Altered interface adhesion molecules in oral lichen planus

To evaluate expression of key epithelial-connective tissue interface adhesion molecules (basal keratinocyte integrins and extracellular matrix receptors) in oral lichen planus (LP).

Integrins alpha 3, alpha 6, beta 1, beta 4 and basement membrane proteins laminin 1, laminin 5, collagen IV, and collagen VII were immunohistochemically identified in frozen biopsy specimens (14 oral LP and II matched controls) using a standard avidin-biotin-peroxidase technique.

An increased staining intensity of all antigens in LP was shown, as compared to controls. Integrin expression by LP keratinocytes was generally more intense and appeared on more upper level cells. Staining for basement membrane-associated extracellular matrix proteins was also generally more intense, although fragmentation and gaps were typically seen. Reactions for alpha 6, beta 4, laminin 5, and collagen VII stains were particularly intense along the basement membrane. In LP, strands of laminin 5, collagen IV, and collagen VII appeared in the submucosa approximating or duplicating the basement membrane.

The apparent increased expression of the interface-associated adhesion molecules may be reflective of a keratinocyte compensatory response (due to lymphocyte-mediated damage) that would functionally help resist epithelial separation (ulceration). Expression of alpha 3 beta 1 and alpha 6 beta 4 would also assist in epithelial migration associated with wound repair. We interpret the submucosal extensions and deposits of basement membrane proteins as representing remnants of basement membrane, indicating recent remodeling or atrophy of epithelial rete ridges.