| Title | Hyaluronic acid induces wound closure by primary human skin fibroblasts in a wound healing model | ||
| Authors | D. Economou¹, E. Papakonstantinou², I. Klagas², Ath. Sakadamis³ and A. Sioga¹
1. Department of Histology-Embryology and 2. Department of Pharmacology, 3. 2nd Department of Surgery, School of Medicine, Aristotle University of Thessaloniki, Greece |
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| Citation | Economou, D., Papakonstantinou, E., Klagas, I., Sakadamis, A., Sioga, A.: Hyaluronic acid induces wound closure by primary human skin fibroblasts in a wound healing model, Epitheorese Klin. Farmakol. Farmakokinet. 22(2): 138-140 (2008) | ||
| Publication Date | 23-25 May 2008 | ||
| Full Text Language | English | ||
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| Keywords | Glycosaminoglycans, matrix metalloproteinase-2, primary human skin fibroblasts, migration, wound healing. | ||
| Other Terms | Review article | ||
| Summary | Hyaluronic acid (HA) is the most common glycosaminoglycan present in the extracellular matrix of epidermis and dermis. In the present study, we investigated the effect of HA on the migration of primary human skin fibroblasts in a wound healing model. 5e found that HA (1 μg/ml) enhances in a time-dependent manner (2-48 h) the migration of human skin fibroblasts. This effect was associated with an increased secretion of MMP-2 gelatinolytic activity and an induction in MMP-2 gene expression, as assessed by gelatin zymography and RT-PCR, respectively. Our results indicate that HA regulates the migration of human skin fibroblasts by stimulation of MMP-2 and may offer an additional target for pharmacological intervention in wound healing. | ||
| References | 1. Papakonstantinou E., Karakiulakis G., Eickelberg O., et al.: A 340 kDa hyaluronic acid secreted by human vascular smooth muscle cells regulates their proliferation and migration. Glycobiology 8: 821-830 (1998)
2. Ruoslahti E., Yamaguchi Y.: Proteoglycans as modulators of growth factor activities. Cell 64: 867-869 (1991) 3. Stocker W., Grams F., Baumann U., et al.: The metzincins-topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases. Protein Sci. 4: 823-840 (1995) 4. Kerkela E., Saarialho-Kere U.: Matrix metalloproteinases in tumor progression: focus on basal and squamous cell skin cancer. Exp. Dermatol. 12: 109-125 (2003) 5. Nova D., Le Griel C., Holvoet S., et al. Comparative studies on the secretion and activation of MMPs in two reconstructed human skin models using HaCaT- and HaCaT-ras-transfected cell lines. Clin. Exp. Metastasis 20: 675-683 (2003) 6. Singer A.J., Clark R.A.F.: Cutaneous wound healing. N. Engl. J. Med. 341: 738-746 (1999) 7. Karakiulakis G., Papanikolaou C., Jankovic S.M., et al.: Increased type IV collagen-degrading activity in metastases originating from primary tumors of the human colon. Invasion Metastasis 17: 158-168 (1997) 8. Karakiulakis G., Papakonstantinou E., Aletras A.J., Tamm M., Roth M.: Cell type-specific effect of hypoxia and platelet-derived growth factor-BB on extracellular matrix turnover and its consequences for lung remodeling. J. Biol. Chem.: (2007) 9. Gotte M., Kresse H.: Defective glycosaminoglycan substitution of decorin in a patient with progeroid syndrome is a direct consequence of two point mutations in the galactosyltransferase I (beta4GalT-7) gene. Biochem. Genet. 43: 65-77 (2005) 10. Clark R.A., Lin F., Greiling D., An J., Couchman J.R.: Fibroblast invasive migration into fibronectin/fibrin gels requires a previously uncharacterized dermatan sulfate- CD44 proteoglycan. J. Invest Dermatol. 122: 266-277 (2004) |
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| Relative Papers | |||
Online ISSN 1011-6575
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Articles published in this Journal are Indexed or Abstracted in: • Chemical Abstracts • Elsevier’s Bibliographic Databases: Scopus, EMBASE, EMBiology, Elsevier BIOBASE SCImago Journal and Country Rank Factor
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