scholarly journals Carrier-mediated gamma-aminobutyric acid uptake in human spermatozoa indicating the presence of a high-affinity gamma-aminobutyric acid transport protein

1996 ◽  
Vol 54 (4) ◽  
pp. 841-846 ◽  
Author(s):  
A. Aanesen
Keyword(s):  
Transport Protein ◽  
Human Spermatozoa ◽  
Aminobutyric Acid ◽  
Acid Uptake ◽  
Gamma Aminobutyric Acid ◽  
Acid Transport ◽  
High Affinity

scholarly journals Inhibition of high-affinity gamma-aminobutyric acid uptake in primary astrocyte cultures by phorbol esters and phospholipase C

1991 ◽  
Vol 275 (2) ◽  
pp. 435-439 ◽  
Author(s):  
J Gomeza ◽  
M Casado ◽  
C Gimenez ◽  
C Aragon
Keyword(s):  
Phospholipase C ◽  
Glial Cells ◽  
Kinase Inhibitor ◽  
Primary Cultures ◽  
Aminobutyric Acid ◽  
Gaba Uptake ◽  
Acid Uptake ◽  
Gamma Aminobutyric Acid ◽  
Gaba Transport ◽  
High Affinity

The effects of phorbol 12-myristate 13-acetate (PMA), a potent activator of protein kinase C (PKC), on high-affinity Na(+)-dependent gamma-aminobutyric acid (GABA) uptake were investigated in primary cultures of neurons and glial cells from rat brain cortex. Incubation of glial cells with PMA led to concentration- and time-dependent decreases in the GABA transport in glial cells. This effect could be completely suppressed by addition of the PKC inhibitor H7. The PMA effects could be mimicked by oleoylacetylglycerol, the diacylglycerol kinase inhibitor R59022 and exogenous phospholipase C. Treatment with PMA did not affect GABA transport in neuronal cells.

scholarly journals Functional Characterization of the γ-Aminobutyric Acid Transporter from Mycobacterium smegmatis MC2 155 Reveals Sodium-Driven GABA Transport

2020 ◽  
Author(s):  
Ana Pavić ◽  
Yurui Ji ◽  
Agnese Serafini ◽  
Acely Garza-Garcia ◽  
Martin J. McPhillie ◽  
...  
Keyword(s):  
Mycobacterium Smegmatis ◽  
Drug Targets ◽  
Functional Characterization ◽  
Transport Protein ◽  
New Drugs ◽  
Size Exclusion ◽  
Aminobutyric Acid ◽  
Acid Uptake ◽  
Acid Transport

Characterizing the mycobacterial transporters involved in the uptake and/or catabolism of host-derived nutrients required by mycobacteria may identify novel drug targets against tuberculosis. Here, we identify and characterize a member of the amino acid-polyamine- organocation superfamily, a potential γ-aminobutyric acid transport protein, GabP, from Mycobacterium smegmatis. The protein was expressed to a level allowing its purification to homogeneity and Size Exclusion Chromatography-Multi Angle Laser Light Scattering analysis of the purified protein showed that it was dimeric. We showed that GabP transported γ-aminobutyric acid in vitro and when over-expressed in E. coli. Additionally, transport was greatly reduced in the presence of β-alanine, suggesting that it could be either substrate or inhibitor of GabP. Using GabP reconstituted into proteoliposomes, we demonstrated that γ-aminobutyric acid uptake is driven by the sodium gradient and is stimulated by membrane potential. Molecular docking showed that γ-aminobutyric acid binds MsGabP, another Mycobacterium smegmatis putative GabP and the Mycobacterium tuberculosis homologue in the same manner. This study represents the first expression, purification and characterization of an active γ-aminobutyric acid transport protein from mycobacteria. IMPORTANCE The spread of multidrug resistant tuberculosis increases its global health impact in humans. As there is transmission both to and from animals, the spread of the disease also increases its effects in a broad range of animal species. Identifying new mycobacterial transporters will enhance our understanding of mycobacterial physiology and furthermore provides new drug targets. Our target protein is the gene product of msmeg_6196, annotated as GABA permease, from Mycobacterium smegmatis strain MC2 155. Our current study demonstrates that it is a sodium-dependent GABA transporter that may also transport β-alanine. As GABA may well be an essential nutrient for mycobacterial metabolism inside the host, this could be an attractive target for the development of new drugs against tuberculosis.

scholarly journals Concurrent acetylcholinesterase staining and gamma-aminobutyric acid uptake of cortical neurons in culture.

1981 ◽  
Vol 29 (2) ◽  
pp. 306-308 ◽  
Author(s):  
M M Mesulam ◽  
M Dichter
Keyword(s):  
Tissue Culture ◽  
Cortical Neurons ◽  
Gabaergic Neurons ◽  
Aminobutyric Acid ◽  
Gaba Uptake ◽  
Acid Uptake ◽  
Gamma Aminobutyric Acid ◽  
Acetylcholinesterase Staining ◽  
Culture Positive

Gamma-aminobutyric acid (GABA) uptake and acetylcholinesterase (AChE) content were demonstrated concurrently in cortical neurons grown in tissue culture. Positive reactions either for GABA uptake or for AChE content were encountered in pyramidal and stellate, as well as spindle-shaped neurons. Neither reaction was confined to a specific morphological subtype. Nearly half the neurons were negative for either reaction. Most of the remaining neurons were positive only for GABA or only for AChE. However, a subpopulation of neurons showed not only a high AChE content, but also an avid GABA uptake. Thus, four types of neurons could be identified on the basis of these two reactions. The high AChE content in some of the cortical neurons that also showed GABA uptake indicates that there are at least two distinct types of GABAergic neurons.

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