ArticleInternational journal of molecular sciences2024
Human Keratin Matrices Suppress Matrix Metalloproteinase Activity to Support Wound Healing.
Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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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 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 Zn
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