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Título: | Protein degradation in a LAMP-2-deficient B-lymphoblastoid cell line from a patient with Danon disease |
Autor: | Sánchez-Lanzas, Raul; Álvarez-Castelao, Beatriz CSIC ORCID; Castaño, José G. CSIC ORCID | Palabras clave: | Alpha-synuclein Chaperone-mediated autophagy Rcan1 Glyceraldehyde-3-phosphate dehydrogenase IkappaB Danon disease LAMP-2 Autophagy Ubiquitin proteasome |
Fecha de publicación: | 2016 | Editor: | Elsevier | Citación: | BBA - Molecular Basis of Disease 1862(8): 1423-1432 (2016) | Resumen: | Danon disease, a condition characterized by cardiomyopathy, myopathy, and intellectual disability, is caused by mutations in the LAMP-2 gene. Lamp-2A protein, generated by alternative splicing from the Lamp-2 pre-mRNA, is reported to be the lysosomal membrane receptor essential for the chaperone-mediated autophagic pathway (CMA) aimed to selective protein targeting and translocation into the lysosomal lumen for degradation. To study the relevance of Lamp-2 in protein degradation, a lymphoblastoid cell line was obtained by EBV transformation of B-cells from a Danon patient. The derived cell line showed no significant expression of Lamp-2 protein. The steady-state mRNA and protein levels of alpha-synuclein, IΚBα, Rcan1, and glyceraldehyde-3-phosphate dehydrogenase, four proteins reported to be selective substrates of the CMA pathway, were similar in control and Lamp-2-deficient cells. Inhibition of protein synthesis showed that the half-life of alpha-synuclein, IΚBα, and Rcan1 was similar in control and Lamp-2-deficient cells, and its degradation prevented by proteasome inhibitors. Both in control and Lamp-2-deficient cells, induction of CMA and macroautophagy by serum and aminoacid starvation of cells for 8 h produced a similar decrease in IΚBα and Rcan1 protein levels and was prevented by the addition of lysosome and autophagy inhibitors. In conclusion, the results presented here showed that Lamp-2 deficiency in human lymphoblastoid cells did not modify the steady-state levels or the degradation of several protein substrates reported as selective substrates of the CMA pathway. | URI: | http://hdl.handle.net/10261/150933 | DOI: | 10.1016/j.bbadis.2016.04.014 | Identificadores: | doi: 10.1016/j.bbadis.2016.04.014 issn: 0925-4439 |
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