Summary
An invariable feature of wounded skin, whether the lesion is healing normally or chronic, is the expression of interstitial collagenase by migrating basal keratinocytes. Collagenase is a member of the matrix metalloproteinase family of enzymes and is the principal human enzyme which cleaves native fibrillar collagen. This proteinase may serve to accelerate the movement of keratinocytes during repair; however, its overexpression at the migrating front of the epidermis may actually impair healing in chronic ulcers. This potential inhibitory effect of human collagenase in nonhealing lesions is both spatially removed and mechanistically distinct from débridement of necrotic tissues overlying the wound bed by the topical application of bacterial collagenase and other broad-acting proteinases.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Parks WC, Sires UI (1995) Matrix metalloproteinases and skin biology. Curr Opin Dermatol 3: 240–247
Woessner JF (1991) Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J 5: 2145–2154
Birkedal-Hansen H, Moore WGI, Bodden MK, Windsor LJ, Birkedal-Hansen B, DeCarlo A, Engler JA (1993) Matrix metalloproteinases: a review. Crit Rev Oral Biol Med 4: 197–250
Sato H, Takino T, Okada Y, Cao J, Shinagawa A, Yamamoto E, Seiki M (1994) A matrix metalloproteinase expressed on the cell surface of invasive tumour cells. Nature 370: 61–65
Olerud JE, Gown AM, Bickembach J, Dale B, Odland GF (1988) An assessment of human epidermal repair in elderly normal subjects using immunohistochemical methods. J Invest Dermatol 90: 845–850
Saarialho-Kere UK, Kovacs SO, Pentland AP, Olerud J, Welgus HG, Parks WC (1993) Cell-matrix interactions modulate interstitial collage-nase expression by human keratinocytes actively involved in wound healing. J Clin Invest 92: 2858–2866
Prosser IW, Stenmark KR, Suthar M, Crouch EC, Mecham RP, Parks WC (1989) Regional heterogeneity of elastin and collagen gene expression in intralobar arteries in response to hypoxic pulmonary hypertension as demonstrated by in situ hybridization. Am J Pathol 135: 1073–1088
Pentland AP, Jacobs Sc, Mahoney M, Holzman MJ (1990) Ultraviolet light potentiates histamine-induced release of prostaglandin in cultured human keratinocytes: a mechanism for irradiation erythema. J Clin Invest 86: 566–574
Agren MS, Taplin CJ, Woessner JF, Eaglstein WH, Mertz PM (1992) Collagenase in wound healing: effect of wound age and type. J Invest Dermatol 99: 709–714
Buckley-Sturrock A, Woodward SC, Senior RM, Griffin GL, Klagsbrun M, Davidson JM (1989) Differential stimulation of collagenase and chemotactic activity in fibroblasts derived from rat wound repair tissue and human skin by growth factors. J Cell Physiol 138: 70–78
Porras-Reyez BH, Blair HC, Jeffrey JJ, Mustoe TA (1991) Collagenase production at the border of granulation tissue in a healing wound: macrophage and mesenchymal collagenase production in vivo. Connect Tissue Res 27: 63–71
Stricklin GP, Li L, Jancic V, Wenczak BA, Nanney LB (1993) Localization of mRNAs representing collagenase and TIMP in sections of healing human burn wounds. Am J Pathol 143: 1657–1666
Saarialho-Kere UK, Chang ES, Welgus HG, Parks ‘A/C (1992) Distinct localization of collagenase and TIMP expression in wound healing associated with ulcerative pyogenic granuloma. J Clin Invest 90: 1952–1957
Saarialho-Kere UK, Chang ES, Welgus HG, Parks WC (1993) Expression of interstitial collagenase, 92 kDa gelatinase, and TIMP-1 in granuloma annulare and necrobiosis lipoidica diabeticorum. J Invest Dermatol 100: 335–342
Welgus HG, Stricklin GP (1983) Human skin fibroblast collagenase inhibitor: comparative studies in human connective tissues, serum and amniotic fluid. J Biol Chem 258: 12259–12264
Saarialho-Kere UK, Vaalamo M, Airola K, Niemi K-M, Oikarinen AI, Parks WC (1995) Interstitial collagenase is expressed by keratinocytes which are actively involved in re-epithelialization in blistering skin diseases. J Invest Dermatol 104: 982–988
Stenn KS, Malhotra R (1992) Epithelialization: In: Cohen IK, Diegelmann RF, Linblad WI (eds) Wound healing: biochemical and clinical aspects. Saunders, Philadelphia, pp 115–127
Clark RAF, Lanigan JM, DellaPelle P, Manseau E, Dvorak HF, Colvin RB (1982) Fibronectin and fibrin provide a provisional matrix for epidermal cell migration during wound re-epithelization. J Invest Dermatol 79: 264–269
Sudbeck PD, Parks WC, Welgus HG, Pentland AP (1994) Collagen-mediated induction of keratinocyte collagenase is mediated by tyrosine kinase and protein kinase C activities. J Biol Chem 269: 30022–30029
Petersen MI, Woodley DT, Stricklin GP, O’Keefe EJ (1990) Enhanced synthesis of collagenase by human keratinocytes cultured on type I or type IV collagen. J Invest Dermatol 94: 341–346
Cavani A, Zambruno G, Marconi A, Manca V, Marchetti M, Giannetti A (1993) Distinctive integrin expression in the newly forming epidermis during wound repair. J Invest Dermatol 101: 600–604
Hertle MD, Kubler M-D, Leigh IM, Watt FM (1992) Aberrant integrin expression during epidermal wound healing and in psoriatic epidermis. J Clin Invest 89: 1892–1901
Juhasz I, Murphey GF, Yan H-C, Herlyn M, Albelda SM (1993) Regulation of extracellular matrix proteins and integrin cell substratum adhesion receptors on epithelium during cutaneous wound healing in vivo. Am J Pathol 143: 1458–1469
Larjava H, Salo T, Haapasalmi K, Kramer RH, Heino J (1993) Expression of integrins and basement membrane components by wound keratinocytes. J Clin Invest 92: 1425–1435
Staatz WD, Rajpara SM, Wayner EA, Carter WG, Santoro SA (1989) The membrane glycoprotein la—lla (VLA-2) complex mediates the Mg+2-dependent adhesion of platelets to collagen. J Cell Biol 108: 1917–1924
Firestein GS, Paine MM, Littman BH (1991) Gene expression (collage-nase, tissue inhibitor to metalloproteinases, complement, and HLA-DR) in rheumatoid arthritis and osteoarthritis synovium. Quantitative analysis and effect of intraarticular corticosteroids. Arthritis Rheum 34: 1094–1105
Thompson RW, Mertens RA, Liao S, Holmes DR, Mecham RP, Welgus HG, Parks WC (1995) Production and localization of 92-kD gelatinase in abdominal aortic aneurysms: an elastolytic metalloproteinase expressed by aneurysm-infiltrating macrophages. J Clin Invest 96: 318–327
Saarialho-Kere UK, Kovacs SO, Pentland AP, Parks WC, Welgus HG (1994) Distinct populations of keratinocytes express stromelysin-1 and -2 in chronic wounds. J Clin Invest 94: 79–88
Bullen EC, Longaker MT, Updike DL, Benton R, Ladin D, Hou Z, Howard EW (1995) Tissue inhibitor of metalloproteinases-1 is decreased and activated gelatinases are increased in chronic wounds. J Invest Dermatol 104: 236–240
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1996 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Parks, W.C. (1996). Interstitial Collagenase in the Healing Epidermis. In: Abatangelo, G., Donati, L., Vanscheidt, W. (eds) Proteolysis in Wound Repair. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-61130-8_3
Download citation
DOI: https://doi.org/10.1007/978-3-642-61130-8_3
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-60815-8
Online ISBN: 978-3-642-61130-8
eBook Packages: Springer Book Archive