ISSN:
1365-2133
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Medicine
Notes:
Basal cell carcinoma (BCC) is a frequent skin cancer with low metastalic potential. Expression of the anchoring filament proteins, native laminin-5 and its individual α3, β3 and γ2 chains, uncein, and linear IgA antigen was examined by immunostaining in 17 BCC with different histological subtypes. Immunoreactivity of the hemidesmosomal proteins, integrin α6β4. 230-kDa bullous pemphigoid antigen (BP-230 Ag) and plectin/HD-1, and that of dermal-epidermal junction (DEJ) components, integrin α2β1, laminin-1, collagen IV, and collagen VII was also analysed. Around tumour nests, the labelling of laminin-5 was absent or markedly reduced in 12 BCC (comprising eight solid BCC, three adenoid BCC and one keratotic BCC) and strong in five BCC (comprising three adenoid BCC, one keratotic BCC and one adenoid and keratotic BCC). Intriguingly, in tumour cells of 12 BCC including laminin-5 negative tumours, a cytoplasmic reactivity of the laminin 72 chain was detected, but not that of the α3 and β3 chains. In the basement membrane of the epidermis overlying tumour nests, the labelling of laminin-5 was always strong. Uncein, linear IgA disease antigen, and integrin α6β4 were absent in solid BCC and weakly expressed in adenoid or keratotic BCC. For plectin/HD-1 and BP-230 Ag, a cytoplasmic reactivity was detected in the majority of the tumour cells. The labelling of integrin α2β1, laminin-1, collagen IV and collagen VII indicated no alteration in the synthesis of these proteins. In peritumoral lacunae, immunoreactivity of hemidesmosome and anchoring filament proteins was absent, except for plectin/HD-1 on the tumour side and sometimes for laminin-5 on the stromal side, while laminin-1, collagen IV and collagen VII were detected on the stromal side. These findings suggest that the components of the hemidesmosome-anchoring filament complex are not synthetized or assembled properly in BCC, and that the alteration of these adhesion structures may be the cause of peritumoral lacunae.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1046/j.1365-2133.1997.d01-1139.x
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