The DOI matches its Crossref record.
MMP-8 Is the Predominant Collagenase in Healing Wounds and Nonhealing Ulcers
Abstract
Background The initial cleavage of collagen by collagenase represents the rate-limiting step in the degradation of this central extracellular matrix protein. Chronic nonhealing ulcers, especially pressure ulcers, typically contain elevated levels of collagenolytic activity. However, there have been no detailed attempts to identify the source of these collagenases and their activity either in normal healing wounds or in chronic nonhealing ulcers.Materials and methods Levels of the matrix metalloproteinases, MMP-1 and MMP-8, and the tissue inhibitor of matrix metalloproteinases, TIMP-1, were measured in fluids and tissues of healing human wounds and nonhealing ulcers by ELISA. Relative MMP-1 and MMP-8 levels were also analyzed by substrate preference in a functional assay.Results The patterns of the collagenases MMP-1 and MMP-8 in healing wounds were distinct, with MMP-8 appearing in significantly greater amounts than MMP-1. Chronic nonhealing ulcers were characterized by significantly higher levels of MMP-1 and MMP-8, and lower levels of TIMP-1, than in healing wounds. Levels of both MMP-1 and MMP-8 varied greatly in chronic ulcers, although MMP-8 was always the predominant collagenase present in these wounds. Interestingly, these collagenases were present almost exclusively in their inactive forms in healing wounds, whereas nonhealing ulcers possessed significant levels of the active forms of these enzymes.Conclusions These results clearly demonstrate that the neutrophil-derived MMP-8 is the predominant collagenase present in normal healing wounds and suggest that overexpression and activation of this collagenase may be involved in the pathogenesis of nonhealing chronic ulcers. In addition, excessive collagenolytic activity in chronic ulcers is made possible, partly because of the reduced levels of the inhibitor, TIMP-1.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Specifically, MMP‐1 and MMP‐8 are important, as they have been found to be active during wound healing and remodeling.”
From Unraveling and Harnessing the Immune Response at the Cell–Biomaterial Interface for Tissue Engineering Purposes (2024) · cites this paper as [257]
In the citing paper
“Both are used in the cleavage of collagen, with MMP‐1 being more proficient in the cleavage of collagen type III, while MMP‐8 is more efficient in degrading collagen type I and is the main collagenase active in regular healing.”
From Unraveling and Harnessing the Immune Response at the Cell–Biomaterial Interface for Tissue Engineering Purposes (2024) · cites this paper as [257]
In the citing paper
“neutrophil-derived proteases, such as elastase and matrix metalloproteinases (MMPs), can degrade healthy extracellular matrix (ECM), and increased levels of these proteases have been repeatedly detected in chronic wounds [52–56].”
From Immunology of Wound Healing (2018) · cites this paper as [55]
Citations
Cited by
Sorted by citations
Items 201–300 of 358
How and Why to Surgically Debride Neuropathic Diabetic Foot Wounds
Armstrong, D. G., Lavery, L. A., Vazquez, J. R., et al. (2002) · Journal of the American Podiatric Medical Association · doi:10.7547/87507315-92-7-402 · Cited by 20
Restoring balance: biofilms and wound dressings
Percival, S. L. (2018) · Journal of Wound Care · doi:10.12968/jowc.2018.27.2.102 · Cited by 20
Regulation of matrix remodelling phenotype in gingival fibroblasts by substratum topography
Kim, S. S., Wen, W., Prowse, P. D. H., et al. (2015) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12451 · Cited by 20
“MMP-8, also known as neutrophil collagenase, is significantly up-regulated in gingival healing around titanium implants in humans [52], as well as in skin healing [53] suggesting it is a prominent regulator of remodelling in these tissues.”
BackgroundGenetic Association ofMMP10,MMP14, andMMP16with Dental Caries
Lewis, D. D., Shaffer, J. R., Feingold, E., Cooper, M. E., Vanyukov, M. M., Maher, B. S., Slayton, R. L., Willing, M. C., Reís, S. E., McNeil, D. W., et al. (2017) · International Journal of Dentistry · doi:10.1155/2017/8465125 · Cited by 21
“MMPs are involved in several diseases such as cancer [18], arthritis [19], tissue ulceration [20], periodontitis [21, 22], early tooth development [23, 24], and dental caries [16, 25, 26].”
BackgroundJamadagni, P. S., Jamadagni, S. B., Mukherjee, K., Upadhyay, S. N., Gaidhani, S. N., & Hazra, J. (2016) · AYU (An International Quarterly Journal of Research in Ayurveda) · doi:10.4103/ayu.ayu_51_17 · Cited by 19
Bhattacharyya, J., Mondal, G., Kuncha, M., Agawane, S. B., Sistla, R., Gangireddy, S. R., Madhavi, R. D., Reddy, P. K., Konda, V. R., Rao, S. R., et al. (2009) · Molecular Pharmaceutics · doi:10.1021/mp800231z · Cited by 19
Goldberg, S. R., & Diegelmann, R. F. (2012) · Critical Care Nursing Clinics of North America · doi:10.1016/j.ccell.2012.03.002 · Cited by 19
Leg Ulcer Treatment Outcomes with New Ovine Collagen Extracellular Matrix Dressing
Bohn, G. A., & Gass, K. (2014) · Advances in Skin & Wound Care · doi:10.1097/01.asw.0000453728.12032.6f · Cited by 19
“Specifically, in a study of fluids and tissues of healing and nonhealing ulcers, Nwomeh et al(35) found that neutrophil-derived MMP-8 is the predominant collagenase present in normal healing wounds; results of that study suggest that overexpression and activation of collagenase MMP-8 is likely involved in the pathogen…”
BackgroundKari, O., Määttã, M., Tervahartiala, T. I., et al. (2009) · Graefe s Archive for Clinical and Experimental Ophthalmology · doi:10.1007/s00417-009-1042-5 · Cited by 18
Protease-modulating matrix treatments for healing venous leg ulcers
Westby, M. J., Dumville, J. C., Stubbs, N. C., Norman, G., & Cullum, N. A. (2015) · Cochrane Database of Systematic Reviews · doi:10.1002/14651858.cd011918 · Cited by 18
McDaniel, J. C., Rausch, J., & Tan, A. (2020) · Trials · doi:10.1186/s13063-019-3970-7 · Cited by 18
Xu, J., Du, W., Xue, X., Chen, M., Zhou, W., & Luo, X. (2023) · Frontiers in Surgery · doi:10.3389/fsurg.2023.1113491 · Cited by 17
“Another group of scholars has argued that leukocytes are not an ideal component of platelet-rich plasma and that the release of collagenases such as matrix metalloproteinase 8 and matrix metalloproteinase 6 by leukocytes has a detrimental effect on tendon matrix deposition (67, 68).”
BackgroundExploring the sources and potential applications of marine collagenases
Barzkar, N., Babich, O., Сухих, С. А., Maran, B. A. V., Jahromi, S. T., Luwor, R. B., Sorsa, T. A., & Das, R. (2024) · Biocatalysis and Agricultural Biotechnology · doi:10.1016/j.bcab.2024.103150 · Cited by 17
A biodegradable copolymer for the slow release of growth hormone expedites scarring in diabetic rats
García‐Esteo, F., Pascual, G., Gallardo, A., San‐Román, J., Buján, J., & Bellón, J. M. (2006) · Journal of Biomedical Materials Research Part B Applied Biomaterials · doi:10.1002/jbm.b.30665 · Cited by 17
Mayer, D., Armstrong, D. G., Schultz, G., Percival, S. L., Malone, M., Romanelli, M., Keast, D. H., & Jeffery, S. (2018) · Journal of Wound Care · doi:10.12968/jowc.2018.27.9.594 · Cited by 17
Wound fluid sampling methods for proteomic studies: A scoping review
Harvey, J., Mellody, K. T., Cullum, N. A., Watson, R. E. B., & Dumville, J. C. (2022) · Wound Repair and Regeneration · doi:10.1111/wrr.13009 · Cited by 17
Pirayesh, A., Dessy, L. A., Rogge, F. J., Hoeksema, H., Sinove, Y., Antonia, A. D., Jawad, M. A., Gilbert, P. M., Rubino, C., Scuderi, N., et al. (2007) · Acta chirurgica Belgica · doi:10.1080/00015458.2007.11680145 · Cited by 17
“MMP-1 is associated with keratinocyte migration (22, 41-42), MMP-3 plays a pivotal role in formation of a basement membrane whereas MMP-2 and MMP-9 are essential for degradation of denatured collagen and granulation tissue formation (43-44).”
BackgroundRossi, P. F., dos Santos, F. V., Alves, A. L. M. M., Semensato, L. H., Oliveira, L. F. R., Santos, D. M. D., Bianchi, T., Inada, N. M., Filho, S. P. C., Oréfice, R. L., et al. (2024) · ACS Applied Nano Materials · doi:10.1021/acsanm.4c03615 · Cited by 17
Jayasree, A., Mohandas, A., Seethalakshmy, S., et al. (2017) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.12.043 · Cited by 15
Dickson, R. A., Fleischer, T., Ekuadzi, E., et al. (2010) · Pharmacognosy Journal · doi:10.1016/s0975-3575(10)80007-0 · Cited by 14
“These neutrophils release the enzymes collagenase and elastase which are responsible for the destruction of the connective tissue matrix and important growth factors respectively.[4] Antimicrobial agents may prevent this occurring and may underlie their use in treating wounds.”
BackgroundMolekulare Grundlagen der Wundheilung bei diabetischem Fu�syndrom
Lobmann, R., Schultz, G. S., & Lehnert, H. (2003) · Medizinische Klinik - Intensivmedizin und Notfallmedizin · doi:10.1007/s00063-003-1260-2 · Cited by 14
Juneja, S. C. (2013) · Journal of Tissue Engineering · doi:10.1177/2041731413492741 · Cited by 14
Efficacy of Concentrated Surfactant-Based Wound Dressings in Wound Repair and Biofilm Reduction
Salisbury, A., Mayer, D., Chen, R., & Percival, S. L. (2018) · Advances in Wound Care · doi:10.1089/wound.2017.0782 · Cited by 13
Theoretical targets for TCDD: A bioinformatics approach
Olivero‐Verbel, J., Cabarcas-Montalvo, M., & Ortega-Zúñiga, C. A. (2010) · Chemosphere · doi:10.1016/j.chemosphere.2010.06.020 · Cited by 13
Tavakoli, F., Faramarzi, M., Salimnezhad, S., Jafari, B., Eslami, H., & MohammadPourTabrizi, B. (2024) · Clinical and Experimental Dental Research · doi:10.1002/cre2.865 · Cited by 12
“MMP ‐ 8 breaks the triple helix structure of collagen during collagen decomposition (Murphy & Knäuper, 1997) and increases the expression of this factor in neutrophils during wound healing inflammation (Nwomeh et al., 1999).”
BackgroundMinematsu, T., Huang, L., Ibuki, A., Nakagami, G., Akase, T., Sugama, J., Nagase, T., Yoshimura, K., & Sanada, H. (2011) · Biological Research For Nursing · doi:10.1177/1099800411410870 · Cited by 12
Basic Science of Wound Healing
Goldberg, S. R., & Diegelmann, R. F. (2016) · Springer eBooks · doi:10.1007/978-3-319-31991-9_14 · Cited by 15
Singh, H., Samani, D., Nambiar, N., Ghate, M., & Gangakhedkar, R. (2017) · Gene · doi:10.1016/j.gene.2017.12.061 · Cited by 11
Mitosis increases levels of secretory leukocyte protease inhibitor in keratinocytes
Lai, J., Borson, N. D., Strausbauch, M. A., et al. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.02.065 · Cited by 12
Human Skeletal Muscle Myoblast Culture in Aligned Bacterial Nanocellulose and Commercial Matrices
Mastrodimos, M. B., Jain, S., Badv, M., Shen, J., Montazerian, H., Meyer, C. E., Annabi, N., & Weiss, P. S. (2024) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.4c07612 · Cited by 11
A 'test and treat' strategy for elevated wound protease activity for healing in venous leg ulcers
Norman, G., Westby, M. J., Stubbs, N. C., Dumville, J. C., & Cullum, N. A. (2016) · Cochrane Database of Systematic Reviews · doi:10.1002/14651858.cd011753.pub2 · Cited by 12
The potential adverse effects of aromatase inhibitors on wound healing:in vitroandin vivoevidence
Howgate, D. J., Gamie, Z., Panteliadis, P., Bhalla, A., Mantalaris, A., & Tsiridis, E. E. (2009) · Expert Opinion on Drug Safety · doi:10.1517/14740330903190674 · Cited by 11
“Wound healing involves MMP activity and it is thought that the over-expression of MMP-2, -8 or -9 is related to the pathogenesis of non-healing wounds [98].”
BackgroundAn, F., Du, J., Cao, Y., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.15371 · Cited by 11
“Second, since MMP-8 is highly expressed in neutrophils, increased expression and activity of MMP-8 can reflect neutrophils (associated with the initial inflammatory stages of wound repair) in the fluids of healing wounds, and can influence the wound healing [14, 16].”
BackgroundPrinciples of Plastic and Reconstructive Surgery
Provost, P. J., & Bailey, J. V. (2011) · Elsevier eBooks · doi:10.1016/b978-1-4377-0867-7.00024-7 · Cited by 11
Mass-Encoded Reporters Reporting Proteolytic Activity from within the Extracellular Matrix
Dodt, K., Lamer, S., Drießen, M. D., et al. (2020) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.0c00691 · Cited by 11
Continuous topical irrigation for severely infected wound healing
Tao, Q., Ren, J., Ji, Z., et al. (2015) · Journal of Surgical Research · doi:10.1016/j.jss.2015.04.004 · Cited by 11
Biological wound matrices with native dermis-like collagen efficiently modulate protease activity
Tati, R., Nordin, S. L., Abdillahi, S. M., & Mörgelin, M. (2018) · Journal of Wound Care · doi:10.12968/jowc.2018.27.4.199 · Cited by 10
Kaur, K., Singh, A., Attri, S., Malhotra, D., Verma, A., Bedi, N., & Bedi, P. M. S. (2020) · IntechOpen eBooks · doi:10.5772/intechopen.92982 · Cited by 13
Snyder, R., Cullen, B., & Nisbet, L. (2012) · International Wound Journal · doi:10.1111/j.1742-481x.2012.01040.x · Cited by 10
Inflammation in Venous Disease
Coleridge-Smith, P., & Bergan, J. J. (2003) · Springer eBooks · doi:10.1007/978-2-8178-0761-4_25 · Cited by 10
Arey, M. L., Sullivan, B. R., Reinert, C. G., et al. (2007) · Cornea · doi:10.1097/ico.0b013e31814b1b19 · Cited by 10
A 'test and treat' strategy for elevated wound protease activity for healing in venous leg ulcers
Norman, G., Westby, M. J., Stubbs, N. C., Dumville, J. C., & Cullum, N. A. (2015) · Cochrane Database of Systematic Reviews · doi:10.1002/14651858.cd011753 · Cited by 10
Pathomechanism of chronic venous insufficiency and leg ulcer
Sándor, T. (2004) · Acta Physiologica Hungarica · doi:10.1556/aphysiol.91.2004.2.5 · Cited by 9
Osteoblasts and Fibroblasts Interaction with a Porcine Acellular Dermal Matrix Membrane
Felice, P., D’Amico, E., Pierfelice, T. V., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24043649 · Cited by 9
“MMP8 has been shown to be the predominant collagenase in healing skin wounds, with a 100-fold increase of MMP8 in chronic wounds compared with acute wounds [23].”
Ebaid, H., Abdel-Salam, B. K. A., Hassan, I., Al‐Tamimi, J., Metwalli, A., Rady, A. M., & Alhazza, I. M. (2020) · BioMed Research International · doi:10.1155/2020/3592425 · Cited by 9
“Neutrophils release significant amounts of enzymes such as collagenase [28] and elastase, which can alter the levels of important healing factors such as plateletderived growth factor (PDGF) and transforming growth factor beta (TGF-β) [29].”
BackgroundInsulin suppresses collagenase stimulatory effect of stratifin in dermal fibroblasts
Lam, E. C., Tredget, E. E., Marcoux, Y., Li, Y., & Ghahary, A. (2004) · Molecular and Cellular Biochemistry · doi:10.1023/b:mcbi.0000049156.82563.2d · Cited by 9
“The protein levels of MMP-1 are three-fold higher in chronic wound fluids than is observed for peak levels of fluids from healing dermal wounds [17].”
BackgroundMatrix metalloproteinase landscape in the imiquimod-induced skin inflammation mouse model
Noddeland, H. K., Canbay, V., Lind, M. L., Savickas, S., Jensen, L. B., Petersson, K., Malmsten, M., Koch, J., Keller, U. A. D., & Heinz, A. (2024) · Biochimie · doi:10.1016/j.biochi.2024.03.011 · Cited by 9
“In fi ltrating neutrophils in psoriasis lesions, in turn, express several in fl ammatory mediators including not only MMP-9, but also MMP-8, which mostly cleaves collagens [35].”
BackgroundPotential anti-inflammatory treatments for chronic wounds
McKelvey, K. J., Xue, M., Whitmont, K., et al. (2012) · Wound Practice & Research: Journal of the Australian Wound Management Association · Cited by 8
Re‐Epithelialization of Wounds
Larjava, H., Häkkinen, L., & Koivisto, L. (2012) · Wiley eBooks · doi:10.1002/9781118704509.ch5 · Cited by 8
Skurska, A., Dymicka-Piekarska, V., Milewski, R. J., et al. (2021) · Biomolecules · doi:10.3390/biom11050731 · Cited by 7
“Comparative studies evaluating acute and chronic wounds revealed distinctly different levels of two enzymes in question [25].”
BackgroundHow might we achieve oxygen balance in wounds?
Davis, P. J. (2007) · International Wound Journal · doi:10.1111/j.1742-481x.2007.00384.x · Cited by 7
Syzygium mundagam bark methanol extract restores skin to normal in diabetic wounded rats
Chandran, R., Abrahamse, H., Thangaraj, P., et al. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.07.114 · Cited by 7
Dysfunctional wound healing in chronic wounds
Stephens, P. (2011) · Elsevier eBooks · doi:10.1533/9780857093301.1.3 · Cited by 7
Biochemical Pathways of Wound Healing: Implications for Development of Disease‐Specific Diagnostics
Menke, N. B., & Diegelmann, R. F. (2006) · Advances in clinical chemistry · doi:10.1016/s0065-2423(05)41005-7 · Cited by 7
Culture confluence regulates gene expression of normal human keratinocytes
Lai, J., & Pittelkow, M. R. (2004) · Wound Repair and Regeneration · doi:10.1111/j.1067-1927.2004.12606.x · Cited by 7
Buerk, A. A., Vitello, W. A., & Laughlin, R. T. (2000) · Current Opinion in Orthopedics · doi:10.1097/00001433-200004000-00004 · Cited by 7
Proteolytic signaling in cutaneous wound healing
Kalogeropoulos, K., Bundgaard, L., & Keller, U. A. D. (2022) · Proteolytic Signaling in Health and Disease · doi:10.1016/b978-0-323-85696-6.00006-8 · Cited by 1
Harmon, K. A., Burnette, M. D., Avery, J. T., Kimmerling, K. A., & Mowry, K. C. (2024) · Journal of Tissue Engineering and Regenerative Medicine · doi:10.1155/2024/6632276 · Cited by 6
“Aberrant expressions of collagenases (MMP-1, -8, and -13) and gelatinases (MMP-2 and -9) are hallmarks of the chronic wound microenvironment, with MMP-8 levels often being highly elevated due to continual neutrophil recruitment in the infammatory state [37].”
Suppression by an RAR-γ Agonist of Collagen Degradation Mediated by Corneal Fibroblasts
Kimura, K., Zhou, H., Orita, T., Kobayashi, M., Nishida, T., & Sonoda, K. (2017) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.15-18701 · Cited by 6
Alves, A., Attik, N., Bayon, Y., Royet, E., Wirth, C., Bourges, X., Piat, A., Dolmazon, G., Clermont, G., Boutrand, J.-P., et al. (2018) · Biomedical Materials · doi:10.1088/1748-605x/aaa9d4 · Cited by 6
“It has been demonstrated than in delayed healing, the inflammatory cells in excess release significant amounts of enzymes such as collagenase (matrix metalloproteinase-8) destroying the connective tissue, or elastase able of eliminating critical growth factors such as PDGF and TGF-ß [43, 44].”
Jha, A., George, J. P., & Chandrashekhar, G. (2019) · PubMed · Cited by 6
Sipponen, A. (2013) · Työväentutkimus Vuosikirja · Cited by 6
Leg Ulcers: Biochemical Factors
Smith, P. D. C. (2000) · Phlebology The Journal of Venous Disease · doi:10.1177/026835550001500315 · Cited by 6
“In another study chronic non-healing ulcers were found to contain increased levels of MMP-l and MMP-8 and decreased amounts of TIMP-l [29].”
BackgroundMatrix metalloproteinases in chronic rhinosinusitis
Huang, Y., Yan, B., Chen, M., Zhang, L., & Wang, C. (2024) · Expert Review of Clinical Immunology · doi:10.1080/1744666x.2024.2302362 · Cited by 6
“MMP-8, also known as collagenase 2, is typically found in wound-healing skin [92].”
BackgroundChen, S., Fan, Y., Wu, Q., et al. (2024) · Archives of Medical Research · doi:10.1016/j.arcmed.2024.103072 · Cited by 5
Biological Reasons for an Incisional Hernia
Bellón, J. M. (2007) · Springer eBooks · doi:10.1007/978-3-540-68988-1_16 · Cited by 5
Proteomic Approaches for Studying the Phases of Wound Healing
Edsberg, L. E. (2009) · Studies in mechanobiology, tissue engineering and biomaterials · doi:10.1007/978-3-642-00534-3_15 · Cited by 5
“Nwomeh et al. ( 30 ) used ELISA to measure MMP-1, MMP-8, and TIMP-1 in healing acute experimental wounds in humans, as well as non-healing pressure ulcers and venous ulcers, and reported that MMP-8 was significantly greater in healing wounds than MMP-1.”
BackgroundMethodResultInfluentialHeparan Sulfate Proteoglycan Mimetics Promote Tissue Regeneration: An Overview
van, J., Tuk, B., Barritault, D., & Tong, M. (2012) · InTech eBooks · doi:10.5772/25622 · Cited by 6
Sucrose Octasulfat – Evidenz in der Behandlung chronischer Wunden
Dissemond, J., Augustin, M., Dietlein, M., Keuthage, W., Läuchli, S., Lobmann, R., Münter, K., Stücker, M., Traber, J., Vanscheidt, W., et al. (2020) · Der Hautarzt · doi:10.1007/s00105-020-04637-9 · Cited by 5
Dik, B., Baş, A. L., & Yazıhan, N. (2016) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/cjpp-2016-0439 · Cited by 5
The Physiology of Wound Bed Preparation
Schultz, G. S. (2007) · CRC Press eBooks · doi:10.3109/9780849382550-2 · Cited by 5
Photodynamic therapy based on curcumin-mediated nanomedicines for wound healing
Alexeree, S. M. I. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-22027-2.00029-4 · Cited by 4
Khan, O. F., Jean‐François, J., & Sefton, M. V. (2009) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.32634 · Cited by 4
Lin, S., Xu, H., Xiao, J., Liu, Y., Zhang, Y., Cai, L., Li, X., & Tan, Y. (2009) · Eisei kagaku · doi:10.1248/jhs.55.910 · Cited by 4
Decellularization of Skin Tissue
Naveen Kumar, C. P., Kumar, V., Purohit, S., et al. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-82735-9_15 · Cited by 4
Correlations between different protein species of oral rinse MMP‐8 and patient‐related factors
Leppilahti, J. M., Tervahartiala, T. I., Kautiainen, H., et al. (2023) · Clinical and Experimental Dental Research · doi:10.1002/cre2.803 · Cited by 4
“MMP ‐ 8 is not only involved in pathologic tissue destruction but also in physiologic tissue modeling and remodeling as well as tissue repair (Nwomeh et al., 1999; Pirilä et al., 2007).”
BackgroundEfficiency of Silicate-Based Composites in the Healing Process of Diabetic Wound
Rajaei, M., Eslami, H., Zare‐Zardini, H., Ansari, M., & Akbari, N. (2024) · BioNanoScience · doi:10.1007/s12668-024-01314-2 · Cited by 4
“Therefore, the level of secretion of proteolytic enzymes in the wound increases [18].”
Impaired Wound Healing in Diabetes Mellitus
Kwon, M. J., & Park, J. H. (2009) · Korean Diabetes Journal · doi:10.4093/kdj.2009.33.2.83 · Cited by 4
The physiology of wound bed preparation
Schultz, G. S. (2012) · CRC Press eBooks · doi:10.3109/9781841849270-4 · Cited by 4
Principles of Reconstructive and Plastic Surgery
Bailey, J. V. (2006) · Elsevier eBooks · doi:10.1016/b1-41-600123-9/50026-7 · Cited by 4
Dodt, K., Drießen, M. D., Lamer, S., Schlösser, A., Lühmann, T. C., & Meinel, L. (2020) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.0c01134 · Cited by 4
Treatment of Pressure Ulcers with Noncontact Normothermic Wound Therapy
Whitney, J. D., Salvadalena, G., Higa, L., et al. (2001) · Journal of Wound Ostomy and Continence Nursing · doi:10.1097/00152192-200109000-00007 · Cited by 4
Peptides and Wound Healing: From Monomer to Combination
Liu, C., Yang, Q., & Zhou, Y. L. (2024) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-024-10627-5 · Cited by 3
“They are able to degrade collagen and growth factors that can promote wound healing to cause wound healing abnormalities (Lobmann et al. 2005, 2002; Nwomeh et al. 1999; Sun et al. 2023; Ongenae et al. 2000).”
Human fingertip regeneration follows clinical phases with distinct proteomic signatures
Schultz, J., Patel, P. A., Aires, R., et al. (2025) · npj Regenerative Medicine · doi:10.1038/s41536-025-00441-y · Cited by 3
“A detailed description of chemicals, instrumentation, and software parameters are provided in Tables 3 – 5.”
Matrix metalloproteinase inhibition and antibiotics in the treatment of chronic wounds
Naidoo, C. C. (2009) · Cited by 3
Percival, S., & Cutting, K. (2010) · CRC Press eBooks · doi:10.1201/9781420079944-13 · Cited by 3
Kumar, P., Mishra, S., & Singh, S. (2017) · Journal des Anti-infectieux · doi:10.1016/j.antinf.2017.01.002 · Cited by 3
Wounds, Enzymes, and Proteases
Percival, S. L., & Cochrane, C. A. (2010) · CRC Press eBooks · doi:10.1201/9781420079944-c9 · Cited by 3
Matrix Metalloproteinase 14 in Corneal Neovascularization
Qin, K., Setter, N. W., Yu, L., Vasi, Z., Wu, W., Hwang, Y., Lee, H., Chang, J., Rosenblatt, M. I., Han, K., et al. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27042027 · Cited by 2
Tokmakova, A. Y., Zaytseva, E. L., Doronina, L. P., et al. (2015) · Terapevticheskii arkhiv · doi:10.17116/terarkh2015871072-79 · Cited by 2
Moore, A. L., Marshall, C. D., Nauta, A., Lorenz, H. P., & Longaker, M. T. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-809880-6.00005-9 · Cited by 2
The Role of E-Cadherin-Catenin Complex in Prostate Cancer Progression
Anuradha, K., & James, S. (2013) · InTech eBooks · doi:10.5772/52751 · Cited by 2
“However, unregulated expression of MMP-8 is associated with chronic leg ulcers (Armstrong and Jude, 2002; Nwomeh et al., 1999).”
BackgroundStrategy of Surgical Management of Peripheral Neuropathy Form of Diabetic Foot Syndrome in Ghana
Rdeini, W. M., Agbenorku, P., & Mitish, V. A. (2014) · Plastic Surgery International · doi:10.1155/2014/185023 · Cited by 2
“It helped to reduce the rate of infection and provided an ideal healing environment by converting chronic wounds into acute; it also helped to reduce chronic inflammatory by-products as demonstrated by other authors in their studies [33–35].”
Extracellular Matrix and Other Factors that Impact on Cutaneous Scarring
Zhao, R., Jackson, C., & Xue, M. (2018) · Recent clinical techniques, results, and research in wounds · doi:10.1007/15695_2018_132 · Cited by 2
Grigsby, J. G., & Derbel, F. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.83159 · Cited by 2
Preparation of the Wound Bed of the Diabetic Foot Ulcer
Falanga, V. (2007) · Humana Press eBooks · doi:10.1007/978-1-59745-075-1_15 · Cited by 2
“In contrast, it has been suggested that excessive activity (or maldistribution) of other enzymes (MMP-2, MMP-8, MMP-9) contribute to healing impairment (30, 31 ).”
BackgroundBiological Activity and Implications of the Metalloproteinases in Diabetic Foot Ulcers
la Rosa, C. C.-D., Veloz, I. G., Cardenas‐Vargas, E., Castañeda-Miranda, R., Solís-Sánchez, L. O., Ortiz-Rodriguez, J. M., Vega-Carrillo, H. R., Martínez-Blanco, M. D. R., Flores‐Morales, V., Hernandez-Delgadillo, G. P., et al. (2017) · InTech eBooks · doi:10.5772/intechopen.71725 · Cited by 2
“Chronic wounds, including venous leg ulcers (VLUs) [40, 61, 62], DFUs [63, 64], PUs [65] dehiscent surgical wounds and acute wounds that have become chronic, were found to have elevated MMP activity.”
BackgroundMäkitalo, L. (2010) · Työväentutkimus Vuosikirja · Cited by 2
Non-invasive optical technologies to monitor wound healing
Zhu, L., & Papazoglou, E. S. (2007) · doi:10.17918/etd-2757 · Cited by 2
Current Trends in the Development of Wound Dressings, Biomaterials and Devices
Banerjee, A., & Bhattacharyya, J. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820352-1.00117-6 · Cited by 2
Metadata
- Authors
- Nwomeh, B. C., Liang, H.-X., Cohen, I. K., & Yager, D. R.
- Affiliations
- Virginia Commonwealth University (US)
- ORCID
- Nwomeh, Benedict C.
- Venue
- Journal of Surgical Research
- Publisher
- Elsevier BV
- Published
- 1999-02
- Volume
- 81
- Issue
- 2
- Pages
- 189-195
- ISSN
- 0022-4804 (ISSN-L)
- OpenAlex
- W1988325190
- Cited by
- 357
- References
- 0
- Citations by year
- 2026: 6 · 2025: 9 · 2024: 14 · 2023: 8 · 2022: 8 · 2021: 11 · 2020: 13 · 2019: 10 · 2018: 18 · 2017: 18 · 2016: 18 · 2015: 14 · 2014: 9 · 2013: 15 · 2012: 20
- FWCI
- 12.03
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Surgical Research (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (GM20298)
- Topics
- Health Sciences › Medicine › Surgery › Wound Healing and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Pineapple and bromelain studies
- Keywords
- MMP-8, MMP-1, TIMP-1, collagenase, wound healing, chronic non-healing ulcers, pressure ulcers, collagen degradation, extracellular matrix, neutrophils, matrix metalloproteinases, collagenolytic activity
- MeSH terms
- Adult, Chronic Disease, Pressure Ulcer, Enzyme-Linked Immunosorbent Assay, Female, Humans, Male, Mastectomy, Middle Aged, Skin, Surgical Flaps, Time Factors, Varicose Ulcer, Wound Healing, Wounds and Injuries, Collagenases, Tissue Inhibitor of Metalloproteinase-1, Matrix Metalloproteinase 1, Matrix Metalloproteinase 8
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review