, extracellular matrix remodeling, angiogenesis, and immune responses involved in these processes.

This Special Issue will provide a comprehensive overview of the latest advances in molecular research on burn and wound healing. This collection will not only enrich our understanding of the fundamental mechanisms driving tissue repair but also potentially uncover novel therapeutic targets for improving clinical outcomes in patients with burns and wounds. We encourage contributions from diverse disciplines, including cell biology, molecular biology, immunology, genetics, and regenerative medicine, in relation to their clinical applications.

By highlighting the latest discoveries in this field, this Special Issue will foster collaboration and inspire further research to ultimately translate molecular insights into improved clinical strategies for burn and wound management.

Prof. Dr. Alisha R. Oropallo
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • burn
  • wound
  • molecular mechanisms
  • cell signaling
  • growth factors
  • cytokines
  • extracellular matrix
  • angiogenesis
  • healing

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Published Papers (1 paper)

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Research

10 pages, 1469 KiB  
Article
Human Keratin Matrices Suppress Matrix Metalloproteinase Activity to Support Wound Healing
by Allison N. Ramey-Ward, Shakesia Smith, Howard Walthall and Thomas H. Barrows
Int. J. Mol. Sci. 2024, 25(23), 12898; https://doi.org/10.3390/ijms252312898 - 30 Nov 2024
Viewed by 380
Abstract
Elevated protease activity is a hallmark of non-healing chronic wounds. Though multiple biomaterials exist that are successful in treating wounds, their roles in modulating the enzymatic environment of the wound are only beginning to be elucidated. Because keratin has long been known to [...] Read more.
Elevated protease activity is a hallmark of non-healing chronic wounds. Though multiple biomaterials exist that are successful in treating wounds, their roles in modulating the enzymatic environment of the wound are only beginning to be elucidated. Because keratin has long been known to be resistant to degradation by most enzymes, we studied a keratin biomaterial, the human keratin matrix (HKM), in the presence of enzymes identified to contribute to wound chronicity: neutrophil-derived elastase (NE), matrix metalloproteinase 1 (MMP-1), and MMP-9. Upon finding the suppression of MMP-9 activity in the presence of HKM without reducing enzyme protein levels, we further studied the ability of HKM to bind metal ions in the wound and showed the reduction of Zn2+ ion concentration in the presence of HKM. Finally, because of the enzyme resistance of keratin and the suppression of wound enzymes, we demonstrated that HKM was durable in the wound environment, and did not degrade in wound healing efficacy when left in place for two weeks compared to one week in a diabetic mouse model of wound non-healing. In this way, we show HKM is a unique and effective biomaterial for the treatment of chronic wounds through the modulation of wound MMP activity. Full article
(This article belongs to the Special Issue Molecular Advances in Burn and Wound Healing)
►▼ Show Figures

Figure 1

Figure 1
<p>Human keratin matrix (HKM) reduces the activity of matrix metalloproteinase 9 (MMP-9) and resists degradation. (<b>a</b>) Bar graph showing the effect of HKM on neutrophil-derived elastase (NE) activity compared to the NE inhibitor elastatinal. (<b>b</b>) Bar graph showing the effect of HKM on MMP-9 activity compared to the MMP inhibitor N-Isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid (NNGH). (<b>c</b>) Bar graph showing the effect of HKM on MMP-1 activity compared to the MMP inhibitor NNGH. (<b>d</b>) Bar graph showing the weight of bulk HKM samples incubated with MMP-9 was not changed during the duration of the enzymatic activity assays (1 h) or up to 1 day after. Bars represent mean ± standard deviation of n = 3 independent replicates. * <span class="html-italic">p</span> &lt; 0.05, ** <span class="html-italic">p</span> &lt; 0.01, *** <span class="html-italic">p</span> &lt; 0.001; ns = not significant by Brown–Forsythe and Welch analysis of variance (ANOVA) with Dunnett’s multiple comparisons.</p> Full article ">Figure 2
<p>Human keratin matrix (HKM) does not reduce matrix metalloproteinase (MMP) activity by reduction in protein levels. (<b>a</b>) A bar graph showing MMP-1 protein levels after incubation with HKM as determined by ELISA. (<b>b</b>) A bar graph showing MMP-9 protein levels after incubation with HKM as determined by ELISA. Bars represent mean ± standard deviation. * <span class="html-italic">p</span> &lt; 0.05, ** <span class="html-italic">p</span> &lt; 0.01 by Brown–Forsythe and Welch analysis of variance (ANOVA) with Dunnet’s multiple comparisons for n = 3 independent replicates.</p> Full article ">Figure 3
<p>Human keratin matrix (HKM) reduces Zn<sup>2+</sup> ion concentration in solution. Bar graph shows the concentration of zinc ions in solution after incubation with HKM compared with metal ion chelator ethylenediaminetetraacetic acid (EDTA). Bars represent mean ± standard deviation for n = 3 independent replicates. ** <span class="html-italic">p</span> &lt; 0.01 by one-way analysis of variance (ANOVA) with Tukey’s multiple comparisons.</p> Full article ">Figure 4
<p>Human keratin matrix (HKM) maintains healing efficacy for at least two weeks in a diabetic mouse wound model. (<b>a</b>) Diagram of mouse with 4 dorsal wounds each treated with 2 control and 2 HKM in randomized locations. (<b>b</b>) Picture of a mouse with wounds dressed. (<b>c</b>) Representative photo of a mouse at week 4, showing HKM wound closed and control wound still open. (<b>d</b>) Graph of wound size over time for each treatment: control (black, circle), HKM changed bi-weekly (blue, triangle). HKM is changed weekly (gold, square) and is reprinted with permission from previous work for comparison under the Creative Commons Attribution license [<a href="#B19-ijms-25-12898" class="html-bibr">19</a>]. Points represent the mean; error bars represent the standard error of the mean for n = 12 mice. **** <span class="html-italic">p</span> &lt; 0.0001 (control vs. HKM 2 Week), #### <span class="html-italic">p</span> &lt; 0.0001 (Control vs. HKM 1 Week), ^ <span class="html-italic">p</span> &lt; 0.05 (HKM 2 Week vs. HKM 1 Week) by two-way analysis of variance (ANOVA) with Tukey’s multiple comparisons. (<b>e</b>) Graph of the percentage of wounds healed for each treatment group at each timepoint (control—black, HKM changed weekly—gold [<a href="#B19-ijms-25-12898" class="html-bibr">19</a>], HKM changed bi-weekly—blue). *** <span class="html-italic">p</span> &lt; 0.001 by Fisher’s exact test.</p> Full article ">
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