Effects of some conformationally restricted GABA analogues on GABA membrane binding and nerve ending transport

Robert Hitzemann, Horace H. Loh

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

By using a series of aminocyclopentane- and aminocyclohexanecarboxylic acids, as well as some naturally occurring amino acids, it was possible to determine some aspects of the spatial topography of the GABA membrane binding and transport sites. The Na-independent GABA binding site was found to have a different spatial topography than the Na-dependent binding site in that trans-3-aminocyclopentanecarboxylic acid (trans-3-ACPC) was 7 times more potent than cis-3-ACPC to inhibit Na-independent binding, but only 1.6 times more potent to inhibit Na-dependent binding. The nerve ending GABA transport site was found to be cis- and trans-3-ACPC. However, the transport site differs from the binding site in that similar to the Na-dependent GABA binding site in that it will accommodate both cis-3-aminocyclohexanecarboxylic acid (cis-3-ACHC) is a potent inhibitor of transport but a weak inhibitor of binding. In addition to the differences in spatial characteristics, differences in the subcellular distribution of Na-independent and Na-dependent binding sites were observed. The former were found primarily in the nerve ending-mitochondrial fraction, while the latter were primarily found in the microsomal fraction.

Original languageEnglish (US)
Pages (from-to)63-73
Number of pages11
JournalBrain Research
Volume144
Issue number1
DOIs
StatePublished - Apr 7 1978
Externally publishedYes

Fingerprint

Nerve Endings
gamma-Aminobutyric Acid
Binding Sites
Membranes
Cycloleucine
Amino Acids
Acids

ASJC Scopus subject areas

  • Developmental Biology
  • Molecular Biology
  • Clinical Neurology
  • Neuroscience(all)

Cite this

Effects of some conformationally restricted GABA analogues on GABA membrane binding and nerve ending transport. / Hitzemann, Robert; Loh, Horace H.

In: Brain Research, Vol. 144, No. 1, 07.04.1978, p. 63-73.

Research output: Contribution to journalArticle

@article{f3cd3b5cf5214994a25d842183dd4168,
title = "Effects of some conformationally restricted GABA analogues on GABA membrane binding and nerve ending transport",
abstract = "By using a series of aminocyclopentane- and aminocyclohexanecarboxylic acids, as well as some naturally occurring amino acids, it was possible to determine some aspects of the spatial topography of the GABA membrane binding and transport sites. The Na-independent GABA binding site was found to have a different spatial topography than the Na-dependent binding site in that trans-3-aminocyclopentanecarboxylic acid (trans-3-ACPC) was 7 times more potent than cis-3-ACPC to inhibit Na-independent binding, but only 1.6 times more potent to inhibit Na-dependent binding. The nerve ending GABA transport site was found to be cis- and trans-3-ACPC. However, the transport site differs from the binding site in that similar to the Na-dependent GABA binding site in that it will accommodate both cis-3-aminocyclohexanecarboxylic acid (cis-3-ACHC) is a potent inhibitor of transport but a weak inhibitor of binding. In addition to the differences in spatial characteristics, differences in the subcellular distribution of Na-independent and Na-dependent binding sites were observed. The former were found primarily in the nerve ending-mitochondrial fraction, while the latter were primarily found in the microsomal fraction.",
author = "Robert Hitzemann and Loh, {Horace H.}",
year = "1978",
month = "4",
day = "7",
doi = "10.1016/0006-8993(78)90435-3",
language = "English (US)",
volume = "144",
pages = "63--73",
journal = "Brain Research",
issn = "0006-8993",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - Effects of some conformationally restricted GABA analogues on GABA membrane binding and nerve ending transport

AU - Hitzemann, Robert

AU - Loh, Horace H.

PY - 1978/4/7

Y1 - 1978/4/7

N2 - By using a series of aminocyclopentane- and aminocyclohexanecarboxylic acids, as well as some naturally occurring amino acids, it was possible to determine some aspects of the spatial topography of the GABA membrane binding and transport sites. The Na-independent GABA binding site was found to have a different spatial topography than the Na-dependent binding site in that trans-3-aminocyclopentanecarboxylic acid (trans-3-ACPC) was 7 times more potent than cis-3-ACPC to inhibit Na-independent binding, but only 1.6 times more potent to inhibit Na-dependent binding. The nerve ending GABA transport site was found to be cis- and trans-3-ACPC. However, the transport site differs from the binding site in that similar to the Na-dependent GABA binding site in that it will accommodate both cis-3-aminocyclohexanecarboxylic acid (cis-3-ACHC) is a potent inhibitor of transport but a weak inhibitor of binding. In addition to the differences in spatial characteristics, differences in the subcellular distribution of Na-independent and Na-dependent binding sites were observed. The former were found primarily in the nerve ending-mitochondrial fraction, while the latter were primarily found in the microsomal fraction.

AB - By using a series of aminocyclopentane- and aminocyclohexanecarboxylic acids, as well as some naturally occurring amino acids, it was possible to determine some aspects of the spatial topography of the GABA membrane binding and transport sites. The Na-independent GABA binding site was found to have a different spatial topography than the Na-dependent binding site in that trans-3-aminocyclopentanecarboxylic acid (trans-3-ACPC) was 7 times more potent than cis-3-ACPC to inhibit Na-independent binding, but only 1.6 times more potent to inhibit Na-dependent binding. The nerve ending GABA transport site was found to be cis- and trans-3-ACPC. However, the transport site differs from the binding site in that similar to the Na-dependent GABA binding site in that it will accommodate both cis-3-aminocyclohexanecarboxylic acid (cis-3-ACHC) is a potent inhibitor of transport but a weak inhibitor of binding. In addition to the differences in spatial characteristics, differences in the subcellular distribution of Na-independent and Na-dependent binding sites were observed. The former were found primarily in the nerve ending-mitochondrial fraction, while the latter were primarily found in the microsomal fraction.

UR - http://www.scopus.com/inward/record.url?scp=0017802708&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0017802708&partnerID=8YFLogxK

U2 - 10.1016/0006-8993(78)90435-3

DO - 10.1016/0006-8993(78)90435-3

M3 - Article

C2 - 205318

AN - SCOPUS:0017802708

VL - 144

SP - 63

EP - 73

JO - Brain Research

JF - Brain Research

SN - 0006-8993

IS - 1

ER -