As additional control of APT-1 activity, we evaluated the effect of ectopically expressed APT-1 on H-RasG12V deacylation and its consequences on subcellular distribution.
As CHO-K1 cells do not naturally express APT-1, the results strongly suggest the existence of other uncharacterized acyl-protein thioesterase.
In a clear contrast, we observed that in cells expressing APT-2, the half-time of N13GAP-43(C3S) deacylation was reduced to 3 min (Fig. 5B), demonstrating that APT-2 catalyze in vivo deacylation of N13GAP-43(C3S).
The known miRNAs with normalized read-count less that ten in the two libraries were not used for further analysis, because the use of low expressed miRNAs is apt to cause false results [ 39].
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We could show that during all post-embryonic developmental stages Apt is expressed in NBs, GMCs and immature neurons.
Interestingly, we demonstrated that APT-1 is not expressed in CHO-K1 cells and that APT-1 overexpression did not significantly increase the deacylation rate of monoacylated or wild-type GAP-43 but did enhance the deacylation rate of H-RasG12V protein.
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Among several candidates, we found that APT-2 is expressed both in CHO-K1 and HeLa cells and its overexpression increased the deacylation rate of single acylated GAP-43 and affected the steady-state localization of diacylated GAP-43 and H-Ras.
Thus, results demonstrated that APT-1 is not expressed in CHO-K1 cells.
Our data illustrate that Apt-alphavbeta3 binds alphavbeta3 integrin expressed on the surface of live HUVECs.
