Characterization of rapid and high-affinity uptake of L-serine in neurons and astrocytes in primary culture
The non-essential amino acid L-serine was shown to be required to support the survival of rat cerebellar Purkinje neurons because of lack of the expression of the L-serine biosynthesis enzyme 3-phosphoglycerate dehydrogenase in them. In the present study, we investigated L-[3H]serine uptake in prima...
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Published in | FEBS letters Vol. 548; no. 1-3; pp. 69 - 73 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
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England
Elsevier B.V
31.07.2003
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Abstract | The non-essential amino acid L-serine was shown to be required to support the survival of rat cerebellar Purkinje neurons because of lack of the expression of the L-serine biosynthesis enzyme 3-phosphoglycerate dehydrogenase in them. In the present study, we investigated L-[3H]serine uptake in primary cultures of neurons and astrocytes from the rat telencephalon. In both neurons and astrocytes, L-[3H]serine uptake was dependent on temperature and Na+ ions, and exhibited a single component of high-affinity uptake sites (Km=15.0 and 17.2 μM for neurons and astrocytes, respectively). Kinetic analysis of L-[3H]serine uptake also revealed that the uptake into neurons was faster than that into astrocytes. The selectivity of inhibition by amino acids of the L-[3H]serine uptake resembled that of the system ASC transporters ASCT1 and ASCT2. Neutral amino acids L-alanine, L-serine, L-cysteine, and L-threonine strongly inhibited the uptake by both cell types. Furthermore, in astrocytes, but not in neurons, L-valine and L-proline also inhibited L-[3H]serine uptake. Neither α-methyl aminoisobutyric acid (a system A-specific substrate) nor 2-aminobicyclo(2,2,1)heptane-2-carboxylic acid (a system L-specific substrate) inhibited the uptake of L-[3H]serine in both neurons and astrocytes. Expression of ASCT transporters in both neurons and astrocytes was examined by use of reverse transcriptase polymerase chain reaction and immunoblot analysis. Whereas transcripts (mRNAs) of both ASCT1 and ASCT2 transporters were detected in astrocytes, only the mRNA of the former subtype was detected in neurons. Immunoblot analysis confirmed the presence of ASCT1 in both neurons and astrocytes. These findings indicate that neurons accumulate a high level of L-serine by using a Na+-dependent, high-affinity transport system, operating predominantly through the ASCT1 transporter subtype. |
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AbstractList | The non‐essential amino acid L‐serine was shown to be required to support the survival of rat cerebellar Purkinje neurons because of lack of the expression of the L‐serine biosynthesis enzyme 3‐phosphoglycerate dehydrogenase in them. In the present study, we investigated L‐[3H]serine uptake in primary cultures of neurons and astrocytes from the rat telencephalon. In both neurons and astrocytes, L‐[3H]serine uptake was dependent on temperature and Na+ ions, and exhibited a single component of high‐affinity uptake sites (K
m=15.0 and 17.2 μM for neurons and astrocytes, respectively). Kinetic analysis of L‐[3H]serine uptake also revealed that the uptake into neurons was faster than that into astrocytes. The selectivity of inhibition by amino acids of the L‐[3H]serine uptake resembled that of the system ASC transporters ASCT1 and ASCT2. Neutral amino acids L‐alanine, L‐serine, L‐cysteine, and L‐threonine strongly inhibited the uptake by both cell types. Furthermore, in astrocytes, but not in neurons, L‐valine and L‐proline also inhibited L‐[3H]serine uptake. Neither α‐methyl aminoisobutyric acid (a system A‐specific substrate) nor 2‐aminobicyclo(2,2,1)heptane‐2‐carboxylic acid (a system L‐specific substrate) inhibited the uptake of L‐[3H]serine in both neurons and astrocytes. Expression of ASCT transporters in both neurons and astrocytes was examined by use of reverse transcriptase polymerase chain reaction and immunoblot analysis. Whereas transcripts (mRNAs) of both ASCT1 and ASCT2 transporters were detected in astrocytes, only the mRNA of the former subtype was detected in neurons. Immunoblot analysis confirmed the presence of ASCT1 in both neurons and astrocytes. These findings indicate that neurons accumulate a high level of L‐serine by using a Na+‐dependent, high‐affinity transport system, operating predominantly through the ASCT1 transporter subtype. The non‐essential amino acid L ‐serine was shown to be required to support the survival of rat cerebellar Purkinje neurons because of lack of the expression of the L ‐serine biosynthesis enzyme 3‐phosphoglycerate dehydrogenase in them. In the present study, we investigated L ‐[ 3 H]serine uptake in primary cultures of neurons and astrocytes from the rat telencephalon. In both neurons and astrocytes, L ‐[ 3 H]serine uptake was dependent on temperature and Na + ions, and exhibited a single component of high‐affinity uptake sites ( K m =15.0 and 17.2 μM for neurons and astrocytes, respectively). Kinetic analysis of L ‐[ 3 H]serine uptake also revealed that the uptake into neurons was faster than that into astrocytes. The selectivity of inhibition by amino acids of the L ‐[ 3 H]serine uptake resembled that of the system ASC transporters ASCT1 and ASCT2. Neutral amino acids L ‐alanine, L ‐serine, L ‐cysteine, and L ‐threonine strongly inhibited the uptake by both cell types. Furthermore, in astrocytes, but not in neurons, L ‐valine and L ‐proline also inhibited L ‐[ 3 H]serine uptake. Neither α‐methyl aminoisobutyric acid (a system A‐specific substrate) nor 2‐aminobicyclo(2,2,1)heptane‐2‐carboxylic acid (a system L‐specific substrate) inhibited the uptake of L ‐[ 3 H]serine in both neurons and astrocytes. Expression of ASCT transporters in both neurons and astrocytes was examined by use of reverse transcriptase polymerase chain reaction and immunoblot analysis. Whereas transcripts (mRNAs) of both ASCT1 and ASCT2 transporters were detected in astrocytes, only the mRNA of the former subtype was detected in neurons. Immunoblot analysis confirmed the presence of ASCT1 in both neurons and astrocytes. These findings indicate that neurons accumulate a high level of L ‐serine by using a Na + ‐dependent, high‐affinity transport system, operating predominantly through the ASCT1 transporter subtype. The non-essential amino acid L-serine was shown to be required to support the survival of rat cerebellar Purkinje neurons because of lack of the expression of the L-serine biosynthesis enzyme 3-phosphoglycerate dehydrogenase in them. In the present study, we investigated L-[3H]serine uptake in primary cultures of neurons and astrocytes from the rat telencephalon. In both neurons and astrocytes, L-[3H]serine uptake was dependent on temperature and Na+ ions, and exhibited a single component of high-affinity uptake sites (Km=15.0 and 17.2 μM for neurons and astrocytes, respectively). Kinetic analysis of L-[3H]serine uptake also revealed that the uptake into neurons was faster than that into astrocytes. The selectivity of inhibition by amino acids of the L-[3H]serine uptake resembled that of the system ASC transporters ASCT1 and ASCT2. Neutral amino acids L-alanine, L-serine, L-cysteine, and L-threonine strongly inhibited the uptake by both cell types. Furthermore, in astrocytes, but not in neurons, L-valine and L-proline also inhibited L-[3H]serine uptake. Neither α-methyl aminoisobutyric acid (a system A-specific substrate) nor 2-aminobicyclo(2,2,1)heptane-2-carboxylic acid (a system L-specific substrate) inhibited the uptake of L-[3H]serine in both neurons and astrocytes. Expression of ASCT transporters in both neurons and astrocytes was examined by use of reverse transcriptase polymerase chain reaction and immunoblot analysis. Whereas transcripts (mRNAs) of both ASCT1 and ASCT2 transporters were detected in astrocytes, only the mRNA of the former subtype was detected in neurons. Immunoblot analysis confirmed the presence of ASCT1 in both neurons and astrocytes. These findings indicate that neurons accumulate a high level of L-serine by using a Na+-dependent, high-affinity transport system, operating predominantly through the ASCT1 transporter subtype. The non-essential amino acid L-serine was shown to be required to support the survival of rat cerebellar Purkinje neurons because of lack of the expression of the L-serine biosynthesis enzyme 3-phosphoglycerate dehydrogenase in them. In the present study, we investigated L-[(3)H]serine uptake in primary cultures of neurons and astrocytes from the rat telencephalon. In both neurons and astrocytes, L-[(3)H]serine uptake was dependent on temperature and Na(+) ions, and exhibited a single component of high-affinity uptake sites (K(m)=15.0 and 17.2 micro M for neurons and astrocytes, respectively). Kinetic analysis of L-[(3)H]serine uptake also revealed that the uptake into neurons was faster than that into astrocytes. The selectivity of inhibition by amino acids of the L-[(3)H]serine uptake resembled that of the system ASC transporters ASCT1 and ASCT2. Neutral amino acids L-alanine, L-serine, L-cysteine, and L-threonine strongly inhibited the uptake by both cell types. Furthermore, in astrocytes, but not in neurons, L-valine and L-proline also inhibited L-[(3)H]serine uptake. Neither alpha-methyl aminoisobutyric acid (a system A-specific substrate) nor 2-aminobicyclo(2,2,1)heptane-2-carboxylic acid (a system L-specific substrate) inhibited the uptake of L-[(3)H]serine in both neurons and astrocytes. Expression of ASCT transporters in both neurons and astrocytes was examined by use of reverse transcriptase polymerase chain reaction and immunoblot analysis. Whereas transcripts (mRNAs) of both ASCT1 and ASCT2 transporters were detected in astrocytes, only the mRNA of the former subtype was detected in neurons. Immunoblot analysis confirmed the presence of ASCT1 in both neurons and astrocytes. These findings indicate that neurons accumulate a high level of L-serine by using a Na(+)-dependent, high-affinity transport system, operating predominantly through the ASCT1 transporter subtype. |
Author | Yamamoto, Toshifumi Nishizaki, Itone Takahashi, Kenzo Hirabayashi, Yoshio Okuyama, Shigeru Furuya, Shigeki Yamamoto, Hideko |
Author_xml | – sequence: 1 givenname: Toshifumi surname: Yamamoto fullname: Yamamoto, Toshifumi email: yamamoto@yokohama-cu.ac.jp organization: Laboratory of Molecular Recognition, Graduate School of Integrated Science, Yokohama City University, 22-2 Seto, Kanazawa-ku, Yokohama 236-0027, Japan – sequence: 2 givenname: Itone surname: Nishizaki fullname: Nishizaki, Itone organization: Laboratory of Molecular Recognition, Graduate School of Integrated Science, Yokohama City University, 22-2 Seto, Kanazawa-ku, Yokohama 236-0027, Japan – sequence: 3 givenname: Shigeki surname: Furuya fullname: Furuya, Shigeki organization: Neuronal Circuit Mechanism Research Group, Brain Science Institute, Frontier Research Program, RIKEN, Wako, Saitama 351-0198, Japan – sequence: 4 givenname: Yoshio surname: Hirabayashi fullname: Hirabayashi, Yoshio organization: Neuronal Circuit Mechanism Research Group, Brain Science Institute, Frontier Research Program, RIKEN, Wako, Saitama 351-0198, Japan – sequence: 5 givenname: Kenzo surname: Takahashi fullname: Takahashi, Kenzo organization: Medical Research Laboratory, Taisyo Pharmaceutical Co., Ltd., Saitama 330-8530, Japan – sequence: 6 givenname: Shigeru surname: Okuyama fullname: Okuyama, Shigeru organization: Medical Research Laboratory, Taisyo Pharmaceutical Co., Ltd., Saitama 330-8530, Japan – sequence: 7 givenname: Hideko surname: Yamamoto fullname: Yamamoto, Hideko organization: Department of Molecular Psychiatry, Tokyo Institute of Psychiatry, 2-1-8 Kamikitazawa, Setagaya-ku, Tokyo 156-0057, Japan |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/12885409$$D View this record in MEDLINE/PubMed |
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ContentType | Journal Article |
Copyright | 2003 FEBS Letters 548 (2003) 1873-3468 © 2015 Federation of European Biochemical Societies |
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Keywords | Serine transport ASCT1 Reverse transcriptase polymerase chain reaction MeAIB, α-methyl aminoisobutyric acid BCH, 2-aminobicyclo(2,2,1)heptane-2-carboxylic acid 3-Phosphoglycerate dehydrogenase 3PGDH, 3-phosphoglycerate dehydrogenase |
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Snippet | The non-essential amino acid L-serine was shown to be required to support the survival of rat cerebellar Purkinje neurons because of lack of the expression of... The non‐essential amino acid L‐serine was shown to be required to support the survival of rat cerebellar Purkinje neurons because of lack of the expression of... The non‐essential amino acid L ‐serine was shown to be required to support the survival of rat cerebellar Purkinje neurons because of lack of the expression of... |
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SubjectTerms | 3-Phosphoglycerate dehydrogenase 3PGDH, 3-phosphoglycerate dehydrogenase Amino Acid Transport System ASC - analysis Amino Acid Transport System ASC - genetics Amino Acid Transport System ASC - metabolism Amino Acids, Neutral - pharmacology Animals ASCT1 Astrocytes - chemistry Astrocytes - cytology Astrocytes - metabolism BCH, 2-aminobicyclo(2,2,1)heptane-2-carboxylic acid Cell Culture Techniques Fetus Kinetics MeAIB, α-methyl aminoisobutyric acid Minor Histocompatibility Antigens Neurons - chemistry Neurons - cytology Neurons - metabolism Rats Reverse transcriptase polymerase chain reaction RNA, Messenger - analysis Serine - metabolism Serine transport Sodium - pharmacology Temperature |
Title | Characterization of rapid and high-affinity uptake of L-serine in neurons and astrocytes in primary culture |
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