The E2 protein of @entity1082 type 8 increases the expression of matrix metalloproteinase-9 in XXXX keratinocytes and organotypic skin cultures.

@entity1 @entity72770 @entity5 @entity1489 @entity281 @entity1082 @entity1495 @entity3 @entity72771
@entity1489 ( @entity1489 ) is the most frequent @entity1 @entity5 of Caucasian populations. Although the ultraviolet irradiation is a key contributor to the establishment of this keratinocyte malignancy, the @entity281 by some types of @entity1082 ) has also been implicated in @entity1489 development. Cancers occur as a result of a complex series of interactions between the @entity5 cell and its surrounding matrix. The matrix metalloproteinases (MMPs) play a role in degrading the extracellular matrix. @entity1495 is an important gelatinase involved in processes such as cell migration, invasion and @entity3 . In this report, we demonstrated by EMSA experiments that the @entity1495 promoter contains a binding site for the transcriptional regulator E2 of HPV8. Transient reporter gene assays showed that HPV8-E2 activated the @entity1495 promoter in a dose-dependent manner in @entity1 epidermal keratinocytes. An E2 transactivation-defective mutant ( @entity72770 ) as well as a DNA-binding deficient mutant ( @entity72771 ) demonstrated no activation of the @entity1495 promoter, suggesting that both an intact transactivation and DNA-binding domain are required for E2 activation of the @entity1495 -promoter. The functional role of the E2 binding site within the @entity1495 promoter was also confirmed by mutating the E2 binding site. In organotypic cultures of @entity1 skin, an overexpression of @entity1495 was observed in suprabasal layers of the HPV8 E2-expressing epidermis thus confirming the results of the monolayer cultures. These results demonstrate that the early gene E2 of HPV8 is able to increase the expression of @entity1495 by direct activation of the @entity1495 -promoter.
