BIOMAT Database Logo BIOMAT Database Logo

Altered spectrin dimer-dimer association and instability of erythrocyte membrane skeletons in hereditary pyropoikilocytosis. 1981

S C Liu, and J Palek, and J Prchal, and R P Castleberry

Hereditary pyropoikilocytosis (HPP) is a hemolytic anemia characterized by microspherocytosis, poikilocytosis, and an unusual thermal sensitivity of erythrocytes. We have investigated the contribution of abnormal membrane skeletal assembly to these abnormal HPP erythrocyte properties. Skeletons prepared from fresh HPP ghosts with Triton X-100 were considerably more fragile than skeletons from control erythrocytes. Spectrin, the major skeleton component, extracted at 0 degrees C from normal erythrocytes, was present primarily as tetramers and high molecular weight complexes. In contrast, spectrin extracted from HPP erythrocytes under identical conditions contained a significant amount of dimers with a concomitant decrease of tetramers. Furthermore, spectrin dimers from HPP erythrocytes differed from normal spectrin dimers in their failure to reassociate into tetramers both in solution and in the membrane. Presumptive HPP carriers (asymptomatic mothers of the two patients) exhibited a mild but reproducible increase of spectrin dimers in 0 degrees C extracts and a defective reassociation of spectrin dimers of tetramers both in solution and in the membrane. We conclude that in HPP, self-association of spectrin dimers into tetramers is defective, which accounts for the instability of membrane skeletons.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008565 Membrane Proteins Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors. Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D003593 Cytoplasm The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990) Protoplasm,Cytoplasms,Protoplasms
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
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D013049 Spectrin A high molecular weight (220-250 kDa) water-soluble protein which can be extracted from erythrocyte ghosts in low ionic strength buffers. The protein contains no lipids or carbohydrates, is the predominant species of peripheral erythrocyte membrane proteins, and exists as a fibrous coating on the inner, cytoplasmic surface of the membrane. alpha-Spectrin,beta-Spectrin,alpha Spectrin,beta Spectrin
D013103 Spherocytosis, Hereditary A group of familial congenital hemolytic anemias characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. The erythrocytes have increased osmotic fragility and are abnormally permeable to sodium ions. Hereditary Spherocytoses,Spherocytoses, Hereditary
D046911 Macromolecular Substances Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure. Macromolecular Complexes,Macromolecular Compounds,Macromolecular Compounds and Complexes,Complexes, Macromolecular,Compounds, Macromolecular,Substances, Macromolecular

Related Publications

S C Liu, and J Palek, and J Prchal, and R P Castleberry
Elliptical erythrocyte membrane skeletons and heat-sensitive spectrin in hereditary elliptocytosis.
March 1981, Proceedings of the National Academy of Sciences of the United States of America,
S C Liu, and J Palek, and J Prchal, and R P Castleberry
Partial spectrin deficiency in hereditary pyropoikilocytosis.
April 1986, Blood,
S C Liu, and J Palek, and J Prchal, and R P Castleberry
The spectrin-actin junction of erythrocyte membrane skeletons.
January 1989, Biochimica et biophysica acta,
S C Liu, and J Palek, and J Prchal, and R P Castleberry
Direct involvement of spectrin thiols in maintaining erythrocyte membrane thermal stability and spectrin dimer self-association.
July 1988, Biochimica et biophysica acta,
S C Liu, and J Palek, and J Prchal, and R P Castleberry
Molecular basis of spectrin deficiency in hereditary pyropoikilocytosis.
September 1993, Blood,
S C Liu, and J Palek, and J Prchal, and R P Castleberry
Hereditary pyropoikilocytosis and the spectrin St. Claude allele.
January 2004, British journal of haematology,
S C Liu, and J Palek, and J Prchal, and R P Castleberry
Hematologically important mutations: spectrin variants in hereditary elliptocytosis and hereditary pyropoikilocytosis.
January 1996, Blood cells, molecules & diseases,
S C Liu, and J Palek, and J Prchal, and R P Castleberry
On the structure of erythrocyte spectrin in partially expanded membrane skeletons.
July 1990, Proceedings of the National Academy of Sciences of the United States of America,
S C Liu, and J Palek, and J Prchal, and R P Castleberry
[Congenital hemolytic anemia with erythrocyte thermal instability and defect of spectrin tetrameric polymerization. Study of erythrocyte deformability in a new case of hereditary pyropoikilocytosis using diffraction viscosimetry].
January 1983, Nouvelle revue francaise d'hematologie,
S C Liu, and J Palek, and J Prchal, and R P Castleberry
Nonsense mutations of the alpha-spectrin gene in hereditary pyropoikilocytosis.
November 2008, Haematologica,
Copied contents to your clipboard!