Molecular cloning and chromosomal localization of human membrane cofactor protein (MCP). Evidence for inclusion in the multigene family of complement-regulatory proteins.

Lublin, Douglas M.; Liszewski, M. Kathryn; Post, T W; Arce, MA; Beau, Michelle M. Le; Rebentisch, M B; Lemons, L S; Seya, Tsukasa; Atkinson, John P.

doi:10.1084/jem.168.1.181

Cited by 199 publications

(79 citation statements)

References 44 publications

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“…In humans, there are also three cell-associated regulators: DAF, CD59 and the membrane cofactor protein (MCP or CD46). Human DAF and CD59 behave similarly to their murine homologues, whereas the human MCP has activity similar to Crry [21]. DAF inhibits complement activation by accelerating the decay of C3 and C5 convertases [22].…”

Section: Complement Overviewmentioning

confidence: 99%

Effect of complement and its regulation on myasthenia gravis pathogenesis

Kusner¹,

Kaminski²,

Šoltýs³

2008

Expert Review of Clinical Immunology

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Myasthenia gravis (MG) is primarily caused by antibodies directed towards the skeletal muscle acetylcholine receptor, leading to muscle weakness. Although these antibodies may induce compromise of neuromuscular transmission by blocking acetylcholine receptor function or antigenic modulation, the predominant mechanism of injury to the neuromuscular junction is complement-mediated lysis of the postsynaptic membrane. The vast majority of data to support the role of complement derives from experimentally acquired MG (EAMG). In this article, we review studies that demonstrate the central role of complement in EAMG and MG pathogenesis along with the emerging role of complement in T-and B-cell function, as well as the potential for complement inhibitor-based therapy to treat human MG.

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Section: Complement Overviewmentioning

confidence: 99%

Effect of complement and its regulation on myasthenia gravis pathogenesis

Kusner¹,

Kaminski²,

Šoltýs³

2008

Expert Review of Clinical Immunology

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“…The genes for other Sushi domain proteins are located in the same chromosome 1q32 locus. [94][95][96][97][98] …”

Section: Structure Of the Factor XIII Genesmentioning

confidence: 99%

Role of factor XIII in fibrin clot formation and effects of genetic polymorphisms

Ariëns

Lai

Weisel

et al. 2002

Blood

327

272

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Factor XIII and fibrinogen are unusual among clotting factors in that neither is a serine protease. Fibrin is the main protein constituent of the blood clot, which is stabilized by factor XIIIa through an amide or isopeptide bond that ligates adjacent fibrin monomers. Many of the structural and functional features of factor XIII and fibrin(ogen) have been elucidated by protein and gene analysis, site-directed mutagenesis, and x-ray crystallography. However, some of the molecular aspects involved in the complex processes of insoluble fibrin formation in vivo and in vitro remain unresolved. The findings of a relationship between fibrinogen, factor XIII, and cardiovascular or other thrombotic disorders have focused much attention on these 2 proteins. Of particular interest are associations between common variations in the genes of factor XIII and altered risk profiles for thrombosis. Although there is much debate regarding these observations, the implications for our understanding of clot formation and therapeutic intervention may be of major importance. In this review, we have summarized recent findings on the structure and function of factor XIII. This is followed by a review of the effects of genetic polymorphisms on protein structure/function and their relationship to disease. (Blood. 2002;100:743-754)

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“…Both DAF and CD59 are membrane-linked by posttranslationally added GPI anchors (9,11). MCP, although linked by a conventional polypeptide anchor, contains only a short cytoplasmic sequence (12). These anchor structures permit the three regulators to move freely within the plasma membranes of self-cells to efficiently inhibit the progression of the attack sequence wherever complement activation is initiated on their surfaces (4,13).…”

mentioning

confidence: 99%

Decay-Accelerating Factor Deficiency Increases Susceptibility to Dextran Sulfate Sodium-Induced Colitis: Role for Complement in Inflammatory Bowel Disease

Lin¹,

Spencer

Hatala³

et al. 2004

The Journal of Immunology

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Decay-accelerating factor (DAF or CD55) is expressed on colonic epithelial cells but its function in the mucosa is unknown. In humans, a proportion of DAF-deficient (Cromer INAB) patients develop inflammatory bowel disease (IBD). To evaluate how DAF deficiency may contribute to gut inflammation and thus could play a role in IBD pathogenesis, we compared the severity of dextran sulfate sodium-induced colitis in Daf1 gene-targeted and control mice. Seven days after consuming 3% dextran sulfate sodium in their drinking water, Daf1−/− mice suffered markedly greater weight loss (−24.7 ± 7.5% vs −14.2% ± 4.9%), exhibited uniformly bloody diarrhea as compared with soft stool in control mice, developed shortened colons, and had larger spleens. Histological examination of distal colons showed massively increased neutrophilic and mononuclear cell infiltration, greater epithelial cell destruction, and increased ulcerations. Cytokine production in organ cultures of colonic explants showed increased levels of IL-12 and IL-6. Fourteen days after switching back to regular water, in contrast to the Daf1+/+ controls which showed little stool abnormality, all Daf1−/− mice continued to have diarrhea. Organ culture cytokine measurements at this time point, i.e., the end of the recovery phase, showed markedly increased levels of IL-10 (6-fold), IL-12 (4-fold), and IL-6 (2-fold), as well as TNF-α (>10-fold) compared with the controls. Our findings argue that, as shown for IL-10 in IL-10−/− mice and IL-2 in IL-2−/− mice, DAF control of complement additionally is important in regulating gut homeostasis and consequently its activity may participate in protecting against IBD.

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Molecular cloning and chromosomal localization of human membrane cofactor protein (MCP). Evidence for inclusion in the multigene family of complement-regulatory proteins.

Cited by 199 publications

References 44 publications

Effect of complement and its regulation on myasthenia gravis pathogenesis

Effect of complement and its regulation on myasthenia gravis pathogenesis

Role of factor XIII in fibrin clot formation and effects of genetic polymorphisms

Decay-Accelerating Factor Deficiency Increases Susceptibility to Dextran Sulfate Sodium-Induced Colitis: Role for Complement in Inflammatory Bowel Disease

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