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. 2018 May 4;9(1):230–245. doi: 10.1080/19491034.2018.1460185

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© 2018 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 1. — HGPS aging defects are most pronounced in mechanically stressed tissues. (A) HGPS disproportionately affects stiff and mechanically stressed tissues (e.g. skeletal/cardiac muscle) while soft tissues (e.g. brain, marrow) appear normal, regardless of lineage or developmental origin. (B) Post-translational processing of normal lamin-A/C and progerin. The truncated mutant, progerin, retains a C-terminus farnesyl group. Upper right box: A-type lamin isoforms differ in molecular weight (MW) by ∼5 kDa. Lower right: Venn diagram of unique and common A-type lamin peptides. The majority of the peptides are shared by all three isoforms, with the exception of isoform-specific peptides at the C-terminus. ‘FTase’ = Farnesyl transferase; ‘RCE1’ = Ras converting CAAX endopeptidase 1; ‘ZMPSTE24’ = Zinc metallopeptidase STE24; ‘ICMT’ = Isoprenylcysteine carboxyl methyltransferase.