title: Proteolytic enzymes do not destroy the N-methyl-D-aspartate (NMDA) sensitivity of acutely isolated hippocampal CA1 and CA3 neurons from postnatal rats.
abstract: Using whole cell recordings in combination with the concentration clamp technique it was shown that even enzymatically isolated hippocampal CA1 and CA3 neurons exhibit N-methyl-D-aspartate (NMDA) and L-aspartate currents. These currents were completely blocked by 0.5 mM Mg2+ or partially blocked (72.7 +/- 2.4%) by DL-2-amino-5-phosphonovalerate (50 microM) whereas 10 microM glycine (Gly) potentiated the NMDA responses (3.1 +/- 1.6-fold). A half-maximum dose of 55 microM was calculated from the sigmoid NMDA dose-response curve in the presence of 10 microM Gly. The amplitudes of these currents did not depend on the type of the proteolytic enzyme used for cell isolation.
authors.affiliation: Institute for Neurobiology and Brain Research, Academy of Sciences GDR, Magdeburg.
authors.forename: J
authors.initials: J
authors.lastname: Gündel
authors.forename: C
authors.initials: C
authors.lastname: Steinhäuser
authors.forename: H
authors.initials: H
authors.lastname: Matthies
mesh_terms: D015763:2-Amino-5-phosphonovalerate / Q000494:pharmacology; D000818:Animals; D000831:Animals, Newborn; D001224:Aspartic Acid; D002469:Cell Separation; D004305:Dose-Response Relationship, Drug; D004357:Drug Synergism; D004553:Electric Conductivity; D005998:Glycine / Q000494:pharmacology; D006624:Hippocampus / Q000166:cytology / Q000187:drug effects* / Q000378:metabolism; D007473:Ion Channels / Q000187:drug effects / Q000378:metabolism / Q000502:physiology; D008274:Magnesium / Q000494:pharmacology; D016202:N-Methylaspartate / Q000494:pharmacology*; D009474:Neurons / Q000187:drug effects* / Q000378:metabolism; D010447:Peptide Hydrolases / Q000494:pharmacology*; D051381:Rats
chemical_list: D007473:Ion Channels; D001224:Aspartic Acid; D016202:N-Methylaspartate; D015763:2-Amino-5-phosphonovalerate; D010447:Peptide Hydrolases; D008274:Magnesium; D005998:Glycine