Urokinase plasminogen activator mRNA is induced by @entity1192 and XXXX in in vitro acantholysis.

@entity1 @entity7271 @entity310 @entity1192 @entity1351 @entity563 @entity2290
The role of @entity2290 ( @entity2290 ) has been well documented in the pathogenesis of @entity7271 ( @entity7271 ). Activation of plasminogen into active @entity563 protease @entity1351 initiates extracellular proteolysis leading to acantholysis but the mechanisms underlying this process are not clearly understood. We have previously shown that keratinocyte derived cytokines @entity1192 and @entity310 are involved in @entity7271 -induced acantholysis. In the present study we sought to examine whether keratinocyte-derived @entity1192 and @entity310 are correlated with @entity2290 induction in keratinocytes during acantholysis. Normal @entity1 keratinocytes were incubated with diluted @entity7271 serum. mRNAs for @entity1192 , @entity310 and @entity2290 were examined with RT-PCR at various time points and acantholysis was measured. @entity1192 , @entity310 and @entity2290 mRNAs were all induced in keratinocytes following @entity7271 serum stimulation; @entity1192 / @entity310 mRNAs' expression was earlier than the expression of @entity2290 mRNA. To further examine the role of @entity1192 , @entity310 and @entity2290 in acantholysis, we performed antibody blocking studies. Anti- @entity1192 , anti- @entity310 and anti- @entity2290 antibodies suppressed acantholysis by 76%, 80% and 90%, respectively. In addition, anti- @entity1192 and anti- @entity310 antibodies inhibited @entity2290 mRNA induction, whereas anti- @entity2290 antibodies did not alter @entity1192 / @entity310 mRNAs' expression. Our results confirm the role of @entity2290 in acantholysis and suggest an involvement of @entity1192 / @entity310 in @entity2290 induction.
