Turing patterns inside cells

• Autores: Strier, D.E.; Dawson, S.P.
• Año de publicación: 2007
• Idioma: inglés
• Tipo de recurso: artículo
• Fuente: PLoS ONE 2007;2(10)
• Materia: 6 phosphofructokinase; adenosine diphosphate; adenosine triphosphate; 6 phosphofructokinase; adenosine diphosphate; adenosine triphosphate; animal cell; article; catalysis; cell division; cell metabolism; cell size; concentration response; diffusion coefficient; enzyme kinetics; enzyme mechanism; glycolysis; mathematical computing; molecular mechanics; nonhuman; oscillation; protein protein interaction; regulatory mechanism; steady state; yeast; biological model; biophysics; chemical model; chemistry; diffusion; glycolysis; metabolism; methodology; morphogenesis; oscillometry; theoretical model; Adenosine Diphosphate; Adenosine Triphosphate; Biophysics; Catalysis; Cell Division; Diffusion; Glycolysis; Models, Biological; Models, Chemical; Models, Theoretical; Morphogenesis; Oscillometry; Phosphofructokinases
• Institución: Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales

Concentration gradients inside cells are involved in key processes such as cell division and morphogenesis. Here we show that a model of the enzymatic step catalized by phosphofructokinase (PFK), a step which is responsible for the appearance of homogeneous oscillations in the glycolytic pathway, displays Turing patterns with an intrinsic length-scale that is smaller than a typical cell size. All the parameter values are fully consistent with classic experiments on glycolytic oscillations and equal diffusion coefficients are assumed for ATP and ADP. We identify the enzyme concentration and the glycolytic flux as the possible regulators of the pattern. To the best of our knowledge, this is the first closed example of Turing pattern formation in a model of a vital step of the cell metabolism, with a built-in mechanism for changing the diffusion length of the reactants, and with parameter values that are compatible with experiments. Turing patterns inside cells could provide a check-point that combines mechanical and biochemical information to trigger events during the cell division process. © 2007 Strier, Ponce Dawson.
Fil:Strier, D.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Dawson, S.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.