[Molecular interactions of membrane proteins and erythrocyte deformability].
The structural and functional properties of the erythrocytic membrane constitute one of the essential elements of the red cell deformability. They intervene not only in the flexibility of the membrane, but also in the surface/volume relation and, through transmembrane exchanges, in the internal viscosity of the red cells. These properties depend essentially on the molecular composition of the elements which constitute the membrane, and on their interactions. The shape of the red cell and the flexibility of its membrane depend, to a great extent, on the membrane skeleton, whose main components are spectrin, actin, and protein 4.1. The spectrin basic molecule is a heterodimer, but there occur interactions between dimers in vitro as well as in vivo, which lead to the formation of tetrameric and oligomeric structures of higher complexity. Disturbances of these interactions, such as have been observed in pathological cases, lead to an instability of the membrane, a loss of membrane fragments, and a decrease in the surface/volume relation, with, as a consequence, a reduced deformability. The stability of the membrane skeleton also depends on the interactions between spectrin and protein 4.1. These interactions occur through a binding site on the beta chain of spectrin apparently close to actin and calmodulin binding sites. Other interactions occur between the hydrophobic segment of spectrin and membrane lipids. The cytoskeleton is bound to the transmembrane proteins: by ankyrin to the internal segment of protein band 3, and by protein 4.1 to a glycoprotein named glycoconnectin. There seems to exist other, more direct, lower affinity bindings between the cytoskeleton on the one hand, and band 3 and glycophorin transmembrane proteins on the other hand, whose lateral mobilities are modified when the structure of the skeleton is perturbed. The membrane proteins, which are in contact with the cytosol, interact with the cytosolic proteins, in particular with certain enzymes involved in anaerobic glycolysis and with hemoglobin. The Hb-membrane interactions are complex and involve different binding types with various affinities, as through band 3 protein, phospholipids, and glycophorin. These bindings are particularly important in the case of certain abnormal hemoglobins such as S and C. If the existence of molecular interactions inside the membrane and their sites are fairly well known, the mechanisms which control or influence such interactions remain unknown.(ABSTRACT TRUNCATED AT 400 WORDS)
D000199:Actins / Q000097:blood* / Q000502:physiology; D000255:Adenosine Triphosphate / Q000502:physiology; D001457:Anion Exchange Protein 1, Erythrocyte / Q000502:physiology; D017487:Ankyrins; D001798:Blood Proteins / Q000502:physiology*; D002118:Calcium / Q000502:physiology; D003598:Cytoskeletal Proteins; D003600:Cytosol / Q000201:enzymology; D004910:Erythrocyte Membrane / Q000648:ultrastructure; D004912:Erythrocytes / Q000502:physiology*; D006021:Glycophorins / Q000502:physiology; D006801:Humans; D008565:Membrane Proteins / Q000097:blood* / Q000502:physiology; D009479:Neuropeptides; D010084:Oxidation-Reduction; D010743:Phospholipids / Q000502:physiology; D010766:Phosphorylation; D011485:Protein Binding; D013049:Spectrin / Q000502:physiology*
D000199:Actins; D001457:Anion Exchange Protein 1, Erythrocyte; D017487:Ankyrins; D001798:Blood Proteins; D003598:Cytoskeletal Proteins; D006021:Glycophorins; D008565:Membrane Proteins; D009479:Neuropeptides; D010743:Phospholipids; C028841:erythrocyte membrane band 4.1 protein; C120557:erythrocyte membrane protein band 4.1-like 1; D013049:Spectrin; D000255:Adenosine Triphosphate; D002118:Calcium
Interactions molécularies des protéines de la membrane et déformabilité érythrocytaire.