Glycosylation is required for maintenance of functional voltage-activated channels in growing neocortical neurons of the rat

C. Zona, F. Eusebi, R. Miledi

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Abstract

Voltage activated currents were studied in whole-cell patch-clamped rat neocortical neurons growing in culture and treated with tunicamycin (TU), an inhibitor of protein N-glycosylation. The size of the Na + current decreased progressively in the presence of TU (1-2 μM). This decrease was faster in growing 5-14 day-old neurons (to ca. 40% of control after 24 hours of treatment) than in fully grown 20-40-day-old neurons (to ca. 40% of control after 68 hours of treatment). The fast transient K + current (A-current) was abolished, and the delayed rectifier K + current was markedly reduced by a 24 hour treatment with TU (1-2 μM) in growing neurons. In contrast, in fully grown neurons these currents were unaffected by the same TU treatment. The size of the Ca 2+ current was significantly reduced following a 24 hour treatment with TU (1-2 μM) in neurons at early stages of differentiation, but remained stable in 20-40-day-old neurons. It is concluded that protein glycosylation, presumably of the channel proteins themselves, is important for the functional expression of voltage-activated channels in embryonic cortical neurons during the early stages of cell growth in culture; the channels become less dependent on glycosylation in mature neurons.

Original languageEnglish
Pages (from-to)119-127
Number of pages9
JournalProceedings of the Royal Society B: Biological Sciences
Volume239
Issue number1295
Publication statusPublished - 1990

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Glycosylation
glycosylation
Neurons
Rats
neurons
tunicamycin
Maintenance
Tunicamycin
protein
rats
Electric potential
inhibitor
Proteins
proteins
Cell growth
Cell culture
cell growth

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Agricultural and Biological Sciences (miscellaneous)

Cite this

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title = "Glycosylation is required for maintenance of functional voltage-activated channels in growing neocortical neurons of the rat",
abstract = "Voltage activated currents were studied in whole-cell patch-clamped rat neocortical neurons growing in culture and treated with tunicamycin (TU), an inhibitor of protein N-glycosylation. The size of the Na + current decreased progressively in the presence of TU (1-2 μM). This decrease was faster in growing 5-14 day-old neurons (to ca. 40{\%} of control after 24 hours of treatment) than in fully grown 20-40-day-old neurons (to ca. 40{\%} of control after 68 hours of treatment). The fast transient K + current (A-current) was abolished, and the delayed rectifier K + current was markedly reduced by a 24 hour treatment with TU (1-2 μM) in growing neurons. In contrast, in fully grown neurons these currents were unaffected by the same TU treatment. The size of the Ca 2+ current was significantly reduced following a 24 hour treatment with TU (1-2 μM) in neurons at early stages of differentiation, but remained stable in 20-40-day-old neurons. It is concluded that protein glycosylation, presumably of the channel proteins themselves, is important for the functional expression of voltage-activated channels in embryonic cortical neurons during the early stages of cell growth in culture; the channels become less dependent on glycosylation in mature neurons.",
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AU - Zona, C.

AU - Eusebi, F.

AU - Miledi, R.

PY - 1990

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N2 - Voltage activated currents were studied in whole-cell patch-clamped rat neocortical neurons growing in culture and treated with tunicamycin (TU), an inhibitor of protein N-glycosylation. The size of the Na + current decreased progressively in the presence of TU (1-2 μM). This decrease was faster in growing 5-14 day-old neurons (to ca. 40% of control after 24 hours of treatment) than in fully grown 20-40-day-old neurons (to ca. 40% of control after 68 hours of treatment). The fast transient K + current (A-current) was abolished, and the delayed rectifier K + current was markedly reduced by a 24 hour treatment with TU (1-2 μM) in growing neurons. In contrast, in fully grown neurons these currents were unaffected by the same TU treatment. The size of the Ca 2+ current was significantly reduced following a 24 hour treatment with TU (1-2 μM) in neurons at early stages of differentiation, but remained stable in 20-40-day-old neurons. It is concluded that protein glycosylation, presumably of the channel proteins themselves, is important for the functional expression of voltage-activated channels in embryonic cortical neurons during the early stages of cell growth in culture; the channels become less dependent on glycosylation in mature neurons.

AB - Voltage activated currents were studied in whole-cell patch-clamped rat neocortical neurons growing in culture and treated with tunicamycin (TU), an inhibitor of protein N-glycosylation. The size of the Na + current decreased progressively in the presence of TU (1-2 μM). This decrease was faster in growing 5-14 day-old neurons (to ca. 40% of control after 24 hours of treatment) than in fully grown 20-40-day-old neurons (to ca. 40% of control after 68 hours of treatment). The fast transient K + current (A-current) was abolished, and the delayed rectifier K + current was markedly reduced by a 24 hour treatment with TU (1-2 μM) in growing neurons. In contrast, in fully grown neurons these currents were unaffected by the same TU treatment. The size of the Ca 2+ current was significantly reduced following a 24 hour treatment with TU (1-2 μM) in neurons at early stages of differentiation, but remained stable in 20-40-day-old neurons. It is concluded that protein glycosylation, presumably of the channel proteins themselves, is important for the functional expression of voltage-activated channels in embryonic cortical neurons during the early stages of cell growth in culture; the channels become less dependent on glycosylation in mature neurons.

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