@article{Dominici_Fiori_Magnani_Schena_Capanni_Camozzi_D’Apice_Le Dour_Auclair_Caron_Novelli_Vigouroux_Maraldi_Lattanzi_2009, title={Different prelamin A forms accumulate in human fibroblasts: a study in experimental models and progeria}, volume={53}, url={https://www.ejh.it/ejh/article/view/ejh.2009.e6}, DOI={10.4081/ejh.2009.e6}, abstractNote={Lamin A is a component of the nuclear lamina mutated in a group of human inherited disorders known as laminopathies. Among laminopathies, progeroid syndromes and lipodystrophies feature accumulation of prelamin A, the precursor protein which, in normal cells, undergoes a multi-step processing to yield mature lamin A. It is of utmost importance to characterize the prelamin A form accumulated in each laminopathy, since existing evidence shows that drugs acting on protein processing can improve some pathological aspects.We report that two antibodies raised against differently modified prelamin A peptides show a clear specificity to full-length prelamin A or carboxymethylated farnesylated prelamin A, respectively. Using these antibodies, we demonstrated that inhibition of the prelamin A endoprotease ZMPSTE24 mostly elicits accumulation of full-length prelamin A in its farnesylated form, while loss of the prelamin A cleavage site causes accumulation of carboxymethylated prelamin A in progeria cells. These results suggest a major role of ZMPSTE24 in the first prelamin A cleavage step.}, number={1}, journal={European Journal of Histochemistry}, author={Dominici, S and Fiori, V and Magnani, M and Schena, E and Capanni, C and Camozzi, D and D’Apice, MR and Le Dour, C and Auclair, M and Caron, M and Novelli, G and Vigouroux, C and Maraldi, NM and Lattanzi, G}, year={2009}, month={Aug.}, pages={e6} }