Association of CXCR1 and 2 expressions with XXXX @entity3 in ex vivo and @entity5 cell invasion in vitro.

@entity7242 @entity12136 @entity5 @entity1178 @entity7415 @entity4675 @entity1495 @entity3 @entity687 @entity7416 @entity356 @entity1366
BACKGROUND: @entity7415 and @entity7416 , cell surface receptors of @entity687 , regulate cell migration and alteration of their expression has been associated with poor prognosis of @entity5 . The aim of this study was to detect their expression in @entity356 to identify associations with another cell adhesion molecule, @entity1495 ( @entity1495 ), and with clinicopathological data ex vivo, and then explore their potential role in @entity356 cells in vitro. MATERIALS AND METHODS: A total of 172 cases of @entity356 tissue specimens were collected for immunohistochemical analysis of @entity7415 , @entity7416 , and @entity1495 expression. Expression of @entity7415 and @entity7416 proteins was knocked in or down using their cDNA and shRNA, respectively, in @entity356 cell lines to assess the changed cell phenotypes and gene expression. RESULTS: @entity7415 , @entity7416 , and @entity1495 were expressed in 61.0%, 77.9%, and 75.6% of @entity356 tissues, respectively. Moreover, @entity7415 and @entity7416 expression was associated with @entity5 differentiations, advanced clinical stages, lymph node, and distant @entity3 of @entity356 . Similarly, @entity1495 expression was associated with @entity7415 and @entity7416 . Expression of these three proteins was interrelated. In vitro study showed that levels of @entity7415 and @entity7416 proteins were associated with the capacity of @entity356 cell migration, while knockdown of their expression inhibited @entity356 cell migration and invasion abilities in vitro. In contrast, overexpression of @entity7415 and @entity7416 proteins promoted @entity5 cell migration and invasion. At the gene levels, knockdown of @entity7415 or @entity7416 expression suppressed expression of @entity12136 , @entity7242 , and @entity4675 proteins and phosphorylated @entity1178 and @entity1366 . Conversely, upregulation of @entity7415 or @entity7416 promoted expression of @entity12136 , @entity7242 , @entity4675 , and @entity1178 proteins and phosphorylated @entity4675 , @entity1178 and @entity1366 . CONCLUSIONS: These findings suggest that @entity7415 and @entity7416 play an important role in @entity356 progression. Further study will be performed to investigate whether target of their expression can be used as a novel strategy in clinical control of @entity356 @entity3 .
