(A) IHC showing PROX1 localization in normal thyroid
tissues (Normal, n=25), PTC (n=26), follicular thyroid carcinoma (FTC, n=6),
anaplastic or undifferentiated thyroid carcinoma (ATC, n=6). Overview (i, iii,
v, vii) are shown with enlarged images (ii, iv, vi, viii). Scale bars, 50
µm. PROX1 localization: nuclei (N), cytoplasm (C). (B) IF
analyses showing PROX1 localization in LECs (i–iv), BCPAP
(v–viii) and TPC1 (ix–xii). Four different PROX1 antibodies were
used: rabbit polyclonal antibody from Reliatech (Re) (i,v,ix), mouse monoclonal
antibody 5G10 from Millipore (Ch) (ii,vi,x), custom generated rabbit polyclonal
antibodies against PROX1 N-terminus (N) (iii, vii,xi) and C-terminus (C)
(iv,viii,xii). PROX1 was stained in red and the nuclei with DAPI. Scale Bars, 20
µm. (C) Western blot assays showing subcellular
distribution of PROX1 protein. The cytoplasmic (cyt) and nuclear (nuc) fractions
were obtained from LEC, BCPAP and TPC1, and probed for PROX1. Tubulin and lamin
were also detected as the controls for the cytoplasmic and nuclear fractions,
respectively. (D,E) PROX1 protein is more stable in PTC cells than
in LECs. LECs, BCPAP and TPC1 cells were treated with cycloheximide (100
µg/ml) for the indicated time. Western blot analyses showing PROX1
protein (D). PROX1 band is marked with an asterisk for TPC-1 blot.
PROX1 expression was normalized against β-actin (E).
(F,G) Cytoplasmic PROX1 protein is more stable than nuclear
PROX1. TPC1 cells were treated with cycloheximide (100 µg/ml) for 0, 1
and 2 hours, followed by subcellular fractionation. Western blotting for PROX1
in the cytoplasmic (Cyto.) and nuclear (Nucl.) fractions (F).
β-actin and lamin were also detected as the controls for the cytoplasmic
and nuclear fractions, respectively. Normalized band intensities of the
cytoplasmic and nuclear PROX1 proteins to β-actin and lamin proteins,
respectively (G). Error bars present standard deviations.