Abdominal Aortic Calcification

ABSTRACT: Abdominal aortic calcification (AAC) is driven by inflammation, structural remodeling, and vascular smooth muscle cell dysfunction, yet its ubiquitination-mediated regulatory mechanisms remain poorly defined. Using paired calcified and non-calcified abdominal aortic tissues from four donors, we performed integrated proteomic and ubiquitinomic profiling, quantifying 2,325 proteins and 7,041 lysine ubiquitination (Kub) sites. Upregulated proteins and proteins carrying upregulated ubiquitination sites were enriched in immune and inflammatory pathways, whereas their downregulated counterparts were enriched in vascular smooth muscle contraction and cytoskeletal regulation. To identify candidate ubiquitination-driven regulatory nodes, we applied a multi-layer filtering strategy. Protein–protein interaction network analysis identified TLN1, ITGB2, DMD, VCAM1, and SYK as the top five hub proteins among differentially expressed proteins. Among these, SYK showed concurrent upregulation at both the protein and ubiquitination levels and occupied a central position within an ITGAM–SYK–CRK functional module linked to Fcγ R-mediated phagocytosis and cytoskeletal regulation. UbiBrowser 2.0 analysis further revealed that SYK was simultaneously targeted by multiple predicted E3 ligases (CBL, CBLB, NEDD4) and a predicted deubiquitinase (USP10), placing it at the intersection of ubiquitin conjugation and removal networks, a property not shared by the other hub candidates. This study provides the first proteomic and ubiquitinomic landscape of human AAC and lays a foundation for investigating SYK-centered regulatory mechanisms in AAC.

ORGANISM(S): Homo Sapiens

SUBMITTER: Juntao Yang  

PROVIDER: PXD081329 | iProX | Sun Jul 19 00:00:00 BST 2026

REPOSITORIES: iProX