The alpha-3 polypeptide chain of laminin 5: insight into wound healing responses from the study of genodermatoses
Authors: Hamill, K. J.; McLean, W. H. I.
Source: Clinical & Experimental Dermatology, Volume 30, Number 4, July 2005 , pp. 398-404(7)
Publisher: Blackwell Publishing
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Abstract:
Summary Laminin 5 (kalinin/epiligrin/nicein) is an essential structural component of the dermal–epidermal junction, composed of three polypeptide subunits: laminin α3, β3 and γ2. Studies of the inherited skin fragility disorder junctional epidermolysis bullosa (JEB) have suggested that the major role of this heterotrimeric protein is to act as an adhesive ligand essential for binding the epidermis to the underlying dermis and thus maintaining the integrity of the skin. Protein interaction studies have shown that the C terminus of the α3 subunit binds to a range of integrin complexes depending on the motility status of keratinocytes. This allows laminin 5 to interact with either hemidesmosomes or the actin cytoskeleton. Recently we have reported that the absence of the N-terminal region of laminin α3a in laryngo-onchyo-cutaneous syndrome causes excessive granulation tissue production at wound sites. As granulation tissue production is also a problem in JEB, this implicates laminin 5 in control of this wound healing response.Document Type: Research article
DOI: 10.1111/j.1365-2230.2005.01842.x
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