BIOMAT Database Logo BIOMAT Database Logo

Complement lysis of human erythrocytes. III. Differing effectiveness of human and guinea pig C9 on normal and paroxysmal nocturnal hemoglobinuria cells. 1980

S I Rosenfeld, and C H Packman, and D E Jenkins, and J K Countryman, and J P Leddy

UI MeSH Term Description Entries
D003165 Complement System Proteins Serum glycoproteins participating in the host defense mechanism of COMPLEMENT ACTIVATION that creates the COMPLEMENT MEMBRANE ATTACK COMPLEX. Included are glycoproteins in the various pathways of complement activation (CLASSICAL COMPLEMENT PATHWAY; ALTERNATIVE COMPLEMENT PATHWAY; and LECTIN COMPLEMENT PATHWAY). Complement Proteins,Complement,Complement Protein,Hemolytic Complement,Complement, Hemolytic,Protein, Complement,Proteins, Complement,Proteins, Complement System
D003182 Complement C5 C5 plays a central role in both the classical and the alternative pathway of COMPLEMENT ACTIVATION. C5 is cleaved by C5 CONVERTASE into COMPLEMENT C5A and COMPLEMENT C5B. The smaller fragment C5a is an ANAPHYLATOXIN and mediator of inflammatory process. The major fragment C5b binds to the membrane initiating the spontaneous assembly of the late complement components, C5-C9, into the MEMBRANE ATTACK COMPLEX. C5 Complement,Complement 5,Complement C5, Precursor,Complement Component 5,Precursor C5,Pro-C5,Pro-complement 5,C5, Complement,C5, Precursor,C5, Precursor Complement,Complement, C5,Component 5, Complement,Precursor Complement C5,Pro C5,Pro complement 5
D003185 Complement C8 A 150-kDa serum glycoprotein composed of three subunits with each encoded by a different gene (C8A; C8B; and C8G). This heterotrimer contains a disulfide-linked C8alpha-C8gamma heterodimer and a noncovalently associated C8beta chain. C8 is the next component to bind the C5-7 complex forming C5b-8 that binds COMPLEMENT C9 and acts as a catalyst in the polymerization of C9. C8 Complement,Complement 8,Complement Component 8,Complement Component C8 alpha,Complement Component C8 alpha Chain,Complement Component C8 beta,Complement Component C8 beta Chain,Complement Component C8 gamma,Complement Component C8 gamma Chain,C8, Complement,Complement, C8,Component 8, Complement
D003186 Complement C9 A 63-kDa serum glycoprotein encoded by gene C9. Monomeric C9 (mC9) binds the C5b-8 complex to form C5b-9 which catalyzes the polymerization of C9 forming C5b-p9 (MEMBRANE ATTACK COMPLEX) and transmembrane channels leading to lysis of the target cell. Patients with C9 deficiency suffer from recurrent bacterial infections. C9 Complement,Complement 9,Complement Component 9,C9, Complement,Complement, C9,Component 9, Complement
D004492 Edetic Acid A chelating agent that sequesters a variety of polyvalent cations such as CALCIUM. It is used in pharmaceutical manufacturing and as a food additive. EDTA,Edathamil,Edetates,Ethylenediaminetetraacetic Acid,Tetracemate,Calcium Disodium Edetate,Calcium Disodium Versenate,Calcium Tetacine,Chelaton 3,Chromium EDTA,Copper EDTA,Coprin,Dicobalt EDTA,Disodium Calcitetracemate,Disodium EDTA,Disodium Ethylene Dinitrilotetraacetate,Distannous EDTA,Edetate Disodium Calcium,Edetic Acid, Calcium Salt,Edetic Acid, Calcium, Sodium Salt,Edetic Acid, Chromium Salt,Edetic Acid, Dipotassium Salt,Edetic Acid, Disodium Salt,Edetic Acid, Disodium Salt, Dihydrate,Edetic Acid, Disodium, Magnesium Salt,Edetic Acid, Disodium, Monopotassium Salt,Edetic Acid, Magnesium Salt,Edetic Acid, Monopotassium Salt,Edetic Acid, Monosodium Salt,Edetic Acid, Potassium Salt,Edetic Acid, Sodium Salt,Ethylene Dinitrilotetraacetate,Ethylenedinitrilotetraacetic Acid,Gallium EDTA,Magnesium Disodium EDTA,N,N'-1,2-Ethanediylbis(N-(carboxymethyl)glycine),Potassium EDTA,Stannous EDTA,Versenate,Versene,Acid, Edetic,Acid, Ethylenediaminetetraacetic,Acid, Ethylenedinitrilotetraacetic,Calcitetracemate, Disodium,Dinitrilotetraacetate, Disodium Ethylene,Dinitrilotetraacetate, Ethylene,Disodium Versenate, Calcium,EDTA, Chromium,EDTA, Copper,EDTA, Dicobalt,EDTA, Disodium,EDTA, Distannous,EDTA, Gallium,EDTA, Magnesium Disodium,EDTA, Potassium,EDTA, Stannous,Edetate, Calcium Disodium,Ethylene Dinitrilotetraacetate, Disodium,Tetacine, Calcium,Versenate, Calcium Disodium
D004912 Erythrocytes Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN. Blood Cells, Red,Blood Corpuscles, Red,Red Blood Cells,Red Blood Corpuscles,Blood Cell, Red,Blood Corpuscle, Red,Erythrocyte,Red Blood Cell,Red Blood Corpuscle
D006168 Guinea Pigs A common name used for the genus Cavia. The most common species is Cavia porcellus which is the domesticated guinea pig used for pets and biomedical research. Cavia,Cavia porcellus,Guinea Pig,Pig, Guinea,Pigs, Guinea
D006457 Hemoglobinuria, Paroxysmal A condition characterized by the recurrence of HEMOGLOBINURIA caused by intravascular HEMOLYSIS. In cases occurring upon cold exposure (paroxysmal cold hemoglobinuria), usually after infections, there is a circulating antibody which is also a cold hemolysin. In cases occurring during or after sleep (paroxysmal nocturnal hemoglobinuria), the clonal hematopoietic stem cells exhibit a global deficiency of cell membrane proteins. Paroxysmal Cold Hemoglobinuria,Paroxysmal Nocturnal Hemoglobinuria,Marchiafava-Micheli Syndrome,Paroxysmal Hemoglobinuria,Paroxysmal Hemoglobinuria, Cold,Paroxysmal Hemoglobinuria, Nocturnal,Cold Paroxysmal Hemoglobinuria,Hemoglobinuria, Cold Paroxysmal,Hemoglobinuria, Nocturnal Paroxysmal,Hemoglobinuria, Paroxysmal Cold,Hemoglobinuria, Paroxysmal Nocturnal,Marchiafava Micheli Syndrome,Nocturnal Paroxysmal Hemoglobinuria,Syndrome, Marchiafava-Micheli
D006461 Hemolysis The destruction of ERYTHROCYTES by many different causal agents such as antibodies, bacteria, chemicals, temperature, and changes in tonicity. Haemolysis,Extravascular Hemolysis,Intravascular Hemolysis,Extravascular Hemolyses,Haemolyses,Hemolyses, Extravascular,Hemolyses, Intravascular,Hemolysis, Extravascular,Hemolysis, Intravascular,Intravascular Hemolyses
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man

Related Publications

S I Rosenfeld, and C H Packman, and D E Jenkins, and J K Countryman, and J P Leddy
Enhanced complement-mediated lysis of type III paroxysmal nocturnal hemoglobinuria erythrocytes involves increased C9 binding and polymerization.
August 1985, Proceedings of the National Academy of Sciences of the United States of America,
S I Rosenfeld, and C H Packman, and D E Jenkins, and J K Countryman, and J P Leddy
On the lysis of paroxysmal nocturnal hemoglobinuria erythrocytes by complement: dual role of C3b.
October 1982, Blut,
S I Rosenfeld, and C H Packman, and D E Jenkins, and J K Countryman, and J P Leddy
Differential susceptibility of type III erythrocytes of paroxysmal nocturnal hemoglobinuria to lysis mediated by complement and perforin.
July 1989, Biochemical and biophysical research communications,
S I Rosenfeld, and C H Packman, and D E Jenkins, and J K Countryman, and J P Leddy
Enhanced reactive lysis of paroxysmal nocturnal hemoglobinuria erythrocytes. Studies on C9 binding and incorporation into high molecular weight complexes.
October 1986, The Journal of experimental medicine,
S I Rosenfeld, and C H Packman, and D E Jenkins, and J K Countryman, and J P Leddy
Differences in the terminal steps of complement lysis of normal and paroxysmal nocturnal hemoglobinuria red cells.
February 1978, Blood,
S I Rosenfeld, and C H Packman, and D E Jenkins, and J K Countryman, and J P Leddy
Immune lysis of normal human and paroxysmal nocturnal hemoglobinuria (PNH) red blood cells. 3. The membrane defects caused by complement lysis.
June 1966, The Journal of experimental medicine,
S I Rosenfeld, and C H Packman, and D E Jenkins, and J K Countryman, and J P Leddy
Lysis of paroxysmal nocturnal hemoglobinuria erythrocytes by acid-activated serum.
March 1983, Immunobiology,
S I Rosenfeld, and C H Packman, and D E Jenkins, and J K Countryman, and J P Leddy
Complement-mediated lysis in different cationic media of erythrocytes from patients with paroxysmal nocturnal hemoglobinuria.
January 1974, Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.),
S I Rosenfeld, and C H Packman, and D E Jenkins, and J K Countryman, and J P Leddy
Leukocyte antigen-antibody reaction and lysis of paroxysmal nocturnal hemoglobinuria erythrocytes.
September 1970, Blood,
S I Rosenfeld, and C H Packman, and D E Jenkins, and J K Countryman, and J P Leddy
Effect of heparin on complement activation and lysis of paroxysmal nocturnal hemoglobinuria (PNH) red cells.
August 1977, Blood,
Copied contents to your clipboard!