Immunocytochemical localization of the renal neutral and basic amino acid transporter in rat adrenal gland, brainstem, and spinal cord

1995 ◽  
Vol 356 (4) ◽  
pp. 505-522 ◽  
Author(s):  
Melissa J. Nirenberg ◽  
Suresh S. Tate ◽  
Rachel Mosckovitz ◽  
Sidney Udenfriend ◽  
Virginia M. Pickel
Keyword(s):  
Spinal Cord ◽  
Amino Acid ◽  
Adrenal Gland ◽  
Basic Amino Acid ◽  
Amino Acid Transporter ◽  
Immunocytochemical Localization ◽  
Acid Transporter

scholarly journals Multiple components of arginine and phenylalanine transport induced in neutral and basic amino acid transporter-cRNA-injected Xenopus oocytes

1996 ◽  
Vol 318 (3) ◽  
pp. 915-922 ◽  
Author(s):  
George J PETER ◽  
Iain G. DAVIDSON ◽  
Aamir AHMED ◽  
Lynn McILROY ◽  
Alexander R. FORRESTER ◽  
...  
Keyword(s):  
Amino Acid ◽  
Xenopus Oocytes ◽  
Competitive Inhibition ◽  
Protein Complexes ◽  
Basic Amino Acid ◽  
Amino Acid Transporter ◽  
Transport Processes ◽  
Arginine Transport ◽  
Acid Transporter ◽  
Phenylalanine Transport

The induced uptakes of l-[3H]phenylalanine and l-[3H]arginine in oocytes injected with clonal NBAT (neutral and basic amino acid transporter) cRNA show differential inactivation by pre-treatment with N-ethylmaleimide (NEM), revealing at least two distinct transport processes. NEM-resistant arginine transport is inhibited by leucine and phenylalanine but not by alanine or valine; mutual competitive inhibition of NEM-resistant uptake of arginine and phenylalanine indicates that the two amino acids share a single transporter. NEM-senstive arginine transport is inhibited by leucine, phenylalanine, alanine and valine. At least two NEM-sensitive transporters may be expressed because we have been unable to confirm mutual competitive inhibition between arginine and phenylalanine transport. The NEM-resistant transport mechanism appears to involve distinct but overlapping binding sites for cationic and zwitterionic substrates. NBAT is known to form oligomeric protein complexes in cell membranes, and its functional roles when expressed in Xenopus oocytes may include interaction with oocyte proteins, leading to increased native amino acid transport activities; these resemble NBAT-expressed activities in terms of NEM-sensitivity and apparent substrate range (including an unusual inhibition by β-phenylalanine).

Presence of the vesicular inhibitory amino acid transporter in GABAergic and glycinergic synaptic terminal boutons

1999 ◽  
Vol 112 (6) ◽  
pp. 811-823
Author(s):  
A. Dumoulin ◽  
P. Rostaing ◽  
C. Bedet ◽  
S. Levi ◽  
M.F. Isambert ◽  
...  
Keyword(s):  
Spinal Cord ◽  
Amino Acid ◽  
Synaptic Vesicle ◽  
Glycine Receptor ◽  
Primary Cultures ◽  
Ultrastructural Level ◽  
Amino Acid Transporter ◽  
Vesicle Membrane ◽  
Hybridization Data ◽  
Acid Transporter

The characterization of the Caenorhabditis elegans unc-47 gene recently allowed the identification of a mammalian (gamma)-amino butyric acid (GABA) transporter, presumed to be located in the synaptic vesicle membrane. In situ hybridization data in rat brain suggested that it might also take up glycine and thus represent a general Vesicular Inhibitory Amino Acid Transporter (VIAAT). In the present study, we have investigated the localization of VIAAT in neurons by using a polyclonal antibody raised against the hydrophilic N-terminal domain of the protein. Light microscopy and immunocytochemistry in primary cultures or tissue sections of the rat spinal cord revealed that VIAAT was localized in a subset (63-65%) of synaptophysin-immunoreactive terminal boutons; among the VIAAT-positive terminals around motoneuronal somata, 32.9% of them were also immunoreactive for GAD65, a marker of GABAergic presynaptic endings. Labelling was also found apposed to clusters positive for the glycine receptor or for its associated protein gephyrin. At the ultrastructural level, VIAAT immunoreactivity was restricted to presynaptic boutons exhibiting classical inhibitory features and, within the boutons, concentrated over synaptic vesicle clusters. Pre-embedding detection of VIAAT followed by post-embedding detection of GABA or glycine on serial sections of the spinal cord or cerebellar cortex indicated that VIAAT was present in glycine-, GABA- or GABA- and glycine-containing boutons. Taken together, these data further support the view of a common vesicular transporter for these two inhibitory transmitters, which would be responsible for their costorage in the same synaptic vesicle and subsequent corelease at mixed GABA-and-glycine synapses.

scholarly journals Characterization of the rat neutral and basic amino acid transporter utilizing anti-peptide antibodies.

1993 ◽  
Vol 90 (9) ◽  
pp. 4022-4026 ◽  
Author(s):  
R. Mosckovitz ◽  
N. Yan ◽  
E. Heimer ◽  
A. Felix ◽  
S. S. Tate ◽  
...  
Keyword(s):  
Amino Acid ◽  
Basic Amino Acid ◽  
Amino Acid Transporter ◽  
Acid Transporter ◽  
Peptide Antibodies

Cell-surface receptor for ecotropic murine retroviruses is a basic amino-acid transporter

Nature ◽  
1991 ◽  
Vol 352 (6337) ◽  
pp. 729-731 ◽  
Author(s):  
Hao Wang ◽  
Michael P. Kavanaugh ◽  
R. Alan North ◽  
David Kabat
Keyword(s):  
Amino Acid ◽  
Cell Surface ◽  
Basic Amino Acid ◽  
Amino Acid Transporter ◽  
Cell Surface Receptor ◽  
Surface Receptor ◽  
Acid Transporter

scholarly journals Ultrastructural localization of a neutral and basic amino acid transporter in rat kidney and intestine.

1993 ◽  
Vol 90 (16) ◽  
pp. 7779-7783 ◽  
Author(s):  
V. M. Pickel ◽  
M. J. Nirenberg ◽  
J. Chan ◽  
R. Mosckovitz ◽  
S. Udenfriend ◽  
...  
Keyword(s):  
Amino Acid ◽  
Rat Kidney ◽  
Basic Amino Acid ◽  
Ultrastructural Localization ◽  
Amino Acid Transporter ◽  
Acid Transporter

scholarly journals Cloning, functional expression and dietary regulation of the mouse neutral and basic amino acid transporter (NBAT)

1997 ◽  
Vol 328 (2) ◽  
pp. 657-664 ◽  
Author(s):  
Hiroko SEGAWA ◽  
Ken-ichi MIYAMOTO ◽  
Yoshio OGURA ◽  
Hiromi HAGA ◽  
Kyoko MORITA ◽  
...  
Keyword(s):  
Amino Acid ◽  
Xenopus Oocytes ◽  
Physiological Role ◽  
Basic Amino Acid ◽  
Functional Expression ◽  
Amino Acid Transporter ◽  
Amino Acid Transporters ◽  
Transport Activity ◽  
Acid Transporter ◽  
Mouse Ileum

The Na+-independent dibasic and neutral amino acid transporter NBAT is among the least hydrophobic of mammalian amino acid transporters. The transporter contains one to four transmembrane domains and induces amino acid transport activity via a b0,+-like system when expressed in Xenopus oocytes. However, the physiological role of NBAT remains unclear. Complementary DNA clones encoding mouse NBAT have now been isolated. The expression of mouse NBAT in Xenopus oocytes also induced an obligatory amino acid exchange activity similar to that of the b0,+-like system. The amount of NBAT mRNA in mouse kidney increased during postnatal development, consistent with the increase in renal cystine and dibasic transport activity. Dietary aspartate induced a marked increase in cystine transport via the b0,+ system in mouse ileum. A high-aspartate diet also increased the amount of NBAT mRNA in mouse ileum. In the ileum of mice fed on the aspartate diet, the extent of cystine transport was further increased by preloading brush border membrane vesicles with lysine. Hybrid depletion of NBAT mRNA from ileal polyadenylated RNA revealed that the increase in cystine transport activity induced by the high-aspartate diet, as measured in Xenopus oocytes, was attributable to NBAT. These results demonstrate that mouse NBAT has an important role in cystine transport.

scholarly journals Transport Properties of a System y+L Neutral and Basic Amino Acid Transporter

2000 ◽  
Vol 275 (27) ◽  
pp. 20787-20793 ◽  
Author(s):  
Yoshikatsu Kanai ◽  
Yoshiki Fukasawa ◽  
Seok Ho Cha ◽  
Hiroko Segawa ◽  
Arthit Chairoungdua ◽  
...  
Keyword(s):  
Amino Acid ◽  
Transport Properties ◽  
Basic Amino Acid ◽  
Amino Acid Transporter ◽  
Acid Transporter
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