Quantitative single particle tracking of NGF-receptor complexes: Transport is bidirectional but biased by longer retrograde run lengths

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The retrograde transport of nerve growth factor (NGF) in neurite-like processes of living differentiated PC12 cells was studied using streptavidin-quantum dots (QDs) coupled to monobiotin-NGF. These reagents were active in differentiation, binding, internalization, and transport. Ten-35% of the QD-N...

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Detalles Bibliográficos
Autores principales: Echarte, M.M., Bruno, L., Arndt-Jovin, D.J., Jovin, T.M., Pietrasanta, L.I.
Formato: JOUR
Materias:
Live cell imaging
Neurotrophins
NGF
Quantum dots
Retrograde axonal transport
nerve growth factor receptor
quantum dot
streptavidin
animal cell
article
cell differentiation
cell labeling
controlled study
imaging
internalization
microtubule
mouse
neurite
nonhuman
priority journal
protein binding
protein transport
quantitative assay
rat
room temperature
velocity
Animals
Chromogenic Compounds
Endocytosis
Microtubules
Multiprotein Complexes
Neurites
PC12 Cells
Protein Binding
Protein Transport
Quantum Dots
Rats
Receptor, Nerve Growth Factor
Sensitivity and Specificity
Staining and Labeling
Substrate Specificity
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00145793_v581_n16_p2905_Echarte
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
Sumario:The retrograde transport of nerve growth factor (NGF) in neurite-like processes of living differentiated PC12 cells was studied using streptavidin-quantum dots (QDs) coupled to monobiotin-NGF. These reagents were active in differentiation, binding, internalization, and transport. Ten-35% of the QD-NGF-receptor complexes were mobile. Quantitative single particle tracking revealed a bidirectional step-like motion, requiring intact microtubules, with a net retrograde velocity of 0.054 ± 0.020 μm/s. Individual runs had a mean velocity of ∼0.15 μm/s at room temperature, and the run times were exponentially distributed. The photostability and brightness of QDs permit extended real-time analysis of individual QDbNGF- receptor complexes trafficking within neurites. © 2007 Federation of European Biochemical Societies.

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