4.7 Article

Apolipoprotein Signature of HDL and LDL from Atherosclerotic Patients in Relation with Carotid Plaque Typology: A Preliminary Report

期刊

BIOMEDICINES
卷 9, 期 9, 页码 -

出版社

MDPI
DOI: 10.3390/biomedicines9091156

关键词

lipoproteomics; atherosclerosis; plaque instability

资金

  1. University of Sassari
  2. Regione Autonoma della Sardegna [10.5.12-C.U.P. J86C18000270002]
  3. Ministero dell'Istruzione, dell'Universita e della Ricerca (MIUR) [AIM1874325-3, CUP: J54I18000110001]

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Proteins within different lipoprotein classes play a key role in carrying out various functions and are associated with pathological conditions such as atherosclerosis. Detailed information about the composition and structure of these lipoproteins can contribute to understanding the mechanisms of atherosclerosis.
In the past years, it has become increasingly clear that the protein cargo of the different lipoprotein classes is largely responsible for carrying out their various functions, also in relation to pathological conditions, including atherosclerosis. Accordingly, detailed information about their apolipoprotein composition and structure may contribute to the revelation of their role in atherogenesis and the understanding of the mechanisms that lead to atherosclerotic degeneration and toward vulnerable plaque formation. With this aim, shotgun proteomics was applied to identify the apolipoprotein signatures of both high-density and low-density lipoproteins (HDL and LDL) plasma fractions purified from healthy volunteers and atherosclerotic patients with different plaque typologies who underwent carotid endarterectomy. By this approach, two proteins with potential implications in inflammatory, immune, and hemostatic pathways, namely, integrin beta-2 (P05107) and secretoglobin family 3A member 2 (Q96PL1), have been confirmed to belong to the HDL proteome. Similarly, the list of LDL-associated proteins has been enriched with 21 proteins involved in complement and coagulation cascades and the acute-phase response, which potentially double the protein species of LDL cargo. Moreover, differential expression analysis has shown protein signatures specific for patients with hard or soft plaques.

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