Literature DB >> 12566983

Membrane glycine transport proteins.

Godfrey Tunnicliff1.   

Abstract

Structurally, the simplest amino acid is glycine, and it has a number of important yet distinct functions in the body. This review focuses on the different transport systems and the associated carrier proteins for glycine that are responsible for its movement across biological membranes. Transport proteins in the class GLYT appear to be the most specific for glycine. However, the B0+ system also carries significant amounts of glycine. Other amino acid transport systems capable of carrying small amounts of glycine are ASC, asc and system L. In addition, an ATP-dependent transport process exists that takes up glycine into synaptic vesicles at nerve endings. This is known as the vesicular inhibitory amino acid transporter since, in addition to glycine, it can transport possibly two other inhibitory neurotransmitters. Copyright 2003 National Science Council, ROC and S. Karger AG, Basel

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Year:  2003        PMID: 12566983     DOI: 10.1007/BF02255994

Source DB:  PubMed          Journal:  J Biomed Sci        ISSN: 1021-7770            Impact factor:   8.410


  4 in total

1.  Glutathione synthesis and turnover in the human erythrocyte: alignment of a model based on detailed enzyme kinetics with experimental data.

Authors:  Julia E Raftos; Stephney Whillier; Philip W Kuchel
Journal:  J Biol Chem       Date:  2010-05-24       Impact factor: 5.157

2.  A novel physiological mechanism of glycine-induced immunomodulation: Na+-coupled amino acid transporter currents in cultured brain macrophages.

Authors:  Tom Schilling; Claudia Eder
Journal:  J Physiol       Date:  2004-07-08       Impact factor: 5.182

3.  Mutations in the gene encoding GlyT2 (SLC6A5) define a presynaptic component of human startle disease.

Authors:  Mark I Rees; Kirsten Harvey; Brian R Pearce; Seo-Kyung Chung; Ian C Duguid; Philip Thomas; Sarah Beatty; Gail E Graham; Linlea Armstrong; Rita Shiang; Kim J Abbott; Sameer M Zuberi; John B P Stephenson; Michael J Owen; Marina A J Tijssen; Arn M J M van den Maagdenberg; Trevor G Smart; Stéphane Supplisson; Robert J Harvey
Journal:  Nat Genet       Date:  2006-06-04       Impact factor: 38.330

4.  Extracellular glycine is necessary for optimal hemoglobinization of erythroid cells.

Authors:  Daniel Garcia-Santos; Matthias Schranzhofer; Richard Bergeron; Alex D Sheftel; Prem Ponka
Journal:  Haematologica       Date:  2017-05-11       Impact factor: 9.941

  4 in total

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