ArticleThe Journal of biological chemistry2012
Studies of the pattern recognition molecule H-ficolin: specificity and purification.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers, 1 of them a synthesis that pooled it.
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Who cites it
19 citing papers in PubMed, 1 synthesis or guideline pooled it, 37 citations in OpenAlex.
- Ficolin-3 Deficiency Is Associated with Disease and an Increased Risk of Systemic Lupus Erythematosus.Journal of clinical immunology · 2019Pooled it
- Investigations on collectin liver 1.The Journal of biological chemistry · 2013Trial
- Divergent host humoral innate immune response to the smooth-to-rough adaptation ofFrontiers in cellular and infection microbiology · 2025Article
- Ficolin-3 induces apoptosis and suppresses malignant property of hepatocellular carcinoma cells via the complement pathway.Life sciences · 2024Article
- The Lectin Pathway of the Complement System-Activation, Regulation, Disease Connections and Interplay with Other (Proteolytic) Systems.International journal of molecular sciences · 2024Review
- Crystal structures of human immune protein FIBCD1 suggest an extended binding site compatible with recognition of pathogen-associated carbohydrate motifs.The Journal of biological chemistry · 2024Article
- The pattern-recognition molecule H-ficolin in relation to diabetic kidney disease, mortality, and cardiovascular events in type 1 diabetes.Scientific reports · 2021Observational
- Mesangial C4d deposition is independently associated with poor renal survival in patients with primary focal segmental glomerulosclerosis.Clinical and experimental nephrology · 2019Article
- Thiol isomerase ERp57 targets and modulates the lectin pathway of complement activation.The Journal of biological chemistry · 2019Article
- Ficolins and the Recognition of Pathogenic Microorganisms: An Overview of the Innate Immune Response and Contribution of Single Nucleotide Polymorphisms.Journal of immunology research · 2019Review
- Article
- H-ficolin binds Aspergillus fumigatus leading to activation of the lectin complement pathway and modulation of lung epithelial immune responses.Immunology · 2015Article
- A novel IgM-H-ficolin complement pathway to attack allogenic cancer cells in vitro.Scientific reports · 2015Article
- Article
- Oxidative stress sensitizes retinal pigmented epithelial (RPE) cells to complement-mediated injury in a natural antibody-, lectin pathway-, and phospholipid epitope-dependent manner.The Journal of biological chemistry · 2013Article
- Mitochondria and the lectin pathway of complement.The Journal of biological chemistry · 2013Article
- M-ficolin binds selectively to the capsular polysaccharides of Streptococcus pneumoniae serotypes 19B and 19C and of a Streptococcus mitis strain.Infection and immunity · 2013Article
- Human H-ficolin inhibits replication of seasonal and pandemic influenza A viruses.Journal of immunology (Baltimore, Md. : 1950) · 2012Article
- The salivary scavenger and agglutinin binds MBL and regulates the lectin pathway of complement in solution and on surfaces.Frontiers in immunology · 2012Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ficolins are pattern recognition molecules of the innate immune system. H-ficolin is found in plasma associated with mannan-binding lectin-associated serine proteases (MASPs). When H-ficolin binds to microorganisms the MASPs are activated, which in turn activate the complement system. H-ficolin is the most abundant ficolin in humans, yet its ligand binding characteristics and biological role remain obscure. We examined the binding of H-ficolin to Aerococcus viridans as well as to a more defined artificial target, i.e. acetylated bovine serum albumin. A strict dependence for calcium ions and inhibition at high NaCl concentration was found. The binding to acetylated bovine serum albumin was inhibited by acetylsalicylic acid and sodium acetate as well as by N-acetylated glucosamine and galactosamine (GlcNAc and GalNAc) and glycine (GlyNAc). The binding to A. viridans was sensitive to the same compounds, but, importantly, higher concentrations were needed for inhibition. N-Acetylated cysteine was also inhibitory, but this inhibition was parallel with reduction in the oligomerization of H-ficolin and thus represents structural changes of the molecule. Based on our findings, we developed a procedure for the purification of H-ficolin from serum, involving PEG precipitation, affinity chromatography on Sepharose derivatized with acetylated serum albumin, ion exchange chromatography, and gel permeation chromatography. The purified H-ficolin was observed to elute at 700 kDa, similar to what we find for H-ficolin in whole serum. MASP-2 was co-purified with H-ficolin, and the purified H-ficolin·MASP-2 complex could activate complement as measured by cleavage of complement factor C4. This study extends our knowledge of the specificity of this pattern recognition molecule, and the purified product will enable further studies.
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