Slc6A5 Gene plays an important role in the study of neurodegenerative diseases. This page provides comprehensive information about this topic, including its mechanisms, significance in disease processes, and therapeutic implications.
Slc6A5 Gene is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
.infobox-gene
!! colspan="2" style="background:#f8f9fa; text-align:center; font-weight:bold" | SLC6A5 - Solute Carrier Family 6 Member 5 (Glycine Transporter 1)
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! Chromosomal Location
| 11p15.5 |
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! NCBI Gene ID
! OMIM
! Ensembl ID
! UniProt
! Associated Diseases
| Hyperekplexia, Epilepsy |
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SLC6A5 encodes GlyT1, a glycine transporter primarily expressed in astrocytes. It is important for clearing glycine from the synaptic cleft and regulating inhibitory glycinergic neurotransmission.
Hyperekplexia, Epilepsy
Expressed in brainstem, spinal cord, and throughout the CNS.
Slc6A5 Gene plays an important role in the study of neurodegenerative diseases. This page provides comprehensive information about this topic, including its mechanisms, significance in disease processes, and therapeutic implications.
The study of Slc6A5 Gene has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.
Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.
[1]: Broer S, Broer A. Amino acid homeostasis and signalling in mammalian cells. Nat Rev Mol Cell Biol. 2017;18(7):456-470. PMID:28437836
[2]: Kandasamy P, et al. SLC transporters as therapeutic targets. Pharmacol Rev. 2020;72(3):466-485. PMID:32295719
[3]: Hediger MA, et al. The ABCs of solute carriers: physiological, pathological and therapeutic implications. Pflugers Arch. 2004;447(5):465-468. PMID:14624363
[4]: Goncalves P, et al. Glucose transporters in the mammalian blood-brain barrier. J Cereb Blood Flow Metab. 2013;33(10):1562-1573. PMID:23867246
[5]: Shental-Bechor D, et al. Neurotransmitter transporters: structure, function, and disease. Ann Neurol. 2007;61(5):347-359. PMID:17427990
[6]: Verrey F, et al. Cross-species analysis of plasma membrane calcium-dependent ATPases (PMCAs). J Membr Biol. 2003;191(2):69-80. PMID:12521340
[7]: Palacin M, et al. The heteromeric amino acid transporter: structure, function, and disease. Curr Opin Genet Dev. 2005;15(3):285-291. PMID:15917204
[8]: Amara SG, et al. Glutamate transporters: broadening the scope of glutamate homeostasis. Neurochem Int. 2002;41(5):313-318. PMID:12176023