Distribution of membrane cofactor protein of complement on human peripheral blood cells. An altered form is found on granulocytes

Seya, Tsukasa; Ballard, L.; Bora, Nalini S.; Kumar, Vijaya B.; Cui, Wenying; Atkinson, John P.

doi:10.1002/eji.1830180821

Cited by 93 publications

(48 citation statements)

References 23 publications

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“…Mouse monoclonal antibodies (clones GB24 and TRA-2-10) and rabbit polyclonal antibodies to human CD46 have been described elsewhere (14,30,37,59). Mouse monoclonal antibodies (clone E4.3) against human CD46 were purchased from Ancell, Bayport, Minn.…”

Section: Methodsmentioning

confidence: 99%

Adenovirus Type 11 Uses CD46 as a Cellular Receptor

Segerman

Atkinson

Marttila

et al. 2003

J Virol

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252

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Section: Methodsmentioning

confidence: 99%

Adenovirus Type 11 Uses CD46 as a Cellular Receptor

Segerman

Atkinson

Marttila

et al. 2003

J Virol

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308

252

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“…This upper band of Jurkat migrates faster than that of ME-180. MCP displays a characteristic microheterogeneity of M r due to variations in glycosylation among cell types (34,44), and most epithelial-derived cells are a few kDa larger than peripheral blood cells or cell lines. Thus, the RT-PCR results in Fig.…”

Section: Mcp Isoforms Expressed By Jurkat and Me-180 Cellsmentioning

confidence: 99%

Membrane Cofactor Protein (MCP; CD46): Isoform-Specific Tyrosine Phosphorylation

Wang

Liszewski

Chan

et al. 2000

The Journal of Immunology

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Membrane cofactor protein (MCP; CD46) is a widely expressed type 1 transmembrane glycoprotein that inhibits complement activation on host cells. It also is a receptor for several pathogens including measles virus, Streptococcus pyogenes, Neisseria gonorrhea, and Neisseria meningitidis. That MCP may have signaling capability was suggested by its microbial interactions. That is, binding of MCP on human monocytes by measles virus hemagglutinin or cross-linking by an anti-MCP Ab resulted in IL-12 down-regulation, while binding to MCP by Neisseria on epithelial cells produced a calcium flux. Through alternative splicing, MCP is expressed on most cells with two distinct cytoplasmic tails of 16 (CYT-1) or 23 (CYT-2) amino acids. These play pivotal roles in intracellular precursor processing and basolateral localization. We investigated the putative signal transduction pathway mediated by MCP and demonstrate that CYT-2, but not CYT-1, is phosphorylated on tyrosine. We examined MCP tail peptides and performed Ab cross-linking experiments on several human cell lines and MCP isoform transfectants. We found an MCP peptide of CYT-2 was phosphorylated by a src kinase system. Western blots of the cells lines demonstrated that cells bearing CYT-2 were also phosphorylated on tyrosine. Additionally, we provide genetic and biochemical evidence that the src family of kinases is responsible for the latter phosphorylation events. In particular, the src kinase, Lck, is required for phosphorylation of MCP in the Jurkat T cell line. Taken together, these studies suggest a src family-dependent pathway for signaling through MCP.

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“…CD46 is diffusely distributed in the human body and is found on endothelial and epithelial cells, ®broblasts and almost all human blood cells except for erythrocytes [1,20,21]. With regard to variants of sCD46, two groups of sCD46 of different molecular weights whose origins are assumed to be different have been detected [5].…”

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confidence: 99%

Elevated serum levels of soluble membrane cofactor protein (CD46, MCP) in patients with systemic lupus erythematosus (SLE)

Kawano

Seya

Koni

et al. 1999

Clinical and Experimental Immunology

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SUMMARYMembrane cofactor protein (MCP, CD46) is a cell surface complement regulatory protein which acts as a cofactor for the factor I-mediated cleavage of the activated complement components C3b/C4b. To evaluate the clinical usefulness of serum soluble CD46 as a marker of disease activity in patients with SLE, serum levels of sCD46 were measured by ELISA, using two MoAbs (M160 and M177), each of which recognized two different epitopes on CD46 molecule in SLE, other autoimmune diseases and healthy controls. Serum sCD46 levels in active SLE patients (30´5 6 14´1 ng/ml) were signi®cantly higher than those of inactive SLE (5´8 6 7´1 ng/ml; P 0´0003), rheumatoid arthritis (14´9 6 11´6 ng/ ml; P 0´0218), primary Sjo Ègren's syndrome (12´3 6 11´6 ng/ml; P 0´0039) and normal controls (7´3 6 3´6 ng/ml; P 0´0005). The elevated serum sCD46 levels in active SLE patients signi®cantly decreased from 30´5 6 14´1 ng/ml to 8´0 6 6´3 ng/ml after effective corticosteroid and immunosuppressant therapy (P 0´018). Additionally, we found a signi®cant negative association between increasing concentration of sCD46 and decreasing levels of CH50 in SLE (r ±0´598, P 0´0009). These results suggest that sCD46 re¯ects in vivo activation of complement system and provides an additional useful serum parameter of active SLE.

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Distribution of membrane cofactor protein of complement on human peripheral blood cells. An altered form is found on granulocytes

Cited by 93 publications

References 23 publications

Adenovirus Type 11 Uses CD46 as a Cellular Receptor

Adenovirus Type 11 Uses CD46 as a Cellular Receptor

Membrane Cofactor Protein (MCP; CD46): Isoform-Specific Tyrosine Phosphorylation

Elevated serum levels of soluble membrane cofactor protein (CD46, MCP) in patients with systemic lupus erythematosus (SLE)

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