Biological ion exchanger resins. X. The cytotonus hypothesis: biological contractility and the total regulation of cellular physiology through quantitative control of cell water.
Actin-like (A-L) fraction from normal E. coli was compared with the protein from a potassium-transport mutant strain, and the cell-swelling reaction of both strains was studied. Findings were: (a) The membrane fraction of the mutant by SDS electrophoresis is deficient in the A-L fragment relative to normal whereas the soluble supernatant contains an excess. (b) Important catalytic differences exist between the A-L fractions of the two strains. The parent strain accumulates potassium in low K+ and the A-L fraction polymerizes in low K+. But the A-L fraction from the mutant fails to polymerize in low K media in the K+ concentration region where the mutant fails at K+ uptake. (c) The parent cell swells during low K+ uptake whereas the mutant does not. It is constructed from this that the differences in the characterization of A-L fraction relative to normal are related to the loss of cell-swelling in the mutant and hence to the loss in alkali cation selectivity. Thus two physical mechanisms, one macroscopic and dependent on the Gregor relation for swelling equilibria in ion exchange resins, and one more microscopic based on the dielectric dependence of the coulomb force between ion pairs, could underly regulation of ion selectivity by cell swelling. A similar proposal is made for the regulation of electron transport and oxidative phosphorylation in mitochondria. These findings and interpretations justify a new hypothesis to the effect that cell hydration is regulated by contractile proteins. The hypothesis fits together important observations hitherto unexplained, to wit: (1) The "missing link" as to the role of intermediate metabolism in biological ion exchange. (2) The swelling of bacterial protoplasts and its relation to (Mg2 + Ca2+)ATPase activity. (3) The swelling-contraction cycles of mitochondria and their role in electron transport. (4) The role of ATPase's in transport. (5) The significance of actomyosin fibers in nerve endings. (6) The significance of altered actomyosin structures in the cancerous cell.
D000199:Actins / Q000502:physiology*; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D001426:Bacterial Proteins / Q000502:physiology*; D001693:Biological Transport, Active; D001826:Body Fluids / Q000502:physiology*; D003285:Contractile Proteins / Q000502:physiology; D004548:Elasticity; D004553:Electric Conductivity; D004579:Electron Transport; D004926:Escherichia coli / Q000502:physiology* / Q000648:ultrastructure; D007424:Intracellular Fluid / Q000502:physiology*; D007475:Ion Exchange Resins; D008565:Membrane Proteins / Q000502:physiology; D008854:Microscopy, Electron; D008928:Mitochondria / Q000378:metabolism / Q000648:ultrastructure; D008933:Mitochondrial Swelling; D008954:Models, Biological; D010085:Oxidative Phosphorylation; D010641:Phenotype; D011188:Potassium / Q000378:metabolism; D013045:Species Specificity; D013053:Spectrophotometry
D000199:Actins; D001426:Bacterial Proteins; D003285:Contractile Proteins; D007475:Ion Exchange Resins; D008565:Membrane Proteins; D000251:Adenosine Triphosphatases; D011188:Potassium