## Abstract In this study, we examined the transport mechanisms for guanine and guanosine in rat neurons and astrocytes, and compared their characteristics. In the both types of cell, the uptake of [^3^H]guanine and [^3^H]guanosine was timeβ, temperatureβ, and concentrationβdependent, and Na^+^βind
Characterization of L-DOPA transport in cultured rat and mouse astrocytes
β Scribed by M.J. Tsai; E.H.Y. Lee
- Publisher
- John Wiley and Sons
- Year
- 1996
- Tongue
- English
- Weight
- 583 KB
- Volume
- 43
- Category
- Article
- ISSN
- 0360-4012
No coin nor oath required. For personal study only.
β¦ Synopsis
The present work studied the transport of L-DOPA in cultured rat and mouse astrocytes. Results indicated that the uptake of L-[14C]DOPA in both rat and mouse astrocytes was Na+ independent and temperature sensitive. It was mediated by a carrier-mediated mechanism with K, values of 36 and 60.3 pM, and V,,, values of 2.4 and 1.9 nmollminlmg protein for rat and mouse cells, respectively. L-DOPA uptake was potently inhibited by aromatic or branched-chain amino acids. Interestingly, the release of intracellular L-[ 14C]DOPA was also trans stimulated by competitors that affect L-DOPA uptake. The 14C recovered in the 2-min uptake process was identified as L-[14C]DOPA. However, [14C]dopamine (DA) was also detected in both rat and mouse astrocytes after 30 min L-DOPA incubation, indicating the existence of aromatic L-amino acid decarboxylase (AADC). Taken together, L-DOPA was uphill transported into rat and mouse astrocytes by a Na + -independent exchanger with preference for aromatic and branchedchain amino acids. Rat astrocytes possessed higher affinity for L-DOPA uptake than mouse astrocytes. Both cells synthesized DA from exogenous L-DOPA. Thus, astrocytes serve not only as a temporary storage site for L-DOPA but also as a DA-producing machinery. These results may be of particular importance to parkinsonian patients under L-DOPA medication.
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