RGD Reference Report - Transport characteristics of N-acetyl-L-aspartate in rat astrocytes: involvement of sodium-coupled high-affinity carboxylate transporter NaC3/NaDC3-mediated transport system. - Rat Genome Database

Send us a Message



Submit Data |  Help |  Video Tutorials |  News |  Publications |  Download |  REST API |  Citing RGD |  Contact   

Transport characteristics of N-acetyl-L-aspartate in rat astrocytes: involvement of sodium-coupled high-affinity carboxylate transporter NaC3/NaDC3-mediated transport system.

Authors: Fujita, T  Katsukawa, H  Yodoya, E  Wada, M  Shimada, A  Okada, N  Yamamoto, A  Ganapathy, V 
Citation: Fujita T, etal., J Neurochem. 2005 May;93(3):706-14.
RGD ID: 2303956
Pubmed: (View Article at PubMed) PMID:15836629
DOI: Full-text: DOI:10.1111/j.1471-4159.2005.03067.x

We investigated in the present study the transport characteristics of N-acetyl-L-aspartate in primary cultures of astrocytes from rat cerebral cortex and the involvement of NA+-coupled high-affinity carboxylate transporter NaC3 (formerly known as NaDC3) responsible for N-acetyl-L-aspartate transport. N-acetyl-L-aspartate transport was NA+-dependent and saturable with a Michaelis-Menten constant (Km) of approximately 110 microm. NA+-activation kinetics revealed that the NA+ to-N-acetyl-L-aspartate stoichiometry was 3 : 1 and concentration of Na+ necessary for half-maximal transport (KNA m) was 70 mm. NA+-dependent N-acetyl-L-aspartate transport was competitively inhibited by succinate with an inhibitory constant (Ki) of 14.7 microm, which was comparable to the Km value of NA+-dependent succinate transport (29.4 microm). L-aspartate also inhibited NA+-dependent [14C]N-acetyl-L-aspartate transport with relatively low affinity (Ki = 2.2 mm), whereas N-acetyl-L-aspartate was not able to inhibit NA+-dependent aspartate transport in astrocytes. In addition, Li+ was found to have a significant inhibitory effect on the NA+-dependent N-acetyl-L-aspartate transport in a concentration-dependent manner. Furthermore, RT-PCR and western blot analyses revealed that NaC3 is expressed in primary cultures of astrocytes. Taken collectively, these results indicate that NaC3 expressed in rat cerebrocortical astrocytes is responsible for NA+-dependent N-acetyl-L-aspartate transport. This transporter is likely to be an essential prerequisite for the metabolic role of N-acetyl-L-aspartate in the process of myelination.

Annotation

Gene Ontology Annotations    

Biological Process

Cellular Component
membrane  (IDA)

Molecular Function

Objects Annotated

Genes (Rattus norvegicus)
Slc13a3  (solute carrier family 13 member 3)


Additional Information