ArticleThe Biochemical journal1990
Isolation and characterization of a membrane-attack-complex-inhibiting protein present in human serum and other biological fluids.
Article in The Biochemical journal, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 65 citations in OpenAlex.
- Phosphotyrosine profiling of human cerebrospinal fluid.Clinical proteomics · 2018Article
- The role of complement in ocular pathology.Seminars in immunopathology · 2008Review
- The role of complement system in ocular diseases including uveitis and macular degeneration.Molecular immunology · 2007Review
- Complement regulatory activity of normal human intraocular fluid is mediated by MCP, DAF, and CD59.Investigative ophthalmology & visual science · 2000Article
- Molecular basis for a link between complement and the vascular complications of diabetes.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Structural composition and functional characterization of soluble CD59: heterogeneity of the oligosaccharide and glycophosphoinositol (GPI) anchor revealed by laser-desorption mass spectrometric analysis.The Biochemical journal · 1996Article
- Enhanced complement susceptibility of avidin-biotin-treated human erythrocytes is a consequence of neutralization of the complement regulators CD59 and decay accelerating factor.The Biochemical journal · 1995Article
- Article
- Cerebrospinal fluid concentrations of the complement MAC inhibitor CD59 in multiple sclerosis and patients with other neurological disorders.Journal of neurology · 1994Article
- Functional and antigenic similarities between a 94-kD protein of Schistosoma mansoni (SCIP-1) and human CD59.The Journal of experimental medicine · 1994Article
- Membrane proteins that protect against complement lysis.Springer seminars in immunopathology · 1994Review
- Platelet activation releases megakaryocyte-synthesized apolipoprotein J, a highly abundant protein in atheromatous lesions.The American journal of pathology · 1993Article
- Regulation of complement membrane attack complex formation in myocardial infarction.The American journal of pathology · 1993Article
- Physiologic relevance of the membrane attack complex inhibitory protein CD59 in human seminal plasma: CD59 is present on extracellular organelles (prostasomes), binds cell membranes, and inhibits complement-mediated lysis.The Journal of experimental medicine · 1993Article
- Apolipoprotein J expression at fluid-tissue interfaces: potential role in barrier cytoprotection.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- Isolation and characterization of a membrane protein from rat erythrocytes which inhibits lysis by the membrane attack complex of rat complement.The Biochemical journal · 1992Article
- Structural properties of the glycoplasmanylinositol anchor phospholipid of the complement membrane attack complex inhibitor CD59.Clinical and experimental immunology · 1992Article
- Membrane attack complex (MAC)-mediated damage to spermatozoa: protection of the cells by the presence on their membranes of MAC inhibitory proteins.Immunology · 1992Article
- Isolation and characterization of the complement-inhibiting protein CD59 antigen from platelet membranes.The Biochemical journal · 1992Article
- Expression and function of membrane attack complex inhibitory proteins on thyroid follicular cells.Immunology · 1992Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
We have previously reported the isolation of a membrane-attack-complex-inhibiting protein (MIP) from human erythrocyte membranes [Watts, Patel & Morgan (1987) Complement 4, 236] and the production of polyclonal antibodies to this protein. Here we report the identification in plasma, urine, saliva and cerebrospinal fluid of a protein immunochemically identical with the membrane-derived MIP. The protein has been isolated from plasma by immunoaffinity chromatography on an anti-(erythrocyte MIP)-Sepharose column and shown by SDS/polyacrylamide-gel electrophoresis to be of similar molecular mass to the erythrocyte protein (55 kDa non-reduced and 65 kDa under reducing conditions). Monoclonal antibodies have been raised against plasma MIP and used to establish a two-site enzyme-linked immunoadsorbent assay, enabling quantification of MIP in plasma, urine and cerebrospinal fluid. Plasma MIP, though not able to incorporate spontaneously into membranes, was deposited on heterologous and homologous erythrocyte membranes during complement activation in a C8-dependent manner. Depletion of MIP from plasma resulted in enhancement of the lytic capacity of the plasma on heterologous erythrocytes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.