@entity14520 is induced in abnormal fibers in XXXX .

@entity1 @entity34113 @entity33644 @entity3963 @entity14520 @entity5589 @entity21323 @entity12363
OBJECTIVE: To investigate alterations in protein kinases and phosphatases that regulate the activity of mitogen activated protein kinase (MAPK) in @entity5589 ( @entity5589 ). BACKGROUND: In vacuolated fibers in @entity5589 , several studies reported upregulation of the @entity3963 ( @entity3963 ) subclass of MAPK family. Whereas MAPK kinases (MKK) activate MAPK, MAPK phosphatases (MKP) inactivate MAPK. @entity14520 is involved in muscle fiber differentiation and it is downregulated during myotube formation. METHODS: Immunolocalization of @entity12363 through @entity33644 and @entity14520 to @entity34113 was tested in muscle specimens from 10 @entity1 with @entity5589 and controls. RESULTS: In @entity5589 , strong and focal deposits of @entity14520 were observed in vacuolated fibers. The @entity14520 -positive deposits were colocalized with @entity3963 . @entity21323 , @entity34113 , and MKK were not associated with vacuolated fibers. CONCLUSIONS: In @entity5589 , @entity14520 is abnormally induced in vacuolated fibers probably to inactivate @entity3963 . Although direct activators other than those tested in the current study might induce @entity3963 , the absence of activation of MKK suggests that the aggregation of @entity3963 protein itself causes the seeming upregulation of the protein kinase in @entity5589 . Like @entity3963 and its nuclear substrate, @entity14520 is an enzyme that forms aggregates in vacuolated fibers and is involved in myogenesis.
