It is one of the leading causes of maternal, as well as perinatal morbidity and Dabrafenib in vivo mortality, even in developed countries. Despite intensive research efforts, the aetiology and pathogenesis of pre-eclampsia are not understood completely.

Increasing evidence suggests that an excessive maternal systemic inflammatory response to pregnancy with activation of both the innate and adaptive arms of the immune system is involved in the pathogenesis of the disease [1,2]. We have demonstrated previously that the complement system is activated with increased terminal complex formation in the third trimester of normal human pregnancy, and further in pre-eclampsia, as shown by the elevated amounts of activation markers in the systemic circulation [3]. However, in our recent study, the role of the mannose-binding lectin (MBL)-mediated

lectin pathway has been ruled out in the pathological complement activation observed in pre-eclampsia [4]. Ficolins are pattern recognition molecules of the innate immune system that bind to carbohydrate moieties present on the surface of microbial pathogens, apoptotic and necrotic cells. They act through two distinct routes: by initiating the lectin pathway of complement activation in concert with attached MBL-associated serine proteases (MASPs) and by a primitive opsonophagocytosis [5]. Ficolins are oligomeric proteins consisting of an N-terminal selleck products cysteine-rich region, a collagen-like domain and a C-terminal globular fibrinogen-like domain. The latter is responsible selleck chemical for carbohydrate binding [6]. Three types of ficolins have been identified in humans: ficolin-2 (L-ficolin), ficolin-3 (H-ficolin) and ficolin-1 (M-ficolin). The mRNA of ficolin-2 is expressed primarily

in the liver and its protein product is secreted into the blood circulation. Ficolin-2 exhibits lectin activity toward N-acetyl-glucosamine (GlcNAc) and 1, 3-β-D-glucan. Ficolin-3 mRNA is expressed in the liver and lung. In the liver, ficolin-3 is produced by bile duct epithelial cells and hepatocytes, and is secreted into the bile and circulation. In the lung, ficolin-3 is produced by ciliated bronchial epithelial cells and type II alveolar epithelial cells, and is secreted into the bronchus and alveolus. Ficolin-3 binds to GlcNAc, N-acetyl-galactosamine (GalNAc) and fucose. Ficolin-1 mRNA is expressed in monocytes, the lung and spleen. Its protein product has been identified in secretory granules of neutrophils and monocytes, as well as in type II alveolar epithelial cells. Nevertheless, it is present in the circulation at very low levels compared to ficolin-2 and ficolin-3. Ficolin-1 exhibits binding activity towards GlcNAc, GalNAc and sialic acid [7].