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Human Keratin Matrices Suppress Matrix Metalloproteinase Activity to Support Wound Healing
HKM is a unique and effective biomaterial for the treatment of chronic wounds through the modulation of wound MMP activity.
By:
Allison N. Ramey-Ward
Shakesia Smith
Howard Walthall
Thomas H. Barrows
ProgenaCare Global, LLC, Marietta, GA 30067, USA*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2024, 25(23), 12898; https://doi.org/10.3390/ijms252312898
Submission received: 31 October 2024 / Revised: 26 November 2024 / Accepted: 27 November 2024 / Published: 30 November 2024
(This article belongs to the Special Issue Molecular Advances in Burn and Wound Healing)
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 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.
Keywords:
keratin; biomaterial; wound healing; MMP; enzyme activity
Read The Entire Article:
https://www.mdpi.com/1422-0067/25/23/12898
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