sub:provenance {
  beldoc: dce:description "Approximately 61,000 statements." ;
    dce:rights "Copyright (c) 2011-2012, Selventa. All rights reserved." ;
    dce:title "BEL Framework Large Corpus Document" ;
    pav:authoredBy sub:_6 ;
    pav:version "20131211" .
  sub:_5 prov:value "We focused on follistatin since it is one of the most highly upregulated transcripts (28fold, Supplemental Table S1) and because of its reported role in muscle development (Lee and McPherron, 2001; Matzuk et al., 1995). In the absence of TSA, follistatin transcription was initiated after 4 to 12 hr of culture in differentiation medium and steadily increased over the next 48 hr (Figure 2G, Control). While being consistently elevated in every sample of TSA-treated cells, the follistatin transcripts displayed two peaks at 4 and 48 hr (Figure 2G, TSA). The transcriptional profile of follistatin was independently analyzed by RT-PCR and found to be concordant with that observed using microarray analysis (Figure 2G, lower panel). VPA and sodium butyrate, another HDAC inhibitor, also increased follistatin expression (Figure 2H). To investigate whether HDAC inhibitors induce follistatin expression in a cell type-spe-cific manner, mouse primary keratinocytes, C2C12 cells (Figures 3A and 3B), and mouse primary myoblasts (Figures 3C and 3D) were exposed to either TSA, sodium butyrate, or VPA for 18 hr and induced to differentiate. HDAC inhibitors increased follistatin levels in C2C12 and primary myoblasts but not in keratinocytes, which also failed to upregulate follistatin during differentiation (Figures 3A to 3D). Similarly, HDAC inhibitors could not augment follistatin expression in C3H10T1/2 and NIH3T3 mouse fibroblasts, as well as in the adipogenic 3T3-L1 and the osteogenic MC3T3-E1 cell lines (Figures 3E and 3F)." ;
    prov:wasQuotedFrom pubmed:15130492 .
  sub:_6 rdfs:label "Selventa" .
  sub:assertion prov:hadPrimarySource pubmed:15130492 ;
    prov:wasDerivedFrom beldoc: , sub:_5 .
}