The effect of enzymatic treatment using proteases on properties of persistent sodium current in CA1 pyramidal neurons of rat hippocampus

We investigated the effect of proteases, widely used for neuron isolation in electrophysiological studies, on the amplitude and kinetic characteristics of persistent sodium current (I(NaP)) in hippocampal CA1 pyramidal neurons. Properties of I(NaP) were studied on neurons isolated by mechanical trea...

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Bibliographic Details
Published in:	Fiziolohichnyi zhurnal (Kiev, Ukraine : 1994) Vol. 60; no. 3; p. 75
Main Authors:	Lun'ko, O O, Isaiev, D S, Maxymiuk, O P, Kryshtal', O O, Isaieva, O V
Format:	Journal Article
Language:	English Ukrainian
Published:	Ukraine 2014
Subjects:	Animals Bacterial Proteins - pharmacology CA1 Region, Hippocampal - cytology CA1 Region, Hippocampal - drug effects CA1 Region, Hippocampal - metabolism Cell Separation - methods Fungal Proteins - pharmacology Ion Transport Membrane Potentials - drug effects Membrane Potentials - physiology Neurons - cytology Neurons - drug effects Neurons - metabolism Patch-Clamp Techniques Peptide Hydrolases - pharmacology Primary Cell Culture Pronase - metabolism Pronase - pharmacology Proteolysis Rats Sodium - metabolism Sodium Channels - metabolism
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Summary:	We investigated the effect of proteases, widely used for neuron isolation in electrophysiological studies, on the amplitude and kinetic characteristics of persistent sodium current (I(NaP)) in hippocampal CA1 pyramidal neurons. Properties of I(NaP) were studied on neurons isolated by mechanical treatment (control group) and by mechanical and enzymatic treatment using pronase E (from Streptomyces griseus) or protease type XXIII (from Aspergillus oryzae). We show that in neurons isolated with pronase E kinetic of activation and density of I(NaP) was unaltered. Enzymatic treatment with protease type XXIII did not alter I(NaP) activation but result in significant decrease in I(NaP) density. Our data indicates that enzymatic treatment using pronase E for neuron isolation is preferable for investigation of I(NaP).
ISSN:	2522-9028
DOI:	10.15407/fz60.03.075