Biomaterial Database

Paroxysmal nocturnal haemoglobinuria. 1985

W F Rosse, and C J Parker

The analysis of the abnormality of the membrane in paroxysmal nocturnal haemoglobinuria is an exercise in complexity complexified--of Ossa atop Pelion. To understand it, we will need to understand fully the complexities of the complement system and the complexities of the structure of the membrane and the complexity of their concert interaction. Added to this are the complexities of growth and development of the haematopoietic cells--a problem we have not discussed at all despite its importance in the pathophysiology of PNH. It is little wonder that a disease which is uncommon but not rare continues to fascinate investigators from a wide variety of disciplines. If, as has been (falsely) said, more people studied the disease than had it, it would be because it presents questions of such fundamental interest. In unravelling its mysteries, many problems related to the normal functioning of cells, complement and a haematopoiesis have been and will continue to be solved.

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
D003170	Complement Pathway, Alternative	Complement activation initiated by the interaction of microbial ANTIGENS with COMPLEMENT C3B. When COMPLEMENT FACTOR B binds to the membrane-bound C3b, COMPLEMENT FACTOR D cleaves it to form alternative C3 CONVERTASE (C3BBB) which, stabilized by COMPLEMENT FACTOR P, is able to cleave multiple COMPLEMENT C3 to form alternative C5 CONVERTASE (C3BBB3B) leading to cleavage of COMPLEMENT C5 and the assembly of COMPLEMENT MEMBRANE ATTACK COMPLEX.	Alternative Complement Pathway,Properdin Pathway,Alternative Complement Activation Pathway,Complement Activation Pathway, Alternative
D003171	Complement Pathway, Classical	Complement activation initiated by the binding of COMPLEMENT C1 to ANTIGEN-ANTIBODY COMPLEXES at the COMPLEMENT C1Q subunit. This leads to the sequential activation of COMPLEMENT C1R and COMPLEMENT C1S subunits. Activated C1s cleaves COMPLEMENT C4 and COMPLEMENT C2 forming the membrane-bound classical C3 CONVERTASE (C4B2A) and the subsequent C5 CONVERTASE (C4B2A3B) leading to cleavage of COMPLEMENT C5 and the assembly of COMPLEMENT MEMBRANE ATTACK COMPLEX.	Classical Complement Pathway,Classical Complement Activation Pathway,Complement Activation Pathway, Classical
D004910	Erythrocyte Membrane	The semi-permeable outer structure of a red blood cell. It is known as a red cell 'ghost' after HEMOLYSIS.	Erythrocyte Ghost,Red Cell Cytoskeleton,Red Cell Ghost,Erythrocyte Cytoskeleton,Cytoskeleton, Erythrocyte,Cytoskeleton, Red Cell,Erythrocyte Cytoskeletons,Erythrocyte Ghosts,Erythrocyte Membranes,Ghost, Erythrocyte,Ghost, Red Cell,Membrane, Erythrocyte,Red Cell Cytoskeletons,Red Cell Ghosts
D004913	Erythrocytes, Abnormal	Oxygen-carrying RED BLOOD CELLS in mammalian blood that are abnormal in structure or function.	Abnormal Erythrocytes,Abnormal Erythrocyte,Erythrocyte, Abnormal
D006021	Glycophorins	The major sialoglycoprotein of human erythrocyte membranes. It consists of at least two sialoglycopeptides and is composed of 60% carbohydrate including sialic acid and 40% protein. It is involved in a number of different biological activities including the binding of MN blood groups, influenza viruses, kidney bean phytohemagglutinin, and wheat germ agglutinin.	Erythrocyte Sialoglycoproteins,Glycoconnectin,Glycoconnectins,Glycophorin,Glycophorin D,MN Sialoglycoprotein,Red Blood Cell Membrane Sialoglycoprotein,Glycophorin A,Glycophorin A(M),Glycophorin B,Glycophorin C,Glycophorin E,Glycophorin HA,Ss Erythrocyte Membrane Sialoglycoproteins,Ss Sialoglycoprotein,beta-Sialoglycoprotein,Sialoglycoprotein, MN,Sialoglycoprotein, Ss,Sialoglycoproteins, Erythrocyte,beta Sialoglycoprotein
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
D000110	Acetylcholinesterase	An enzyme that catalyzes the hydrolysis of ACETYLCHOLINE to CHOLINE and acetate. In the CNS, this enzyme plays a role in the function of peripheral neuromuscular junctions. EC 3.1.1.7.	Acetylcholine Hydrolase,Acetylthiocholinesterase,Hydrolase, Acetylcholine