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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]
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Li, W., Chong, S., Huang, E. Y., & Tuan, T. (2003) · Wound Repair and Regeneration · doi:10.1046/j.1524-475x.2003.11402.x · Cited by 113
Uccioli, L., Izzo, V., Meloni, M., Vainieri, E., Ruotolo, V., & Giurato, L. (2015) · Journal of Wound Care · doi:10.12968/jowc.2015.24.sup4b.35 · Cited by 106
Woo, K. Y., Ayello, E. A., & Sibbald, R. G. (2007) · Advances in Skin & Wound Care · doi:10.1097/00129334-200702000-00009 · Cited by 108
“Excessive accumulation and activation of MMPs can suppress cell proliferation and angiogenesis due to destruction of growth factors and matrix proteins that provide necessary substrates for cellmigration and integrity of the tissue.(49,50) Wound fluids from chronic ulcers have been shown to be proteolytic, from an ove…”
BackgroundWound Fluids: A Window Into the Wound Environment?
Yager, D. R., Kulina, R. A., & Gilman, L. A. (2007) · The International Journal of Lower Extremity Wounds · doi:10.1177/1534734607307035 · Cited by 108
“Fluid has also been obtained from chronic wounds by direct aspiration from under occlusive dressings.(7,8,14,18-23) Because this approach can be somewhat problematic, fluids have also been extracted from materials placed onto the wounds.”
BackgroundMethodInfluentialSelf-citationWilliams, D. T., Enoch, S., Miller, D., Harris, K., Price, P., & Harding, K. G. (2005) · Wound Repair and Regeneration · doi:10.1111/j.1067-1927.2005.130203.x · Cited by 103
Ectopic localization of matrix metalloproteinase-9 in chronic cutaneous wounds
Mirastschijski, U., Impola, U., Jahkola, T., Karlsmark, T., Ågren, M. S., & Saarialho‐Kere, U. (2002) · Human Pathology · doi:10.1053/hupa.2002.32221 · Cited by 103
Norgauer, J., Hildenbrand, T., Idzko, M., Panther, E., Bandemir, E., Hartmann, M., Vanscheidt, W., & Herouy, Y. (2002) · British Journal of Dermatology · doi:10.1046/j.1365-2133.2002.05025.x · Cited by 101
Cowin, A. J., Hatzirodos, N., Holding, C. A., Dunaiski, V., Rayner, T. E., Harries, R. H., Fitridge, R., Cooter, R. D., Schultz, G. S., & Belford, D. A. (2001) · Journal of Investigative Dermatology · doi:10.1046/j.0022-202x.2001.01501.x · Cited by 100
Goldberg, S. R., & Diegelmann, R. F. (2020) · Surgical Clinics of North America · doi:10.1016/j.suc.2020.05.001 · Cited by 100
Self-citationWall, S. J., Bevan, D., Thomas, D. W., Harding, K. G., Edwards, D. R., & Murphy, G. (2002) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2002.01779.x · Cited by 100
Preclinical promise of becaplermin (rhPDGF-BB) in wound healing
LeGrand, E. K. (1998) · The American Journal of Surgery · doi:10.1016/s0002-9610(98)00177-9 · Cited by 100
Modified cotton gauze dressings that selectively absorb neutrophil elastase activity in solution
Edwards, J. V., Yager, D. R., Cohen, I. K., Diegelmann, R. F., Montante, S. J., Bertoniere, N. R., & Bopp, A. F. (2001) · Wound Repair and Regeneration · doi:10.1046/j.1524-475x.2001.00050.x · Cited by 98
Self-citationGabriel, A., Shores, J. T., Bernstein, B., de Leon, J., Kamepalli, R., Wolvos, T. A., Baharestani, M. M., & Gupta, S. C. (2009) · International Wound Journal · doi:10.1111/j.1742-481x.2009.00628.x · Cited by 95
The role of biophysical properties of provisional matrix proteins in wound repair
Chester, D., & Brown, A. C. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.08.004 · Cited by 91
“Neutrophils release significant amounts of proteases, such as collagenase and elastase, leading to destruction of ECM components and growth factors [63,64].”
Chronic wound fluid—thinking outside the box
Widgerow, A. D. (2011) · Wound Repair and Regeneration · doi:10.1111/j.1524-475x.2011.00683.x · Cited by 93
“Chronic wound fluid exudate has been proven to be antiangiogenic as opposed to the angiogenic stimulatory nature of acute wound fluid.(2,6,7,25) Angiogenesis, the formation of new capillaries, is the prelude to granulation tissue formation.”
BackgroundPrognostic value of markers of collagen remodeling in venous ulcers
Tarlton, J. F., Bailey, A. J., Crawford, E., Jones, D., Moore, K., & Harding, K. G. (1999) · Wound Repair and Regeneration · doi:10.1046/j.1524-475x.1999.00347.x · Cited by 88
The Unified Theory of hernia formation
Bendavid, R. (2004) · Hernia · doi:10.1007/s10029-004-0217-6 · Cited by 87
“TIMP-1 and TIMP-2 are inhibitors of metalloproteinases, and their presence at reduced concentrations has been identified, providing a possible contribution to the late occurrence of herniation [47, 54, 55, 56].”
BackgroundMouës, C. M., van Toorenenbergen, A. W., Heule, F., Hop, W. C. J., & Hovius, S. E. R. (2008) · Wound Repair and Regeneration · doi:10.1111/j.1524-475x.2008.00395.x · Cited by 86
Matrix metalloproteinase 9 (MMP-9) is upregulated during scarless wound healing in athymic nude mice
Manuel, J. A., & Gawrońska‐Kozak, B. (2006) · Matrix Biology · doi:10.1016/j.matbio.2006.07.008 · Cited by 86
Resveratrol-Induced Signal Transduction in Wound Healing
Pignet, A.-L., Schellnegger, M., Hecker, A., Kohlhauser, M., Kotzbeck, P., & Kamolz, L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222312614 · Cited by 86
“An increase of these markers leads to an up-regulation of matrix metalloproteinases (MMP), which are especially elevated in chronic wounds [26].”
BackgroundSchmutz, J. ‐., Meaume, S., Fays, S., Ourabah, Z., Guillot, B., Thirion, V., Collier, M. A., Barrett, S., Smith, J. M., Bohbot, S., et al. (2008) · International Wound Journal · doi:10.1111/j.1742-481x.2008.00453.x · Cited by 83
Tandara, A. A., & Mustoe, T. A. (2010) · Journal of Plastic Reconstructive & Aesthetic Surgery · doi:10.1016/j.bjps.2010.03.051 · Cited by 83
“On the other hand excessive levels of MMPs impair wound healing or act destructive on normal tissue as in the case of rheumatoid arthritis or cardiovascular disease [18-20].”
BackgroundInflammation 2: its role in the healing of chronic wounds
Hart, J. (2002) · Journal of Wound Care · doi:10.12968/jowc.2002.11.7.26416 · Cited by 82
Interleukin-1α and Collagenase Activity Are Elevated in Chronic Wounds
Barone, E. J., Yager, D. R., Pozez, A. L., Olutoye, O. O., Crossland, M. C., Diegelmann, R. F., & Cohen, I. K. (1998) · Plastic & Reconstructive Surgery · doi:10.1097/00006534-199809040-00015 · Cited by 80
Self-citationMatrix metalloproteinases in impaired wound healing
Keller, U. A. D., & Sabino, F. (2015) · Metalloproteinases In Medicine · doi:10.2147/mnm.s68420 · Cited by 85
“51 Moreover, the activity of MMP-9 in chronic wounds was found to be a better indicator for chronicity than the total proteolytic activity in wound fluid.”
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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