The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
Wound Fluids from Human Pressure Ulcers Contain Elevated Matrix Metalloproteinase Levels and Activity Compared to Surgical Wound Fluids
Open accessAbstract
Fluid from acute surgical wounds and from nonhealing pressure ulcers was examined for the presence of several matrix metalloproteinases. Gelatin zymography demonstrated the presence of two major gelatinases with apparent molecular masses of 72 kDa and 92 kDa and two minor gelatinases with apparent mobilities of 68 kDa and 125 kDa. Antigen-specific sera identified the 72-kDa protein as matrix melloproteinase-2. The same sera also reacted with the 68-kDa protein, which is consistent with it being an activated form of matrix metalloproteinase-2. Antigen-specific sera identified the 92-kDa and 125-kDa proteins as matrix metalloproteinase-9. Levels of matrix metalloproteinase-2 and matrix metalloproteinase-9 were elevated more than 10-fold and 25-fold, respectively, in fluids from pressure ulcers compared with fluids from healing wounds. Examination of total potential and actual collagenolytic activity revealed that fluid from pressure ulcers contained significantly greater levels of both total and active collagenase compared with that of acute surgical wounds. In addition, an enzyme-linked immunosorbent assay demonstrated that fluids from pressure ulcers contained significantly more collagenase complexed with the inhibitor, tissue inhibitor of metalloproteinases. Together, these observations suggest that an imbalance exists between levels of matrix metalloproteinases and their inhibitors in the fluids of pressure ulcers and that this is primarily the result of elevated levels of the matrix metalloproteinases. The presence of excessive levels of activated forms of matrix-degrading enzymes at the wound surface of pressure ulcers may impede the healing of these wounds and may be relevant to the development of new rationales for treatment.
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“Last, in chronic wounds, there is a marked increase in serine proteases that degrades matrix components, including fibronectin, as well as various key growth factors, all of which are required for remodeling of the ECM and cell growth (38-41).”
From Wound repair and regeneration: Mechanisms, signaling, and translation (2014) · cites this paper as [38]
In the citing paper
“It has been shown that matrix metalloproteinases (MMPs), such as collagenase and gelatinases A and B, are elevated in chronic wound fluids when compared to acute wound fluid (25, 38).”
From Wound repair and regeneration: Mechanisms, signaling, and translation (2014) · cites this paper as [38]
Citations
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Wound repair and regeneration: Mechanisms, signaling, and translation
Eming, S. A., Martin, P., & Tomic-Canic, M. (2014) · Science Translational Medicine · doi:10.1126/scitranslmed.3009337 · Cited by 3,562
“Last, in chronic wounds, there is a marked increase in serine proteases that degrades matrix components, including fibronectin, as well as various key growth factors, all of which are required for remodeling of the ECM and cell growth (38-41).”
Wound healing: an overview of acute, fibrotic and delayed healing
Diegelmann, R. (2004) · Frontiers in Bioscience · doi:10.2741/1184 · Cited by 2,147
“TGF-ß has a three-pronged effect on extracellular matrix deposition (27).”
BackgroundInfluentialAnalysis of the acute and chronic wound environments: the role of proteases and their inhibitors
Trengove, N. J., Stacey, M. C., Macauley, S., Bennett, N., Gibson, J., Burslem, F., Murphy, G., & Schultz, G. (1999) · Wound Repair and Regeneration · doi:10.1046/j.1524-475x.1999.00442.x · Cited by 908
Physiology and healing dynamics of chronic cutaneous wounds
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Why chronic wounds will not heal: a novel hypothesis
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Metadata
- Authors
- Yager, D. R., Zhang, L.-Y., Liang, H.-X., Diegelmann, R. F., & Cohen, I. K.
- Affiliations
- Virginia Commonwealth University Medical Center (US)
- Venue
- Journal of Investigative Dermatology
- Publisher
- Elsevier BV
- Published
- 1996-11
- Volume
- 107
- Issue
- 5
- Pages
- 743-748
- ISSN
- 0022-202X (ISSN-L)
- OpenAlex
- W2061992885
- Cited by
- 389
- References
- 41
- Citations by year
- 2026: 6 · 2025: 7 · 2024: 8 · 2023: 5 · 2022: 9 · 2021: 20 · 2020: 9 · 2019: 9 · 2018: 16 · 2017: 11 · 2016: 23 · 2015: 16 · 2014: 17 · 2013: 18 · 2012: 21
- FWCI
- 4.52
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Journal of Investigative Dermatology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01gm047566-08)
- National Institute of General Medical Sciences (GM-47566, GM20298)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Health Sciences › Medicine › Surgery › Wound Healing and Treatments
- Health Sciences › Medicine › Dermatology › Pressure Ulcer Prevention and Management
- Keywords
- pressure ulcers, matrix metalloproteinases, MMP-2, MMP-9, wound fluid, surgical wounds, collagenase, tissue inhibitors of metalloproteinases, chronic wounds, wound healing, gelatinase
- MeSH terms
- Animals, Pressure Ulcer, Glycoproteins, Humans, Metalloendopeptidases, Rabbits, Surgical Procedures, Operative, Wound Healing, Collagenases, Gelatinases, Tissue Inhibitor of Metalloproteinases, Matrix Metalloproteinase 2, Matrix Metalloproteinase 9
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