scholarly journals D-Serine metabolism in C6 glioma cells: Involvement of alanine-serine-cysteine transporter (ASCT2) and serine racemase (SRR) but not D-amino acid oxidase (DAO)

2010 ◽  
Vol 88 (8) ◽  
pp. 1829-1840 ◽  
Author(s):  
Pilleriin Sikka ◽  
Rosie Walker ◽  
Rebecca Cockayne ◽  
Matthew J.A. Wood ◽  
Paul J. Harrison ◽  
...  
Keyword(s):  
Amino Acid ◽  
Glioma Cells ◽  
C6 Glioma ◽  
Serine Racemase ◽  
C6 Glioma Cells ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Serine Metabolism

D-Serine metabolism: new insights into the modulation of D-amino acid oxidase activity

2013 ◽  
Vol 41 (6) ◽  
pp. 1551-1556 ◽  
Author(s):  
Silvia Sacchi
Keyword(s):  
Enzyme Activity ◽  
Amino Acid ◽  
Oxidase Activity ◽  
Acid Oxidase ◽  
Endogenous Ligand ◽  
Amino Acid Oxidase ◽  
The Brain ◽  
Serine Metabolism ◽  
Synthesis And Degradation

Over the years, accumulating evidence has indicated that D-serine represents the main endogenous ligand of NMDA (N-methyl-D-aspartate) receptors. In the brain, the concentration of D-serine stored in cells is defined by the activity of two enzymes: serine racemase (responsible for both the synthesis and degradation) and D-amino acid oxidase (which catalyses D-serine degradation). The present review is focused on human D-amino acid oxidase, discussing the mechanisms involved in modulating enzyme activity and stability, with the aim to substantiate the pivotal role of D-amino acid oxidase in brain D-serine metabolism.

scholarly journals Factors regulating serine racemase and d-amino acid oxidase expression in the mouse striatum

2021 ◽  
Vol 1751 ◽  
pp. 147202
Author(s):  
Shunsuke Takagi ◽  
Darrick T. Balu ◽  
Joseph T. Coyle
Keyword(s):  
Amino Acid ◽  
Serine Racemase ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Mouse Striatum

scholarly journals d-Amino acid oxidase and serine racemase in human brain: normal distribution and altered expression in schizophrenia

2007 ◽  
Vol 26 (6) ◽  
pp. 1657-1669 ◽  
Author(s):  
Louise Verrall ◽  
Mary Walker ◽  
Nancy Rawlings ◽  
Isabel Benzel ◽  
James N. C. Kew ◽  
...  
Keyword(s):  
Amino Acid ◽  
Human Brain ◽  
Normal Distribution ◽  
Serine Racemase ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Altered Expression

Volume changes and whole cell membrane currents activated during gradual osmolarity decrease in C6 glioma cells: contribution of two types of K+ channels

2004 ◽  
Vol 286 (6) ◽  
pp. C1399-C1409 ◽  
Author(s):  
B. Ordaz ◽  
L. Vaca ◽  
R. Franco ◽  
H. Pasantes-Morales
Keyword(s):  
Amino Acid ◽  
Glioma Cells ◽  
Ionic Currents ◽  
C6 Glioma ◽  
C6 Glioma Cells ◽  
Channel Blockers ◽  
Volume Changes ◽  
Whole Cell ◽  
Outward Currents ◽  
Amino Acid Efflux

Volume changes and whole cell ionic currents activated by gradual osmolarity reductions (GOR) of 1.8 mosM/min were characterized in C6 glioma cells. Cells swell less in GOR than after sudden osmolarity reductions (SOR), the extent of swelling being partly Ca2+ dependent. In nominally Ca2+-free conditions, GOR activated predominantly whole cell outward currents. Cells depolarized from the initial −79 mV to a steady state of −54 mV reached at 18% osmolarity reduction [hyposmolarity of −18% (H-18%)]. Recordings of Cl− and K+ currents showed activation at H-3% of an outwardly rectifying Cl− current, with conductance of 1.6 nS, sensitive to niflumic acid and 5-nitro-2-(3-phenylpropylamino)benzoic acid, followed at H-18% by an outwardly rectifying K+ current with conductance of 4.1 nS, inhibited by clofilium but insensitive to the typical K+ channel blockers. With 200 nM Ca2+ in the patch pipette, whole cell currents activated at H-3% and at H-13% cells depolarized from −77 to −63 mV. A K+ current activated at H-1%, showing a rapid increase in conductance, suppressed by charybdotoxin and insensitive to clofilium. These results show the operation of two different K+ channels in response to GOR in the same cell type, activated by Ca2+ and osmolarity and with different osmolarity activation thresholds. Taurine and glutamate efflux, monitored by labeled tracers, showed delayed osmolarity thresholds of H-39 and H-33%, respectively. This observation clearly separates the Cl− and amino acid osmosensitive pathways. The delayed amino acid efflux may contribute to counteract swelling at more stringent osmolarity reductions.

scholarly journals Characterization of a thioredoxin-related surface protein

1994 ◽  
Vol 304 (3) ◽  
pp. 861-867 ◽  
Author(s):  
M F Dean ◽  
H Martin ◽  
P A Sansom
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Glioma Cells ◽  
Surface Protein ◽  
C6 Glioma ◽  
C6 Glioma Cells ◽  
Terminal Amino Acid ◽  
Terminal Amino ◽  
Terminal Amino Acid Sequence ◽  
Rat C6 Glioma

A surface-associated sulphydryl (thiol) protein (SASP) constitutively present in most nucleated cells was purified from human THP-1 monocytes and rat C6 glioma cells. The human protein was similar in mass and isoelectric point and had the same N-terminal amino acid sequence to adult T-cell leukemia-derived factor (ADF), a growth factor secreted by human lymphoid cells which is able to induce increased expression of interleukin-2 receptors. A further internal amino acid sequence, determined following cleavage of human SASP with cyanogen bromide, was also identical to the corresponding sequence deduced for ADF. Samples of SASP were able to reductively depolymerize human immunoglobulin, a property shared with thioredoxin, a ubiquitous protein, almost identical to ADF, with an essential function in many thiol-dependent reducing reactions. Furthermore, SASP purified from rat C6 glioma cells had an identical N-terminal amino acid sequence to that deduced for rat liver thioredoxin, showing that they were both members of the same family of proteins. The use of membrane-impermeable thiol reagents indicated that SASP was predominantly a cell-surface protein, and was not normally secreted. This SASP protein appeared to be a surface-associated form of thioredoxin that was constitutively present in a wide range of cells and was related to ADF, a secreted form of the same protein.

Ketamine enhances the expression of serine racemase and d-amino acid oxidase mRNAs in rat brain

2006 ◽  
Vol 540 (1-3) ◽  
pp. 82-86 ◽  
Author(s):  
Kazuhide Takeyama ◽  
Masanobu Yoshikawa ◽  
Tetsuo Oka ◽  
Mitsuru Kawaguchi ◽  
Toshiyasu Suzuki ◽  
...  
Keyword(s):  
Amino Acid ◽  
Rat Brain ◽  
Serine Racemase ◽  
Acid Oxidase ◽  
Amino Acid Oxidase

Potential Role for Astroglial d-Amino Acid Oxidase in Extracellular d-Serine Metabolism and Cytotoxicity

2006 ◽  
Vol 139 (2) ◽  
pp. 295-304 ◽  
Author(s):  
Hwan Ki Park ◽  
Yuji Shishido ◽  
Sayaka Ichise-Shishido ◽  
Tomoya Kawazoe ◽  
Koji Ono ◽  
...  
Keyword(s):  
Amino Acid ◽  
Potential Role ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Serine Metabolism

scholarly journals The Postnatal Development ofd-Serine in the Retinas of Two Mouse Strains, Including a Mutant Mouse with a Deficiency ind-Amino Acid Oxidase and a Serine Racemase Knockout Mouse

2014 ◽  
Vol 5 (9) ◽  
pp. 848-854 ◽  
Author(s):  
Gabriel E. Romero ◽  
Amber D. Lockridge ◽  
Catherine W. Morgans ◽  
Dipankar Bandyopadhyay ◽  
Robert F. Miller
Keyword(s):  
Amino Acid ◽  
Postnatal Development ◽  
Knockout Mouse ◽  
Mutant Mouse ◽  
Serine Racemase ◽  
Mouse Strains ◽  
Acid Oxidase ◽  
Amino Acid Oxidase

Effects of MK-801 on the expression of serine racemase and d-amino acid oxidase mRNAs and on the d-serine levels in rat brain

2007 ◽  
Vol 555 (1) ◽  
pp. 17-22 ◽  
Author(s):  
Atsushi Hashimoto ◽  
Masanobu Yoshikawa ◽  
Hidehiro Andoh ◽  
Hiroshi Yano ◽  
Hideo Matsumoto ◽  
...  
Keyword(s):  
Amino Acid ◽  
Rat Brain ◽  
Serine Racemase ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Mk 801
Sign in / Sign up

Export Citation Format

Share Document