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Laminins: Roles and Utility in Wound Repair
Open accessAbstract
Significance: Laminins are complex extracellular macromolecules that are major players in the control of a variety of core cell processes, including regulating rates of cell proliferation, differentiation, adhesion, and migration. Laminins, and related extracellular matrix components, have essential roles in tissue homeostasis; however, during wound healing, the same proteins are critical players in re-epithelialization and angiogenesis. Understanding how these proteins influence cell behavior in these different conditions holds great potential in identifying new strategies to enhance normal wound closure or to treat chronic/nonhealing wounds. Recent Advances: Laminin-derived bioactive peptides and, more recently, laminin-peptide conjugated scaffolds, have been designed to improve tissue regeneration after injuries. These peptides have been shown to be effective in decreasing inflammation and granulation tissue, and in promoting re-epithelialization, angiogenesis, and cell migration. Critical Issues: Although there is now a wealth of knowledge concerning laminin form and function, there are still areas of some controversy. These include the relative contribution of two laminin-based adhesive devices (focal contacts and hemidesmosomes) to the re-epithelialization process, the impact and implications of laminin proteolytic processing, and the importance of laminin polymer formation on cell behavior. In addition, the roles in wound healing of the laminin-related proteins, netrins, and LaNts are still to be fully defined. Future Directions: The future of laminin-based therapeutics potentially lies in the bioengineering of specific substrates to support laminin deposition for ex vivo expansion of autologous cells for graft formation and transplantation. Significant recent advances suggest that this goal is within sight.
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“Keratinocytes themselves further activate fibroblasts in a feedback loop through the production of fibronectin, tenascin C, and laminin 332 (Fig. 2) [93].”
From Immunology of Wound Healing (2018) · cites this paper as [93]
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A simplified laminin nomenclature
Aumailley, M., Bruckner‐Tuderman, L., Carter, W. G., Deutzmann, R., EDGAR, D., Ekblom, P., Engel, J., Engvall, E., Hohenester, E., & Jones, J. (2005) · Matrix Biology · doi:10.1016/j.matbio.2005.05.006 · Cited by 928
Beningo, K. A., Dembo, M., Kaverina, I., Small, J. V., & Wang, Y. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.4.881 · Cited by 750
Supramolecular assembly of basement membranes
Timpl, R., & Brown, J. C. (1996) · BioEssays · doi:10.1002/bies.950180208 · Cited by 701
Miner, J. H., Patton, B. L., Lentz, S. I., Gilbert, D. J., Snider, W. D., Jenkins, N. A., Copeland, N. G., & Sanes, J. R. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.137.3.685 · Cited by 650
Expression and Function of Laminins in the Embryonic and Mature Vasculature
Hallmann, R., Horn, N., Selg, M., Wendler, O., Pausch, F., & Sorokin, L. M. (2005) · Physiological Reviews · doi:10.1152/physrev.00014.2004 · Cited by 597
Miner, J. H., Cunningham, J. M., & Sanes, J. R. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.6.1713 · Cited by 491
Laminins in basement membrane assembly
Hohenester, E., & Yurchenco, P. D. (2013) · Cell Adhesion & Migration · doi:10.4161/cam.21831 · Cited by 478
Laminin-nidogen complex. Extraction with chelating agents and structural characterization
Paulsson, M., Aumailley, M., Deutzmann, R., Timpl, R., Beck, K., & ENGEL, J. (1987) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1987.tb13476.x · Cited by 450
Functional Diversity of Laminins
Domogatskaya, A., Rodin, S., & Tryggvason, K. (2012) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-101011-155750 · Cited by 396
Deletion of the Laminin α4 Chain Leads to Impaired Microvessel Maturation
Thyboll, J., Kortesmaa, J., Cao, R., Soininen, R., Wang, L., Iivanainen, A., Sorokin, L. M., Risling, M., Cao, Y., & Tryggvason, K. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.4.1194-1202.2002 · Cited by 349
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Ellis, S., Lin, E. J., & Tartar, D. (2018) · Current Dermatology Reports · doi:10.1007/s13671-018-0234-9 · Cited by 625
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Ishihara, J., Ishihara, A., Fukunaga, K., Sasaki, K., White, M. J. V., Briquez, P. S., & Hubbell, J. A. (2018) · Nature Communications · doi:10.1038/s41467-018-04525-w · Cited by 244
Klimek, K., & Ginalska, G. (2020) · Polymers · doi:10.3390/polym12040844 · Cited by 220
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Zhu, Y., Cankova, Z., Iwanaszko, M., Lichtor, S., Mrksich, M., & Ameer, G. A. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1804262115 · Cited by 165
Mohsin, F., Javaid, S., Tariq, M., & Mustafa, M. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.112713 · Cited by 153
Fragments generated upon extracellular matrix remodeling: Biological regulators and potential drugs
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Costa, A., Naranjo, J. D., Londono, R., & Badylak, S. F. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a025676 · Cited by 135
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Xiao, H., Chen, X., Liu, X., Wen, G., & Yu, Y. (2023) · Materials Today Bio · doi:10.1016/j.mtbio.2023.100589 · Cited by 124
Vilaça-Faria, H., Noro, J., Reis, R. L., & Pirraco, R. P. (2024) · Bioactive Materials · doi:10.1016/j.bioactmat.2024.01.004 · Cited by 114
Lei, J. L., Priddy, L. B., Lim, J. J., Massee, M., & Koob, T. J. (2016) · Advances in Wound Care · doi:10.1089/wound.2016.0699 · Cited by 109
‘Smart’ wound dressings for advanced wound care: a review
O'Callaghan, S., Galvin, P., O'Mahony, C., Moore, Z. E. H., & Derwin, R. (2020) · Journal of Wound Care · doi:10.12968/jowc.2020.29.7.394 · Cited by 90
Yang, D. H., Seo, D. I., Lee, D., Bhang, S. H., Park, K., Jang, G., Kim, C. H., & Chun, H. J. (2017) · Journal of Industrial and Engineering Chemistry · doi:10.1016/j.jiec.2017.05.007 · Cited by 84
Tyeb, S., Shiekh, P. A., Verma, V., & Kumar, A. (2019) · Biomacromolecules · doi:10.1021/acs.biomac.9b01355 · Cited by 78
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Piperigkou, Z., Götte, M., Theocharis, A. D., & Karamanos, N. K. (2017) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2017.10.008 · Cited by 72
Etich, J., Koch, M., Wagener, R., Zaucke, F., Fabri, M., & Brachvogel, B. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20205086 · Cited by 64
Fischer, N. G., & Aparicio, C. (2022) · Bioactive Materials · doi:10.1016/j.bioactmat.2022.03.019 · Cited by 68
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Jeong, S., Yoon, S., Kim, S., Jung, J., Kor, M., Shin, K., Lim, C., Han, H. S., Lee, H., Park, K.-Y., et al. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms21010073 · Cited by 66
Smart Carriers and Nanohealers: A Nanomedical Insight on Natural Polymers
Raveendran, S., Rochani, A., Maekawa, T., & Kumar, D. S. (2017) · Materials · doi:10.3390/ma10080929 · Cited by 54
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Yu, Y., Xiao, H., Tang, G., Wang, H., Shen, J., Sun, Y., Wang, S., Kong, W., Chai, Y., Liu, X., et al. (2023) · Materials Today Bio · doi:10.1016/j.mtbio.2023.100725 · Cited by 47
Ghasempour, A., Dehghan, H., Mahmoudi, M., & Arab, F. L. (2024) · Stem Cell Research & Therapy · doi:10.1186/s13287-024-04012-8 · Cited by 51
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Zhang, W., Zhang, S., Zhang, W., Yue, Y., Qian, W., & Wang, Z. (2021) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2021.188583 · Cited by 45
Valera, F. C. P., Ruffin, M., Adam, D., Maillé, É., Ibrahim, B., Bérubé, J., Rousseau, S., Brochiero, E., & Desrosiers, M. Y. (2018) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2018.05.035 · Cited by 44
Bullard, J. D., Lei, J. L., Lim, J. J., Massee, M., Fallon, A. M., & Koob, T. J. (2018) · Journal of Biomedical Materials Research Part B Applied Biomaterials · doi:10.1002/jbm.b.34196 · Cited by 43
Dobre, O., Gonzalez‐Oliva, M. A., Ciccone, G., Trujillo, S., Rodrigo‐Navarro, A., Venters, D. C., Llopis-Hernández, V., Vassalli, M., González‐García, C., Dalby, M. J., et al. (2021) · Advanced Functional Materials · doi:10.1002/adfm.202010225 · Cited by 43
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Qu, H., Tian, M., Wang, Y., Tan, L., Huang, B., Zhang, L., Liu, X., Long, M., Zhang, R., Liao, X., et al. (2021) · Diabetes · doi:10.2337/db20-1008 · Cited by 32
Zhang, J., Wang, H., Wang, Y., Dong, W., Jiang, Z., & Yang, G. (2017) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2017.10.030 · Cited by 31
Wenta, T., Nastały, P., Lipińska, B., & Manninen, A. (2024) · Matrix Biology · doi:10.1016/j.matbio.2024.10.007 · Cited by 33
Jia, J., Jeon, E. J., Mei, L., Richards, D., Lee, S., Jung, Y., Barrs, R. W., Coyle, R. C., Li, X., Chou, C. J., et al. (2020) · Science Advances · doi:10.1126/sciadv.aaz5894 · Cited by 30
Oliveira, H., Medina, C. F., Stachowicz, M., dos Santos, B. P., Chagot, L., Dusserre, N., & Fricain, J. (2021) · Bioprinting · doi:10.1016/j.bprint.2021.e00134 · Cited by 32
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Pogozhykh, O., Hofmann, N., Gryshkov, O., von Kaisenberg, C., Mueller, M., Glasmacher, B., Pogozhykh, D., Börgel, M., Blasczyk, R., & Figueiredo, C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21114029 · Cited by 27
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Bagulho, A., Vilas‐Boas, F., Pena, A., Peneda, C., Santos, F. C., Jerónimo, A., de Almeida, R. F. M., & Real, C. (2015) · Redox Biology · doi:10.1016/j.redox.2015.09.006 · Cited by 26
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RetractedVachiramon, V., Pavicic, T., Casabona, G., Green, J. B., Levine, J., Park, J., Spada, J., Muniz, M., Akers, J., Jackson, M. J., et al. (2024) · Journal of Cosmetic Dermatology · doi:10.1111/jocd.16658 · Cited by 28
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Aellos, F., Grauer, J. A., Harder, K. G., Dworan, J. S., Fabbri, G., Cuevas, P. L., Yuan, X., Liu, B., Brunski, J., & Helms, J. A. (2024) · Journal Of Clinical Periodontology · doi:10.1111/jcpe.13980 · Cited by 13
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Avila-Martinez, N., Gansevoort, M., Verbakel, J., Haarshaadri, J., Araújo, I. M., Vitorino, M., Tiscórnia, G., Kuppevelt, T. H. V., & Daamen, W. F. (2023) · Biomaterials Science · doi:10.1039/d3bm00835e · Cited by 15
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Giovani, P. A., Salmon, C. R., Martins, L., Leme, A. F. P., Rebouças, P. D., Puppin‐Rontani, R. M., Mofatto, L. S., Sallum, E. A., Nociti, F. H., & Kantovitz, K. R. (2016) · PLoS ONE · doi:10.1371/journal.pone.0154957 · Cited by 11
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Metadata
- Authors
- Iorio, V., Troughton, L. D., & Hamill, K. J.
- Affiliations
- University of Liverpool (GB)
- Corresponding author
- Hamill, Kevin J.
- Venue
- Advances in Wound Care
- Publisher
- SAGE Publications
- Published
- 2015-04
- Volume
- 4
- Issue
- 4
- Pages
- 250-263
- ISSN
- 2162-1918 (ISSN-L)
- 2162-1934
- PMC
- PMC4397997
- OpenAlex
- W2315246287
- Cited by
- 169
- References
- 120
- Citations by year
- 2026: 14 · 2025: 11 · 2024: 23 · 2023: 23 · 2022: 13 · 2021: 17 · 2020: 23 · 2019: 8 · 2018: 16 · 2017: 12 · 2016: 6 · 2015: 3
- FWCI
- 0.87
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Advances in Wound Care (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- British Skin Foundation
- University of Liverpool
- Biotechnology and Biological Sciences Research Council (BB/L020513/1)
- Topics
- Health Sciences › Medicine › Surgery › Wound Healing and Treatments
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Health Sciences › Medicine › Surgery › Tissue Engineering and Regenerative Medicine
- Keywords
- laminin, wound healing, re-epithelialization, angiogenesis, chronic wounds, focal adhesions, hemidesmosomes, netrin, cell migration, cell adhesion, tissue regeneration, ex vivo cell expansion
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