A second serine protease associated with mannan-binding lectin that activates complement

Thiel, Steffen; Vorup-Jensen, Thomas; Stover, Cordula M.; Schwaeble, Wilhelm; Laursen, Steen; Poulsen, Knud; Willis, Anthony C.; Eggleton, Paul; Hansen, Søren; Holmskov, Uffe; Jensenius, Jens C.

doi:10.1016/s0165-2478(97)85069-9

Cited by 126 publications

(165 citation statements)

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“…In the present study, the binding to MASP-1/3 and mannan was seen only with the largermolecular form of MBL but not with the smaller one, which was consistent with this description. MASP-1 and MASP-2 were found to co-elute largely with the highmolecular-mass MBL (750 kDa) on Superose 6 gel filtration [46]. Further, it was reported that MBL/MASP-2 complex, which was reconstituted between MBL and recombinant MASP-2, was eluted on gel filtration chromatography at the position corresponding to the largermolecular form of MBL [47].…”

Section: Discussionmentioning

confidence: 96%

Relationship between gene polymorphisms of mannose‐binding lectin (MBL) and two molecular forms of MBL

et al. 2003

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Mannose-binding lectin (MBL) activates complement through MBL-associated serine proteases (MASP). A deficiency in MBL due to mutations at exon 1 of the human MBL gene is reported to cause vulnerability to infection. We examined sera of known MBL genotype by gel filtration and assessed their elution patterns using an ELISA for MBL and identified two MBL forms, a high-molecular-mass form and a lower-molecular-mass form. By the identification of either or both forms in individual sera, three types of patterns emerged: type 1 consisted of a high-molecular form; type 2, of a low-molecular form; and type 3, of both forms. Types 1, 2 and 3 corresponded, respectively, to a wild type (A/A), a homozygous mutation at codon 54 (B/B) and their heterozygote (A/B). One exception was a heterozygous LXPA/LYPB phenotype that exhibited the type-2 pattern. Binding to mannan and MASP-1/3 occurred exclusively with the high-molecular form. An apparent MBL deficiency does not in fact represent a deficiency in MBL molecules but rather the presence of circulating oligomeric mutant MBL with impaired function.

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Section: Discussionmentioning

confidence: 96%

Relationship between gene polymorphisms of mannose‐binding lectin (MBL) and two molecular forms of MBL

et al. 2003

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“…13 However, further studies showed that two other proteases, MASP-2 and MASP-3, and a protein with no protease activity named sMAP or MAP19 were also associated with MBL. [14][15][16][17] It is generally believed that MASP-2 is the initiator of the so-called lectin complement pathway, which is illustrated in Figure 1, while the physiological role of the other MASPs is still uncertain. The MASPs were originally named after MBL, but it has been shown that they additionally form proteolytically active complexes with Ficolin-1 (M-ficolin), Ficolin-2 (L-ficolin) and Ficolin-3 (H-ficolin or Hakata antigen), which are also defence collagens.…”

Section: Historical Backgroundmentioning

confidence: 99%

Mannose-binding lectin and its genetic variants

et al. 2006

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Mannose-binding lectin (MBL) is a collagen-like serum protein that mediates activation of the complement system and is of importance for host defence. Common variant alleles situated both in the promoter and structural region of the human MBL gene (MBL2) influence the stability and the serum concentration of the protein. Epidemiological studies have suggested that genetically determined variation in MBL serum concentration influences the susceptibility to and the course of different types of infections, autoimmune, metabolic and cardiovascular diseases, but this is still a subject of debate. The fact that these genetic variations are very frequent indicates a dual role for MBL in host defence. In this survey, we summarize the current molecular understanding of human MBL genetics.

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“…Ultimately, complement activation generates membrane-lytic complexes, opsonins and inflammatory anaphylatoxins (1). Complement activation through the lectin pathway is initiated upon binding of the mannan-binding lectin (MBL) or ficolin, which complex with C1s-related serine proteases known as MBL-associated serine proteases (MASPs), to common carbohydrate structures on microorganisms (2,(4)(5)(6). The alternative pathway is activated when low "tick-over" of C3 activation is amplified on microbial surfaces (1).…”

Section: Introductionmentioning

confidence: 99%

The Classical and Regulatory Functions of C1q in Immunity and Autoimmunity

et al. 2008

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A classical function of C1q is to bind immune complexes and initiate complement activation producing membrane lytic complexes, opsonins and anaphylatoxins. This classical pathway of complement activation is also elicited when C1q binds some other ligands. Besides complement activation, C1q also regulates cell differentiation, adhesion, migration, activation and survival. C1q deficiency is associated with autoimmunity as well as increased susceptibility to infections. In this article, we discuss the basic properties of C1q, its expression, and classical and regulatory functions. Cellular & Molecular Immunology. 2008;5(1):9-21.

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A second serine protease associated with mannan-binding lectin that activates complement

Cited by 126 publications

References 0 publications

Relationship between gene polymorphisms of mannose‐binding lectin (MBL) and two molecular forms of MBL

Relationship between gene polymorphisms of mannose‐binding lectin (MBL) and two molecular forms of MBL

Mannose-binding lectin and its genetic variants

The Classical and Regulatory Functions of C1q in Immunity and Autoimmunity

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