Fig. 7. Western blot analysis of proliferation-associated proteins showed no
alterations in p53 (A, lane 4, wild-type; lane 5, K10-/-; lanes
1,2, a corresponding coomassie-stained blot; lane 3, marker; dot, 56 kDa), a
slight decrease in p21 (B, lane 4, wild-type; lane 5, K10-/-; lanes
2,3, loading control; lane 1, marker; dots, 36 and 26 kDa) and p27 (C, lane 4,
wild-type; lane 5, K10-/-; lanes 1,2, loading control; lane 3,
marker; dots, 36 and 26 kDa), no changes in ß-catenin (D, lane 4,
wild-type; lane 5, K10-/-; lanes 2,3, loading control; lane 1,
marker; dots from top to bottom, 116, 97 and 66 kDa), Rb (E, lane 4,
arrowhead, wild-type; lane 5, K10-/-; lanes 2,3, loading control;
lane 1, marker; dots, 116 and 97 kDa) or phosphorylated Rb (Ser780) (F, lane
4, arrowhead, wild-type; lane 5, K10-/-; lanes 1,2, loading
control; lane 3, marker; dots, 158 and 116 kDa). (G) The level of
unphosphorylated Akt kinase was unaltered (lane 8, wild-type; lane 9,
K10-/-, upper band; lanes 2,3, loading control; lane 1, marker;
dots from top to bottom, 66 and 56 kDa) while phosphorylated Akt
(Thr308-specific detection: lane 10, wild-type; lane 11, K10-/-;
Ser473-specific detection; lane 12, wild-type; lane 13, K10-/-;
lanes 4-7, loading control) was reduced. A and B show blots of 18%, E and F of
8% and C, D, G and H of 10% polyacrylamide gels.
