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  • Progeria-based vascular model identifies networks associated with cardiovascular aging and disease.

Progeria-based vascular model identifies networks associated with cardiovascular aging and disease.

Aging cell (2024-04-05)
Mzwanele Ngubo, Zhaoyi Chen, Darin McDonald, Rana Karimpour, Amit Shrestha, Julien Yockell-Lelièvre, Aurélie Laurent, Ojong Tabi Ojong Besong, Eve C Tsai, F Jeffrey Dilworth, Michael J Hendzel, William L Stanford
ABSTRACT

Hutchinson-Gilford Progeria syndrome (HGPS) is a lethal premature aging disorder caused by a de novo heterozygous mutation that leads to the accumulation of a splicing isoform of Lamin A termed progerin. Progerin expression deregulates the organization of the nuclear lamina and the epigenetic landscape. Progerin has also been observed to accumulate at low levels during normal aging in cardiovascular cells of adults that do not carry genetic mutations linked with HGPS. Therefore, the molecular mechanisms that lead to vascular dysfunction in HGPS may also play a role in vascular aging-associated diseases, such as myocardial infarction and stroke. Here, we show that HGPS patient-derived vascular smooth muscle cells (VSMCs) recapitulate HGPS molecular hallmarks. Transcriptional profiling revealed cardiovascular disease remodeling and reactive oxidative stress response activation in HGPS VSMCs. Proteomic analyses identified abnormal acetylation programs in HGPS VSMC replication fork complexes, resulting in reduced H4K16 acetylation. Analysis of acetylation kinetics revealed both upregulation of K16 deacetylation and downregulation of K16 acetylation. This correlates with abnormal accumulation of error-prone nonhomologous end joining (NHEJ) repair proteins on newly replicated chromatin. The knockdown of the histone acetyltransferase MOF recapitulates preferential engagement of NHEJ repair activity in control VSMCs. Additionally, we find that primary donor-derived coronary artery vascular smooth muscle cells from aged individuals show similar defects to HGPS VSMCs, including loss of H4K16 acetylation. Altogether, we provide insight into the molecular mechanisms underlying vascular complications associated with HGPS patients and normative aging.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Anti-Actin Antibody, smooth muscle, clone ASM-1, clone ASM-1, Chemicon®, from mouse
Sigma-Aldrich
Anti-DNA-PKcs Antibody, clone 3A9.1, clone 3A9.1, from mouse
Sigma-Aldrich
Rabbit anti-MOF/MYST1 Antibody, Affinity Purified, Powered by Bethyl Laboratories, Inc.
Sigma-Aldrich
Anti-Lamin A Antibody, CT, a.a. 598-611, clone 133A2, clone 133A2, Chemicon®, from mouse
Sigma-Aldrich
Anti-acetyl-Histone H4 (Lys16) Antibody, Upstate®, from rabbit
Sigma-Aldrich
Anti-Progerin Antibody, clone 13A4, clone 13A4, Upstate®, from mouse