Clinically Distinct Phenotypes of Canavan Disease Correlate with Residual Aspartoacylase Enzyme Activity

Figures

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  Figure 1. Schematic and structural representation of the ASPA monomer with the location of the amino acid residues addressed in this study. The structural image was generated using the crystal structure of ASPA (PDB ID: 2O4H), obtained using the UCSF Chimera package. Chimera is developed by the Resource for Biocomputing, Visualization, and Informatics at the University of California, San Francisco (supported by NIGMS P41‐GM103311).

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  Figure 2. Schematic representation of the ASPA gene and the distribution of all published mutations (as of September 2016). These mutations are part of the mutation database LOVD (http://www.lovd.nl/ASPA). Variants located in exonic regions are in black, variants in intronic regions are in gray. Novel variants addressed in this study are represented in bold. Large deletions are depicted in the box.

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  Figure 3. Expression levels of ASPA proteins in fusion with mGFP transiently transfected into Human Embryonic Kidney cells (HEK293) monitored by Western blot analysis after SDS‐PAGE. Thirty micrograms of total protein was loaded per lane. An antibody against mGFP was used as primary antibody. The arrow points to the ASPA‐mGFP fusion protein. The * indicates free mGFP.