Distinct Longitudinal Associations of MBL, MASP-1, MASP-2, MASP-3, and MAp44 With Endothelial Dysfunction and Intima–Media Thickness | Zendy

Elisabeth Hertle | Zendy; Ilja C.W. Arts | Zendy; Carla Kallen | Zendy; Edith J. M. Feskens | Zendy; Casper G. Schalkwijk | Zendy; Ingeborg T. HoffmannPetersen | Zendy; Steffen Thiel | Zendy; Coen D.A. Stehouwer | Zendy; Marleen M. J. van Greevenbroek | Zendy

Open Access

Distinct Longitudinal Associations of MBL, MASP-1, MASP-2, MASP-3, and MAp44 With Endothelial Dysfunction and Intima–Media Thickness

Author(s) -

Elisabeth Hertle,

Ilja C.W. Arts,

Carla Kallen,

Edith J. M. Feskens,

Casper G. Schalkwijk,

Ingeborg T. HoffmannPetersen,

Steffen Thiel,

Coen D.A. Stehouwer,

Marleen M. J. van Greevenbroek

Publication year - 2016

Publication title -

arteriosclerosis thrombosis and vascular biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.007

H-Index - 270

eISSN - 1524-4636

pISSN - 1079-5642

DOI - 10.1161/atvbaha.115.306552

Subject(s) - mannan binding lectin , endothelial dysfunction , lectin pathway , inflammation , intima media thickness , complement system , prospective cohort study , endothelial activation , immunology , medicine , biomarker , lectin , biology , alternative complement pathway , antibody , genetics , carotid arteries

Previous studies suggested that the lectin-complement pathway plays a complex role in cardiovascular disease (CVD). To date, no prospective human studies have investigated the relationship between the initiating factor of the lectin pathway, that is, mannose-binding lectin (MBL), and low-grade inflammation, endothelial dysfunction, or carotid intima-media thickness (cIMT). Moreover, MBL-associated proteases (MASPs) and MBL-associated proteins (MAps), which mediate downstream complement activation, have not been studied in the development of CVD.

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