Cited by 96Wound Healing and TreatmentsElectrospun Nanofibers in Biomedical ApplicationsSilk-based biomaterials and applications

Keratin Biomaterials in Skin Wound Healing, an Old Player in Modern Medicine: A Mini Review

Open access
Konop, Marek, Rybka, Mateusz, Drapała, Adrian·2021·Pharmaceutics

Abstract

Impaired wound healing is a major medical problem. To solve it, researchers around the world have turned their attention to the use of tissue-engineered products to aid in skin regeneration in case of acute and chronic wounds. One of the primary goals of tissue engineering and regenerative medicine is to develop a matrix or scaffold system that mimics the structure and function of native tissue. Keratin biomaterials derived from wool, hair, and bristle have been the subjects of active research in the context of tissue regeneration for over a decade. Keratin derivatives, which can be either soluble or insoluble, are utilized as wound dressings since keratins are dynamically up-regulated and needed in skin wound healing. Tissue biocompatibility, biodegradability, mechanical durability, and natural abundance are only a few of the keratin biomaterials’ properties, making them excellent wound dressing materials to treat acute and chronic wounds. Several experimental and pre-clinical studies described the beneficial effects of the keratin-based wound dressing in faster wound healing. This review focuses exclusively on the biomedical application of a different type of keratin biomaterials as a wound dressing in pre-clinical and clinical conditions.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.3390/pharmaceutics13122029

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

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?

  • The traditional practice of using animal horns for wound healing probably derives from keratin's ability to enhance tissue regeneration and wound closure.

    “this type of traditional practice probably derives from the well-documented ability of keratin to enhance tissue regeneration and wound closure (9) , (10)”

    From Efficacy of Carabao Horn Powder as an Organic Ingredient in Soap Production (2026) · cites this paper as [9]

    The Introduction and Concluding Remarks report that keratin-based wound dressings can enhance healing, epithelialization, and tissue recovery. The review does not address the traditional use of animal horns or establish that keratin’s effects explain that practice; that proposed connection remains unsupported by this source. (LLM, conf=0.84)

    Experimental — accuracy not yet measured
  • The marginally positive shift in pH with higher concentration of horn powder indicates that the basicity of the soap is stabilized by a constituent of the alkaline entity of keratinous material.

    “The marginally positive shift in pH with higher concentration of horn powder indicates that the basicity of the soap is stabilized by a constituent of the alkaline entity of keratinous material, an observation reported in research on the biochemical stability of biomaterials derived from keratin (9) , (10)”

    From Efficacy of Carabao Horn Powder as an Organic Ingredient in Soap Production (2026) · cites this paper as [9]

    Section 5, “Biomedical Properties of Keratin” (page unavailable), discusses the water stability of a keratin-containing hydrogel, while its antibacterial subsection discusses keratin’s functional groups. Neither the supplied passages nor searches for horn powder, soap, pH, and alkalinity address whether horn powder stabilizes soap basicity. (LLM, conf=0.75)

    Experimental — accuracy not yet measured

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

Research works printed but not linked: 108

  1. [1]Ehrlich F. Lachner J. Hermann M. Tschachler E. Eckhart L. Convergent Evolution of Cysteine-Rich Keratins in Hard Skin Appendages of Terrestrial Vertebrates Mol. Biol. Evol. 2020 37 982 993 10.1093/molbev/msz279 31822906 PMC7086170 · DOI
  2. [2]Ehrlich F. Fischer H. Langbein L. Praetzel-Wunder S. Ebner B. Figlak K. Weissenbacher A. Sipos W. Tschachler E. Eckhart L. Differential Evolution of the Epidermal Keratin Cytoskeleton in Terrestrial and Aquatic Mammals Mol. Biol. Evol. 2019 36 328 340 10.1093/molbev/msy214 30517738 PMC6367960 · DOI
  3. [3]Vasconcelos A. Cavaco-Paulo A. The use of keratin in biomedical applications Curr. Drug Targets 2013 14 612 619 10.2174/1389450111314050010 23410124 · DOI
  4. [4]Shah A. Tyagi S. Bharagava R.N. Belhaj D. Kumar A. Saxena G. Saratale G.D. Mulla S.I. Keratin Production and Its Applications: Current and Future Perspective Keratin as a Protein Biopolymer: Extraction from Waste Biomass and Applications Sharma S. Kumar A. Springer International Publishing Cham, Switzerland 2019 19 34 978-3-030-02901-2
  5. [5]Shavandi A. Silva T.H. Bekhit A.A. Bekhit A.E.-D.A. Keratin: Dissolution, extraction and biomedical application Biomater. Sci. 2017 5 1699 1735 10.1039/C7BM00411G 28686242 · DOI
  6. [6]Gao J. Zhang L. Wei Y. Chen T. Ji X. Ye K. Yu J. Tang B. Sun X. Hu J. Human hair keratins promote the regeneration of peripheral nerves in a rat sciatic nerve crush model J. Mater. Sci. Mater. Med. 2019 30 82 10.1007/s10856-019-6283-1 31273463 PMC6609591 · DOI
  7. [7]Konop M. Czuwara J. Klodzinska E. Laskowska A.K. Zielenkiewicz U. Brzozowska I. Nabavi S.M. Rudnicka L. Development of a novel keratin dressing which accelerates full-thickness skin wound healing in diabetic mice: In vitro and in vivo studies J. Biomater. Appl. 2018 33 527 540 10.1177/0885328218801114 30227758 · DOI
  8. [8]Konop M. Sulejczak D. Czuwara J. Kosson P. Misicka A. Lipkowski A.W. Rudnicka L. The role of allogenic keratin-derived dressing in wound healing in a mouse model Wound Repair Regen. 2017 25 62 74 10.1111/wrr.12500 27997709 · DOI
  9. [9]Kurzepa K. Róycki K. Bochyñska M. Konop M. Urbanczyk-Lipkowska Z. Lipkowski A.W. Molecular scaffolds for three-dimensional cell and tissue cultures Polimery 2013 58 663 669 10.14314/polimery.2013.663 · DOI
  10. [10]Konop M. Czuwara J. Kłodzińska E. Laskowska A.K. Sulejczak D. Damps T. Zielenkiewicz U. Brzozowska I. Sureda A. Kowalkowski T. Evaluation of keratin biomaterial containing silver nanoparticles as a potential wound dressing in full-thickness skin wound model in diabetic mice J. Tissue Eng. Regen. Med. 2020 14 334 346 10.1002/term.2998 31825159 · DOI
  11. [11]Nasipuri P. Herschend J. Brejnrod A.D. Madsen J.S. Espersen R. Svensson B. Burmølle M. Jacquiod S. Sørensen S.J. Community-intrinsic properties enhance keratin degradation from bacterial consortia PLoS ONE 2020 15 e0228108 10.1371/journal.pone.0228108 32004342 PMC6994199 · DOI
  12. [12]Negut I. Grumezescu V. Grumezescu A.M. Treatment strategies for infected wounds Molecules 2018 23 2392 10.3390/molecules23092392 PMC6225154 30231567 · DOI
  13. [14]Swenty C.F. Principles to Guide Your Dressing Choice J. Nurse Pract. 2016 12 e125 e127 10.1016/j.nurpra.2015.12.006 · DOI
  14. [15]Ousey K. Cutting K.F. Rogers A.A. Rippon M.G. The importance of hydration in wound healing: Reinvigorating the clinical perspective J. Wound Care 2016 25 122 130 10.12968/jowc.2016.25.3.122 26947692 · DOI
  15. [16]Dhivya S. Padma V.V. Santhini E. Wound dressings—A review BioMedicine 2015 5 22 10.7603/s40681-015-0022-9 26615539 PMC4662938 · DOI
  16. [17]Qiu Y. Qiu L. Cui J. Wei Q. Bacterial cellulose and bacterial cellulose-vaccarin membranes for wound healing Mater. Sci. Eng. C 2016 59 303 309 10.1016/j.msec.2015.10.016 26652377 · DOI
  17. [18]Fan L. Yang H. Yang J. Peng M. Hu J. Preparation and characterization of chitosan/gelatin/PVA hydrogel for wound dressings Carbohydr. Polym. 2016 146 427 434 10.1016/j.carbpol.2016.03.002 27112893 · DOI
  18. [19]Dabiri G. Damstetter E. Phillips T. Choosing a Wound Dressing Based on Common Wound Characteristics Adv. Wound Care 2016 5 32 41 10.1089/wound.2014.0586 26858913 PMC4717498 · DOI
  19. [20]Ye S. Jiang L. Wu J. Su C. Huang C. Liu X. Shao W. Flexible Amoxicillin-Grafted Bacterial Cellulose Sponges for Wound Dressing: In Vitro and in Vivo Evaluation ACS Appl. Mater. Interfaces 2018 10 5862 5870 10.1021/acsami.7b16680 29345902 · DOI
  20. [21]RǍdulescu M. Holban A.M. MogoantǍ L. BǍlşeanu T.A. Mogoşanu G.D. Savu D. Popescu R.C. FufǍ O. Grumezescu A.M. Bezirtzoglou E. Fabrication, characterization, and evaluation of bionanocomposites based on natural polymers and antibiotics for wound healing applications Molecules 2016 21 761 10.3390/molecules21060761 PMC6273619 27294905 · DOI
  21. [22]Lin C.W. Chen Y.K. Tang K.C. Yang K.C. Cheng N.C. Yu J. Keratin scaffolds with human adipose stem cells: Physical and biological effects toward wound healing J. Tissue Eng. Regen. Med. 2019 13 1044 1058 10.1002/term.2855 30938939 · DOI
  22. [23]Roy D.C. Tomblyn S. Isaac K.M. Kowalczewski C.J. Burmeister D.M. Burnett L.R. Christy R.J. Ciprofloxacin-loaded keratin hydrogels reduce infection and support healing in a porcine partial-thickness thermal burn Wound Repair Regen. 2016 24 657 668 10.1111/wrr.12449 27238250 · DOI
  23. [24]Gupta A. Briffa S.M. Swingler S. Gibson H. Kannappan V. Adamus G. Kowalczuk M. Martin C. Radecka I. Synthesis of Silver Nanoparticles Using Curcumin-Cyclodextrins Loaded into Bacterial Cellulose-Based Hydrogels for Wound Dressing Applications Biomacromolecules 2020 21 1802 1811 10.1021/acs.biomac.9b01724 31967794 PMC7588018 · DOI
  24. [25]Pang S. Gao Y. Wang F. Wang Y. Cao M. Zhang W. Liang Y. Song M. Jiang G. Toxicity of silver nanoparticles on wound healing: A case study of zebrafish fin regeneration model Sci. Total Environ. 2020 717 137178 10.1016/j.scitotenv.2020.137178 32062274 · DOI
  25. [26]Boer M. Duchnik E. Maleszka R. Marchlewicz M. Structural and biophysical characteristics of human skin in maintaining proper epidermal barrier function Postep. Dermatol. Alergol. 2016 33 1 5 10.5114/pdia.2015.48037 PMC4793052 26985171 · DOI
  26. [27]Lai-Cheong J.E. McGrath J.A. Structure and function of skin, hair and nails Medicine 2017 45 347 351 10.1016/j.mpmed.2017.03.004 · DOI
  27. [28]Joffe R. Plaza J.A. Kajoian A. Tip Chapter: Histology and Physiology of the Skin Minimally Invasive Aesthetic Procedures: A Guide for Dermatologists and Plastic Surgeons Da Costa A. Springer International Publishing Cham, Switzerland 2020 179 192 978-3-319-78265-2
  28. [29]Gantwerker E.A. Hom D.B. Skin: Histology and physiology of wound healing Clin. Plast. Surg. 2012 39 85 97 10.1016/j.cps.2011.09.005 22099852 · DOI
  29. [30]Fuchs E. Epithelial Skin Biology. Three Decades of Developmental Biology, a Hundred Questions Answered and a Thousand New Ones to Address Current Topics in Developmental Biology Elsevier Amsterdam, The Netherlands 2016 9780128029565 PMC5026047 26970628
  30. [31]Baroni A. Buommino E. De Gregorio V. Ruocco E. Ruocco V. Wolf R. Structure and function of the epidermis related to barrier properties Clin. Dermatol. 2012 30 257 262 10.1016/j.clindermatol.2011.08.007 22507037 · DOI
  31. [32]McMillan J.R. Akiyama M. Shimizu H. Epidermal basement membrane zone components: Ultrastructural distribution and molecular interactions J. Dermatol. Sci. 2003 31 169 177 10.1016/S0923-1811(03)00045-8 12727020 · DOI
  32. [33]Bruckner-Tuderman L. Has C. Disorders of the cutaneous basement membrane zone-The paradigm of epidermolysis bullosa Matrix Biol. 2014 33 29 34 10.1016/j.matbio.2013.07.007 23917088 · DOI
  33. [34]Chan L.S. Human skin basement membrane in health and in autoimmune diseases Front. Biosci. 1997 2 343 352 10.2741/A196 9232815 · DOI
  34. [35]Lai-Cheong J.E. Arita K. McGrath J.A. Genetic diseases of junctions J. Investig. Dermatol. 2007 127 2713 2725 10.1038/sj.jid.5700727 18007692 · DOI
  35. [36]Uitto J. Has C. Vahidnezhad H. Youssefian L. Bruckner-Tuderman L. Molecular pathology of the basement membrane zone in heritable blistering diseases: The paradigm of epidermolysis bullosa Matrix Biol. 2017 57 76 85 10.1016/j.matbio.2016.07.009 27496350 · DOI
  36. [37]Daniel B.S. Murrell D.F. Review of autoimmune blistering diseases: The Pemphigoid diseases J. Eur. Acad. Dermatol. Venereol. 2019 33 1685 1694 10.1111/jdv.15679 31087464 · DOI
  37. [38]Didona D. Maglie R. Eming R. Hertl M. Pemphigus: Current and future therapeutic strategies Front. Immunol. 2019 10 1418 10.3389/fimmu.2019.01418 31293582 PMC6603181 · DOI
  38. [40]Rippa A.L. Kalabusheva E.P. Vorotelyak E.A. Regeneration of Dermis: Scarring and Cells Involved Cells 2019 8 607 10.3390/cells8060607 PMC6627856 31216669 · DOI
  39. [41]Woodley D.T. Distinct Fibroblasts in the Papillary and Reticular Dermis: Implications for Wound Healing Dermatol. Clin. 2017 35 95 100 10.1016/j.det.2016.07.004 27890241 · DOI
  40. [42]Dehdashtian A. Stringer T.P. Warren A.J. Mu E.W. Amirlak B. Shahabi L. Anatomy and Physiology of the Skin Melanoma: A Modern Multidisciplinary Approach Riker A.I. Springer International Publishing Cham, Switzerland 2018 15 26 978-3-319-78310-9
  41. [43]Singh V. Wang S. Ng K.W. 2.25 Keratin as a Biomaterial Comprehensive Biomaterials II Ducheyne P. Elsevier Oxford, UK 2017 542 557 978-0-08-100692-4
  42. [44]Pan X. Hobbs R.P. Coulombe P.A. The expanding significance of keratin intermediate filaments in normal and diseased epithelia Curr. Opin. Cell Biol. 2013 25 47 56 10.1016/j.ceb.2012.10.018 23270662 PMC3578078 · DOI
  43. [45]Heid H.W. Moll I. Franke W.W. Patterns of expression of trichocytic and epithelial cytokeratins in mammalian tissues. I. Human and bovine hair follicles Differentiation 1988 37 137 157 10.1111/j.1432-0436.1988.tb00805.x 2456239 · DOI
  44. [46]Heid H.W. Werner E. Franke W.W. The complement of native α-keratin polypeptides of hair-forming cells: A subset of eight polypeptides that differ from epithelial cytokeratins Differentiation 1986 32 101 119 10.1111/j.1432-0436.1986.tb00562.x 2431943 · DOI
  45. [47]Kitahara T. Ogawa H. Coexpression of keratins characteristic of skin and hair differentiation in nail cells J. Investig. Dermatol. 1993 100 171 175 10.1111/1523-1747.ep12462796 7679137 · DOI
  46. [48]Jacob J.T. Coulombe P.A. Kwan R. Omary M.B. Types I and II keratin intermediate filaments Cold Spring Harb. Perspect. Biol. 2018 10 a018275 10.1101/cshperspect.a018275 29610398 PMC5880164 · DOI
  47. [49]Oshima R.G. Apoptosis and keratin intermediate filaments Cell Death Differ. 2002 9 486 492 10.1038/sj.cdd.4400988 11973607 · DOI
  48. [50]Zhang X. Yin M. Zhang L.J. Keratin 6, 16 and 17-Critical Barrier Alarmin Molecules in Skin Wounds and Psoriasis Cells 2019 8 807 10.3390/cells8080807 31374826 PMC6721482 · DOI
  49. [51]Hobbs R.P. Lessard J.C. Coulombe P.A. Keratin intermediate filament proteins—Novel regulators of inflammation and immunity in skin J. Cell Sci. 2012 125 5257 5258 10.1242/jcs.122929 23377656 PMC3561851 · DOI
  50. [52]Wong P. Colucci-Guyon E. Takahashi K. Gu C. Babinet C. Coulombe P.A. Introducing a null mutation in the mouse K6α and K6β genes reveals their essential structural role in the oral mucosa J. Cell Biol. 2000 150 921 928 10.1083/jcb.150.4.921 10953016 PMC2175283 · DOI
  51. [53]Wong P. Coulombe P.A. Loss of keratin 6 (K6) proteins reveals a function for intermediate filaments during wound repair J. Cell Biol. 2003 276 75 81 10.1083/jcb.200305032 PMC2173512 14568992 · DOI
  52. [54]Rotty J.D. Coulombe P.A. A wound-induced keratin inhibits Src activity during keratinocyte migration and tissue repair J. Cell Biol. 2012 197 381 389 10.1083/jcb.201107078 22529101 PMC3341159 · DOI
  53. [55]Kim S. Wong P. Coulombe P.A. A keratin cytoskeletal protein regulates protein synthesis and epithelial cell growth Nature 2006 441 362 365 10.1038/nature04659 16710422 · DOI
  54. [56]Yang L. Jin L. Ke Y. Fan X. Zhang T. Zhang C. Bian H. Wang G. E3 ligase Trim21 ubiquitylates and stabilizes Keratin 17 to induce STAT3 nuclear transport in psoriasis J. Investig. Dermatol. 2018 138 2568 2577 10.1016/j.jid.2018.05.016 29859926 · DOI
  55. [57]Krzyszczyk P. Schloss R. Palmer A. Berthiaume F. The role of macrophages in acute and chronic wound healing and interventions to promote pro-wound healing phenotypes Front. Physiol. 2018 9 419 10.3389/fphys.2018.00419 29765329 PMC5938667 · DOI
  56. [58]Werner S. Keller L. Pantel K. Epithelial keratins: Biology and implications as diagnostic markers for liquid biopsies Mol. Asp. Med. 2020 72 100817 10.1016/j.mam.2019.09.001 31563278 · DOI
  57. [59]Kakkar P. Madhan B. Fabrication of keratin-silica hydrogel for biomedical applications Mater. Sci. Eng. C 2016 66 178 184 10.1016/j.msec.2016.04.067 27207052 · DOI
  58. [60]Husain M.S.B. Gupta A. Alashwal B.Y. Development of keratin based hydrogels for biomedical applications IOP Conference Series: Materials Science and Engineering IOP Publishing Bristol, UK 2019 Volume 702 012031 10.1088/1757-899x/702/1/012031 · DOI
  59. [61]Morais J.M. Papadimitrakopoulos F. Burgess D.J. Biomaterials/tissue interactions: Possible solutions to overcome foreign body response AAPS J. 2010 12 188 196 10.1208/s12248-010-9175-3 20143194 PMC2844517 · DOI · Paper page
  60. [62]Reichl S. Films based on human hair keratin as substrates for cell culture and tissue engineering Biomaterials 2009 30 6854 6866 10.1016/j.biomaterials.2009.08.051 19783297 · DOI
  61. [63]Zafar K. Jamal S. Ghafoor R. Bio-active cements-Mineral Trioxide Aggregate based calcium silicate materials: A narrative review J. Pak. Med. Assoc. 2020 70 497 504 10.5455/JPMA.16942 32207434 · DOI
  62. [64]Bochynska-Czyz M. Redkiewicz P. Kozlowska H. Matalinska J. Konop M. Kosson P. Can keratin scaffolds be used for creating three-dimensional cell cultures? Open Med. 2020 15 249 253 10.1515/med-2020-0031 32292820 PMC7147289 · DOI
  63. [65]Yamauchi K. Maniwa M. Mori T. Cultivation of fibroblast cells on keratin-coated substrata J. Biomater. Sci. Polym. Ed. 1998 9 259 270 10.1163/156856298X00640 9556761 · DOI
  64. [66]Park M. Shin H.K. Kim B.-S. Kim M.J. Kim I.-S. Park B.-Y. Kim H.-Y. Effect of discarded keratin-based biocomposite hydrogels on the wound healing process in vivo Mater. Sci. Eng. C 2015 55 88 94 10.1016/j.msec.2015.03.033 26117742 · DOI
  65. [67]Sadeghi S. Nourmohammadi J. Ghaee A. Soleimani N. Carboxymethyl cellulose-human hair keratin hydrogel with controlled clindamycin release as antibacterial wound dressing Int. J. Biol. Macromol. 2020 147 1239 1247 10.1016/j.ijbiomac.2019.09.251 31739046 · DOI
  66. [68]Prati C. Gandolfi M.G. Calcium silicate bioactive cements: Biological perspectives and clinical applications Dent. Mater. 2015 31 351 370 10.1016/j.dental.2015.01.004 25662204 · DOI
  67. [69]Bernard M. Jubeli E. Pungente M.D. Yagoubi N. Biocompatibility of polymer-based biomaterials and medical devices-regulations: In vitro screening and risk-management Biomater. Sci. 2018 6 2025 2053 10.1039/C8BM00518D 29968869 · DOI
  68. [70]Peplow P.V. Dias G.J. A study of the relationship between mass and physical strength of keratin bars in vivo J. Mater. Sci. Mater. Med. 2004 15 1217 1220 10.1007/s10856-004-5803-8 15880931 · DOI
  69. [71]Patrucco A. Visai L. Fassina L. Magenes G. Tonin C. Keratin-based matrices from wool fibers and human hair Materials for Biomedical Engineering: Biopolymer Fibers Elsevier Amsterdam, The Netherlands 2019 9780128168721
  70. [72]Placone J.K. Navarro J. Laslo G.W. Lerman M.J. Gabard A.R. Herendeen G.J. Falco E.E. Tomblyn S. Burnett L. Fisher J.P. Development and Characterization of a 3D Printed, Keratin-Based Hydrogel Ann. Biomed. Eng. 2017 45 237 248 10.1007/s10439-016-1621-7 27129371 · DOI
  71. [73]Khajavi R. Rahimi M.K. Abbasipour M. Brendjchi A.H. Antibacterial nanofibrous scaffolds with lowered cytotoxicity using keratin extracted from quail feathers J. Bioact. Compat. Polym. 2016 31 60 71 10.1177/0883911515598793 · DOI
  72. [74]Amajuoyi J.N. Ilomuanya M.O. Asantewaa-Osei Y. Azubuike C.P. Adeosun S.O. Igwilo C.I. Development of electrospun keratin/coenzyme Q10/poly vinyl alcohol nanofibrous scaffold containing mupirocin as potential dressing for infected wounds Future J. Pharm. Sci. 2020 6 25 10.1186/s43094-020-00043-z · DOI
  73. [75]He M. Chen M. Dou Y. Ding J. Yue H. Yin G. Chen X. Cui Y. Electrospun Silver Nanoparticles-Embedded Feather Keratin/Poly(vinyl alcohol)/Poly(ethylene oxide) Antibacterial Composite Nanofibers Polymers 2020 12 305 10.3390/polym12020305 PMC7077473 32028586 · DOI
  74. [77]Gu L.-H. Coulombe P.A. Keratin function in skin epithelia: A broadening palette with surprising shades Curr. Opin. Cell Biol. 2007 19 13 23 10.1016/j.ceb.2006.12.007 17178453 · DOI
  75. [78]Coulombe P.A. Kerns M.L. Fuchs E. Epidermolysis bullosa simplex: A paradigm for disorders of tissue fragility J. Clin. Investig. 2009 119 1784 1793 10.1172/JCI38177 19587453 PMC2701872 · DOI
  76. [79]Uttam J. Hutton E. Coulombe P.A. Anton-Lamprecht I. Yu Q.C. Gedde-Dahl T.J. Fine J.D. Fuchs E. The genetic basis of epidermolysis bullosa simplex with mottled pigmentation Proc. Natl. Acad. Sci. USA 1996 93 9079 9084 10.1073/pnas.93.17.9079 8799157 PMC38598 · DOI
  77. [80]Betz R.C. Planko L. Eigelshoven S. Hanneken S. Pasternack S.M. Bussow H. Van Den Bogaert K. Wenzel J. Braun-Falco M. Rutten A. Loss-of-function mutations in the keratin 5 gene lead to Dowling-Degos disease Am. J. Hum. Genet. 2006 78 510 519 10.1086/500850 16465624 PMC1380294 · DOI
  78. [81]Lugassy J. Itin P. Ishida-Yamamoto A. Holland K. Huson S. Geiger D. Hennies H.C. Indelman M. Bercovich D. Uitto J. Naegeli-Franceschetti-Jadassohn syndrome and dermatopathia pigmentosa reticularis: Two allelic ectodermal dysplasias caused by dominant mutations in KRT14 Am. J. Hum. Genet. 2006 79 724 730 10.1086/507792 16960809 PMC1592572 · DOI
  79. [82]Fitch K.R. McGowan K.A. van Raamsdonk C.D. Fuchs H. Lee D. Puech A. Hérault Y. Threadgill D.W. Hrabé de Angelis M. Barsh G.S. Genetics of dark skin in mice Genes Dev. 2003 17 214 228 10.1101/gad.1023703 12533510 PMC195979 · DOI
  80. [83]McGowan K.A. Aradhya S. Fuchs H. de Angelis M.H. Barsh G.S. A mouse keratin 1 mutation causes dark skin and epidermolytic hyperkeratosis J. Investig. Dermatol. 2006 126 1013 1016 10.1038/sj.jid.5700241 16528356 · DOI
  81. [84]McGowan K.A. Fuchs H. Hrabé de Angelis M. Barsh G.S. Identification of a Keratin 4 mutation in a chemically induced mouse mutant that models white sponge nevus J. Investig. Dermatol. 2007 127 60 64 10.1038/sj.jid.5700498 16858417 · DOI
  82. [85]Moll R. Franke W.W. Schiller D.L. Geiger B. Krepler R. The catalog of human cytokeratins: Patterns of expression in normal epithelia, tumors and cultured cells Cell 1982 31 11 24 10.1016/0092-8674(82)90400-7 6186379 · DOI
  83. [86]Omary M.B. Coulombe P.A. McLean W.H.I. Intermediate filament proteins and their associated diseases N. Engl. J. Med. 2004 351 2087 2100 10.1056/NEJMra040319 15537907 · DOI
  84. [87]Loan F. Cassidy S. Marsh C. Simcock J. Keratin-based products for effective wound care management in superficial and partial thickness burns injuries Burns 2016 42 541 547 10.1016/j.burns.2015.10.024 26787130 · DOI
  85. [88]de Chalain T.M. Tang C. Thomson H.G. Burn area color changes after superficial burns in childhood: Can they be predicted? J. Burn Care Rehabil. 1998 19 39 49 10.1097/00004630-199801000-00010 9502023 · DOI
  86. [89]Bhawan J. Whren K. Panova I. Yaar M. Keratin 16 expression in epidermal melanocytes of normal human skin Am. J. Dermatopathol. 2005 27 476 481 10.1097/01.dad.0000179627.81172.37 16314702 · DOI
  87. [90]Derakhshandeh H. Kashaf S.S. Aghabaglou F. Ghanavati I.O. Tamayol A. Smart Bandages: The Future of Wound Care Trends Biotechnol. 2018 36 1259 1274 10.1016/j.tibtech.2018.07.007 30197225 PMC6511580 · DOI
  88. [91]Rajabi M. Ali A. McConnell M. Cabral J. Keratinous materials: Structures and functions in biomedical applications Mater. Sci. Eng. C 2020 110 110612 10.1016/j.msec.2019.110612 32204061 · DOI
  89. [92]Feroz S. Muhammad N. Ranayake J. Dias G. Keratin—Based materials for biomedical applications Bioact. Mater. 2020 5 496 509 10.1016/j.bioactmat.2020.04.007 32322760 PMC7171262 · DOI
  90. [93]Konop M. Laskowska A.K. Rybka M. Kłodzińska E. Sulejczak D. Schwartz R.A. Czuwara J. Keratin Scaffolds Containing Casomorphin Stimulate Macrophage Infiltration and Accelerate Full-Thickness Cutaneous Wound Healing in Diabetic Mice Molecules 2021 26 2554 10.3390/molecules26092554 33925737 PMC8125279 · DOI
  91. [94]Kim S.Y. Park B.J. Lee Y. Park N.J. Park K.M. Hwang Y.S. Park K.D. Human hair keratin-based hydrogels as dynamic matrices for facilitating wound healing J. Ind. Eng. Chem. 2019 73 142 151 10.1016/j.jiec.2019.01.017 · DOI
  92. [95]Li W. Gao F. Kan J. Deng J. Wang B. Hao S. Synthesis and fabrication of a keratin-conjugated insulin hydrogel for the enhancement of wound healing Colloids Surf. B Biointerfaces 2019 175 436 444 10.1016/j.colsurfb.2018.12.020 30562718 · DOI
  93. [96]Poranki D. Whitener W. Howse S. Mesen T. Howse E. Burnell J. Greengauz-Roberts O. Molnar J. Van Dyke M. Evaluation of skin regeneration after burns in vivo and rescue of cells after thermal stress in vitro following treatment with a keratin biomaterial J. Biomater. Appl. 2014 29 26 35 10.1177/0885328213513310 24272161 · DOI
  94. [97]Gao F. Li W. Deng J. Kan J. Guo T. Wang B. Hao S. Recombinant Human Hair Keratin Nanoparticles Accelerate Dermal Wound Healing ACS Appl. Mater. Interfaces 2019 11 18681 18690 10.1021/acsami.9b01725 31038908 · DOI
  95. [98]Chen X. Zhai D. Wang B. Hao S. Song J. Peng Z. Hair keratin promotes wound healing in rats with combined radiation-wound injury J. Mater. Sci. Mater. Med. 2020 31 28 10.1007/s10856-020-06365-x 32125534 · DOI
  96. [99]Shanmugasundaram O.L. Syed Zameer Ahmed K. Sujatha K. Ponnmurugan P. Srivastava A. Ramesh R. Sukumar R. Elanithi K. Fabrication and characterization of chicken feather keratin/polysaccharides blended polymer coated nonwoven dressing materials for wound healing applications Mater. Sci. Eng. C 2018 92 26 33 10.1016/j.msec.2018.06.020 30184750 · DOI
  97. [100]Vakilian S. Jamshidi-adegani F. Al-Shidhani S. Anwar M.U. Al-Harrasi R. Al-Wahaibi N. Qureshi A. Alyaqoobi S. Al-Amri I. Al-Harrasi A. A Keratin-based biomaterial as a promising dresser for skin wound healing Wound Med. 2019 25 100155 10.1016/j.wndm.2019.100155 · DOI
  98. [101]Veerasubramanian P.K. Thangavel P. Kannan R. Chakraborty S. Ramachandran B. Suguna L. Muthuvijayan V. Corrigendum to “An investigation of konjac glucomannan-keratin hydrogel scaffold loaded with Avena sativa extracts for diabetic wound healing” [Colloids Surf. B Biointerfaces 165 (2018) 92–102] (S0927776518300973) (10.1016/j.colsurfb.2018.02.022) Colloids Surf. B Biointerfaces 2018 171 319 10.1016/j.colsurfb.2018.07.038 29471220 · DOI
  99. [102]Ponrasu T. Veerasubramanian P.K. Kannan R. Gopika S. Suguna L. Muthuvijayan V. Morin incorporated polysaccharide-protein (psyllium-keratin) hydrogel scaffolds accelerate diabetic wound healing in Wistar rats RSC Adv. 2018 8 2305 2314 10.1039/C7RA10334D PMC9077386 35541447 · DOI
  100. [103]Vahidnezhad H. Youssefian L. Saeidian A.H. Mozafari N. Barzegar M. Sotoudeh S. Daneshpazhooh M. Isaian A. Zeinali S. Uitto J. KRT5 and KRT14 Mutations in Epidermolysis Bullosa Simplex with Phenotypic Heterogeneity, and Evidence of Semidominant Inheritance in a Multiplex Family J. Investig. Dermatol. 2016 136 1897 1901 10.1016/j.jid.2016.05.106 27283507 · DOI
  101. [104]Khani P. Ghazi F. Zekri A. Nasri F. Behrangi E. Aghdam A.M. Mirzaei H. Keratins and epidermolysis bullosa simplex J. Cell. Physiol. 2018 234 289 297 10.1002/jcp.26898 30078200 · DOI
  102. [105]Than M.P. Smith R.A. Cassidy S. Kelly R. Marsh C. Maderal A. Kirsner R.S. Use of a keratin-based hydrogel in the management of recessive dystrophic epidermolysis bullosa J. Dermatol. Treat. 2013 24 290 291 10.3109/09546634.2011.654108 22208480 · DOI
  103. [106]Kirsner R.S. Cassidy S. Marsh C. Vivas A. Kelly R.J. Use of a Keratin-Based Wound Dressing in the Management of Wounds in a Patient with Recessive Dystrophic Epidermolysis Bullosa Adv. Skin Wound Care 2012 25 400 403 10.1097/01.ASW.0000419404.44947.de 22914035 · DOI
  104. [107]Than M.P. Smith R.A. Hammond C. Kelly R. Marsh C. Maderal A.D. Kirsner R.S. Keratin-based Wound Care Products for Treatment of Resistant Vascular Wounds J. Clin. Aesthet. Dermatol. 2012 5 31 35 23277802 PMC3533319
  105. [108]Davidson A. Jina N.H. Marsh C. Than M. Simcock J.W. Do functional keratin dressings accelerate epithelialization in human partial thickness wounds? A randomized controlled trial on skin graft donor sites Eplasty 2013 13 e45 24058716 PMC3767044
  106. [109]Denyer J. Marsh C. Kirsner R.S. Keratin gel in the management of Epidermolysis bullosa J. Wound Care 2015 24 446 450 10.12968/jowc.2015.24.10.446 26488735 · DOI
  107. [110]Batzer A.T. Marsh C. Kirsner R.S. The use of keratin-based wound products on refractory wounds Int. Wound J. 2016 13 110 115 10.1111/iwj.12245 24580740 PMC7949970 · DOI
  108. [111]Paulsen E. Bygum A. Keratin gel as an adjuvant in the treatment of recalcitrant pyoderma gangrenosum ulcers: A case report Acta Derm. Venereol. 2019 99 234 235 10.2340/00015555-3081 30393816 · DOI

Cited by

Sorted by citations

Authors
Konop, M., Rybka, M., & Drapała, A.
Affiliations
Medical University of Warsaw (PL)
Corresponding author
Konop, Marek
Venue
Pharmaceutics
Publisher
MDPI AG
Published
2021-11-28
Volume
13
Issue
12
Pages
2029
ISSN
1999-4923 (ISSN-L)
OpenAlex
W3214937540
Cited by
96
References
1
Citations by year
2026: 17 · 2025: 31 · 2024: 20 · 2023: 15 · 2022: 13
FWCI
1.39
Type
journal article
Language
en
Open access
Locations
  • Pharmaceutics (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
Medical University of Warsaw ((1S7/2/M/MB/N/20/20:MAT))
Topics
  • Health Sciences › Medicine › Rehabilitation › Wound Healing and Treatments
  • Physical Sciences › Materials Science › Biomaterials › Electrospun Nanofibers in Biomedical Applications
  • Physical Sciences › Materials Science › Biomaterials › Silk-based biomaterials and applications
Keywords
skin wound healing, wound dressings, tissue engineering, skin regeneration, chronic wounds, acute wounds, biodegradable scaffolds, biocompatibility

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