Association between lectin complement pathway initiators, C-reactive protein and left ventricular remodeling in myocardial infarction—A magnetic resonance study

► Ficolin-2, MBL and MAP-1 are regulatory lectin complement pathway (LP) molecules. ► LP was associated with left ventricular (LV) dilatation after myocardial infarction. ► Interaction of ficolin-2 and CRP was associated with infarct size and LV remodeling. ► LP-pentraxin activation might influence ischemic reperfusion injury and remodeling. Lectin complement pathway (LP) activation is an important mechanism in myocardial ischemia reperfusion injury (IRI). LP is activated via the recognition molecules mannose-binding lectin (MBL), ficolins-2 and-3 and is regulated by MBL/Ficolin-associated Protein-1 (MAP-1). Also, C-reactive protein (CRP) and ficolin-2 interact in vitro, but the role of the ficolins in IRI is unknown. In 55 patients with ST segment elevation myocardial infarction, we investigated the association of LP components and CRP in plasma samples with left ventricular (LV) end systolic and diastolic volumes (ESV and EDV) and infarct size, assessed by cardiac magnetic resonance early at 1–3 days after primary percutaneous coronary intervention and at 6 months follow-up. Opposed to MBL, ficolin-3 and MAP-1, ficolin-2 levels were low at baseline. At baseline, ficolin-2>median was associated with ESV and EDV increases by 7.83ml/m2 (p=0.004) and 14.04ml/m2 (pmedian was associated with ESV (11.21ml/m2; p=0.017) and EDV increases (14.72ml/m2; p=0.006). MAP-1median had the greatest LV dilatation (17.61ml/m2). The ficolin-2×CRP interaction variable was positively associated with infarct size and inversely associated with EDV change over 6 months (p=0.006). There was no interaction between CRP and the other LP molecules. The LP initiator molecule ficolin-2 and combinations of ficolin-2, MBL and MAP-1 are associated with LV dilatation after myocardial infarction. Interaction of ficolin-2 and CRP was associated with infarct size and LV remodeling, indicating a potential role for LP and LP-pentraxin cross-activation in IRI and LV remodeling.