Tricaprilin (CER-0001) for the preventive treatment of migraine: A phase 2 randomised, double-blind, placebo-controlled pilot study.

Background: Increasing evidence indicates a metabolic etiology for migraines, with ketosis potentially rectifying metabolic and clinical features. We conducted a pilot study to evaluate CER-0001, a ketogenic agent, for migraine prevention without dietary changes.

Methods: This was a 2-part, double-blind, randomised, placebo-controlled study conducted in Australia.

Severe fibrosis in hepatitis C virus-infected patients is associated with increased activity of the mannan-binding lectin (MBL)/MBL-associated serine protease 1 (MASP-1) complex.

Mannan-binding lectin (MBL) binds microorganisms via interactions with glycans on the target surface. Bound MBL subsequently activates MBL-associated serine protease proenzymes (MASPs). A role for MBL in hepatitis C virus (HCV) infection had been indicated by previous studies examining MBL levels and polymorphisms in relation to disease progression and response to treatment.

Discrete MBL-MASP complexes show wide inter-individual variability in concentration: data from UK vs Armenian populations.

Mannan-binding lectin (MBL) circulates in plasma in complex with MBL-associated serine proteases (MASP) -1, -2 and -3 and a smaller component, MAp19. When MBL binds to the surface of foreign material (microorganisms), MASP-1, -2, -3 are activated. MASP-2 then activates the complement system.

Heterogeneity of MBL-MASP complexes.

In order to study aspects of the stoichiometry and composition of human MBL-MASP complexes in the population, MBL-MASP complexes were bound from sera of 152 healthy individuals onto mannan-coated microtitre plates. Bound mannan-binding lectin (MBL) was measured by ELISA, and the enzyme activities of MBL-bound MASP-1 and MASP-2 were measured by an amidolytic assay and a C4 fixation assay, respectively. MASP-1 activity correlated with MBL concentration, as did MASP-2 activity (in both cases: p<0.

Immune evasion by a staphylococcal complement inhibitor that acts on C3 convertases.

The complement system is pivotal in host defense but also contributes to tissue injury in several diseases. The assembly of C3 convertases (C4b2a and C3bBb) is a prerequisite for complement activation. The convertases catalyze C3b deposition on activator surfaces.

Composition of the lectin pathway of complement in Gallus gallus: absence of mannan-binding lectin-associated serine protease-1 in birds.

The lectin pathway of complement is activated by multimolecular complexes that recognize and bind to microbial polysaccharides. These complexes comprise a multimeric carbohydrate recognition subunit (either mannan-binding lectin (MBL) or a ficolin), three MBL-associated serine proteases (MASP-1, -2, and -3), and MAp19 (a truncated product of the MASP-2 gene). In this study we report the cloning of chicken MASP-2, MASP-3, and MAp19 and the organization of their genes and those for chicken MBL and a novel ficolin.

Differential substrate and inhibitor profiles for human MASP-1 and MASP-2.

The mannan-binding lectin (MBL)-associated serine proteases (MASPs) circulate in serum complexed with mannan-binding lectin, a recognition molecule of the complement system. MASP-2 cleaves the complement components C4 and C2 to form the C3 convertase C4b2a. A definitive natural substrate for MASP-1 has not yet been described.

Biochemistry and genetics of mannan-binding lectin (MBL).

Mannose- or mannan-binding lectin (MBL) is a member of the collectin protein family, which includes lung surfactant proteins SP-A and SP-D. Each member consists of similar or identical polypeptide chains with a region of collagen-like sequence followed by a C-type lectin domain. The polypeptides associate in threes to form a subunit containing a collagen-like helix, with three clustered lectin domains.