Spectrin: structure, function, and abnormalities.
A number of proteins that make up the membrane skeleton have been identified, and we have a rough but tantalizing picture of the ways in which they interact to maintain its integrity. An approximate molecular model of spectrin has been proposed, and many new analytic procedures have been developed to search for biochemical variants that may be related to membrane defects. Even at this rudimentary stage of molecular description we have been able to identify structural changes in spectrin that are correlated with pathophysiologic states. The prospects for some genuine insights into the pathogenesis of some congenital hemolytic anemias seem good.
D000745:Anemia, Hemolytic, Congenital / Q000503:physiopathology*; D000818:Animals; D002151:Calorimetry; D002417:Cattle; D004586:Electrophoresis; D004591:Electrophoresis, Polyacrylamide Gel; D004612:Elliptocytosis, Hereditary / Q000503:physiopathology; D006801:Humans; D007122:Immunoelectrophoresis; D051379:Mice; D008854:Microscopy, Electron; D010455:Peptides / Q000032:analysis; D011487:Protein Conformation; D011498:Protein Precursors / Q000032:analysis; D013049:Spectrin / Q000032:analysis / Q000502:physiology*; D013103:Spherocytosis, Hereditary / Q000503:physiopathology; D013329:Structure-Activity Relationship
D010455:Peptides; D011498:Protein Precursors; D013049:Spectrin