title: Modulation of actin polymerization by the spectrin-band 4.1 complex.
abstract: The effect of human erythrocyte spectrin dimer and band 4.1 on the polymerization of actin was studied by two independent methods: by following the increase in fluorescence of actin covalently conjugated to N-pyrenyl-iodoacetamide (pyrenylactin) and by following the increase in light scattered by actin polymers. Both techniques indicated that the complex of spectrin dimer and band 4.1, but neither spectrin nor band 4.1 alone, stimulates the rate of nucleation (decreases the lag phase of polymerization) and stabilizes oligomers of F-actin. While the band 4.1-spectrin complex, but not spectrin alone, had no immediate effect on the rate of polymerization after the lag phase, it eventually decreases the rate of actin filament growth when the molecular ratio of actin-spectrin-band 4.1 approaches the physiological range. The complex has no detectable effect on the critical actin concentration and does not significantly alter the apparent order of the nucleation reaction.
mesh_terms: D000199:Actins / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D001798:Blood Proteins / Q000494:pharmacology*; D003598:Cytoskeletal Proteins; D004910:Erythrocyte Membrane; D006801:Humans; D008027:Light; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000494:pharmacology*; D009132:Muscles / Q000378:metabolism; D009479:Neuropeptides; D011817:Rabbits; D012542:Scattering, Radiation; D013049:Spectrin / Q000494:pharmacology*; D013050:Spectrometry, Fluorescence; D014783:Viscosity
chemical_list: D000199:Actins; D001798:Blood Proteins; D003598:Cytoskeletal Proteins; D046911:Macromolecular Substances; D008565:Membrane Proteins; D009479:Neuropeptides; C028841:erythrocyte membrane band 4.1 protein; C120557:erythrocyte membrane protein band 4.1-like 1; D013049:Spectrin