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C. Hlli" el al./ Bialag)' of/I<strong>le</strong> <strong>Ce</strong>l/94 (2002} /5-27 23<br />
Fig. 5. PPAR loc~lilalion in C~co-2 cells dllring lhe differcnlinliOrl process. ImmunocylochemiSlty wns perfomlcd as describcd in Mf/<strong>le</strong>ria/s fII,tlmet1to(/s<br />
using PPARu (a-(), produced (d-f) and commercinl (g-I) PPARy rabbilnmiscfn. No signal was obwined wilh commis (e, f, i) perfonned Wilh C3co·2 ecUs<br />
euhurcd for 15 d~y~. Nudear immlloorenclivily (arrows) was observed al dny 5 (Il, d, g) whatevcr Ihe nnlisen'm used. Nuc<strong>le</strong>nr loc~lizmion w~s evidem m<br />
d:lY 15 (b. e. hl. ImmunorenClivity wns slmngesl Wilh PPARu. anliscnJm lhan wilh PPARy anlisera (com<strong>par</strong>e b 10 e, hl.<br />
between day 5 and day 15 ofCaco-2cell cuIJure.lt has been<br />
demonstrated Ihat PPARYI protein is encoded by both<br />
PPARYI and PPARY3 rnRNA (F'Uas et al" 1997 and [998).<br />
Using polyc!ona[ antibodies that recognized both PPARYl<br />
and PPARY2 proteins, our immunocytochemical and W<strong>est</strong>ern<br />
blot data revea[cd an îllcrease in PPARy content during<br />
Caco-2 ccli differentation. lt is Iikely Ihat the PPARYl<br />
protein contrîbutes <strong>par</strong>tI y to this increase for the following<br />
reasons:<br />
• Ihe imensîty of the band recognized by the anti-PPARy<br />
anlibody increased steadi[y during cell culture whereas<br />
Ihe protein <strong>le</strong>vel of PPARY2 remained constant after<br />
10 days of ccli culture;<br />
• Ihe <strong>le</strong>vel of the PPARY3 mRNA enco
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