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Article ; Online: Studies on a unique organelle localization of a liver enzyme, serine:pyruvate (or alanine:glyoxylate) aminotransferase.

Ichiyama, Arata

Proceedings of the Japan Academy. Series B, Physical and biological sciences

2011 Volume 87, Issue 5, Page(s) 274–286

Abstract: Serine:pyruvate (or alanine:glyoxylate) aminotransferase (SPT or AGT) in the liver is unique in that its subcellular distribution is entirely peroxisomal in man and herbivores, and largely mitochondrial in carnivores. In rats, this enzyme is located in ... ...

Abstract	Serine:pyruvate (or alanine:glyoxylate) aminotransferase (SPT or AGT) in the liver is unique in that its subcellular distribution is entirely peroxisomal in man and herbivores, and largely mitochondrial in carnivores. In rats, this enzyme is located in both mitochondria and peroxisomes and only the mitochondrial activity is markedly induced by glucagon. The mechanism of the species-specific dual organelle localization is either transcription of the gene from two different start sites or loss of upstream translation initiation ATG codon by mutations. In herbivores, peroxisomal localization of SPT appears to be indispensable to prevent excessive oxalate production by removing glyoxylate, an immediate precursor of oxalate, formed from glycolate in this organelle. In carnivores, its mitochondrial localization appears to be needed to metabolize glyoxylate formed from L-hydroxyproline in mitochondria. In addition, SPT contributes substantially to gluconeogenesis from serine in rabbit, human and dog livers, irrespective of its mitochondrial or peroxisomal localization. (Communicated by Shigetada Nakanishi, M.J.A.).
MeSH term(s)	Animals ; Base Sequence ; Humans ; Liver/enzymology ; Molecular Sequence Data ; Organelles/enzymology ; Protein Transport ; Species Specificity ; Transaminases/genetics ; Transaminases/metabolism
Chemical Substances	Transaminases (EC 2.6.1.-) ; Alanine-glyoxylate transaminase (EC 2.6.1.44) ; serine-pyruvate aminotransferase (EC 2.6.1.51)
Language	English
Publishing date	2011-05-11
Publishing country	Japan
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	161781-3
ISSN	1349-2896 ; 0386-2208
ISSN (online)	1349-2896
ISSN	0386-2208
DOI	10.2183/pjab.87.274
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Article: Distinctive iron requirement of tryptophan 5-monooxygenase: TPH1 requires dissociable ferrous iron.

Hasegawa, Hiroyuki / Ichiyama, Arata

Biochemical and biophysical research communications

2005 Volume 338, Issue 1, Page(s) 277–284

Abstract: A peripheral type of tryptophan 5-monooxygenase (EC 1.14.16.4), TPH1, is very unstable in vitro, but the inactivation was reversible and full reactivation occurs upon anaerobic incubation with a high concentration of dithiothreitol (DTT, 15 mM). In this ... ...

Abstract	A peripheral type of tryptophan 5-monooxygenase (EC 1.14.16.4), TPH1, is very unstable in vitro, but the inactivation was reversible and full reactivation occurs upon anaerobic incubation with a high concentration of dithiothreitol (DTT, 15 mM). In this study, distinctive iron requirement of TPH1 was revealed through analysis of the enzyme's inactivation and activation by DTT. For this purpose, all the glasswares, plastics, Sephadex G-25 gels, and reagents including protein solutions had been treated with metal chelators, and apo-TPH was prepared by treatment with EDTA. Apo-TPH thus prepared exclusively required free Fe2+ for its catalytic activity; 10(-8) M was enough under the strict absence of Fe3+ but 10(-12) M was too low. No other metal ions including Fe3+ were effective. It appeared that Fe3+ bound to the enzyme with a higher affinity than Fe2+, resulting in the inactivation. Ascorbate, a non-thiol reducing agent, did not substitute DTT in the activation of TPH1, but enhanced the Fe2+-dependent activity of apo-TPH as effectively as DTT. Thus, the DTT-activation was essentially substituted by preparation of apo-TPH by the EDTA treatment and the assay of apo-TPH in the presence of Fe2+ and ascorbate. The activation of TPH1 by incubation with DTT was accompanied by exposure of 9 sulfhydryls out of the total 10 cysteine residues, but the cleavage of disulfide bonds seemed not to be crucial, even if it occurred. The effect of DTT was substituted by some other sulfhydryls whose structure was analogous to that of commonly used metal chelators. Based on these observations, the following dual roles of DTT are proposed: (1) in the activation of TPH, DTT removes inappropriate bound iron (Fe3+) as a chelator, keeping Fe3+ away from the enzyme's binding site which needs to bind Fe2+ for the catalytic activity, and (2) in both the activation and reaction processes, DTT prevents oxidation of Fe2+ to Fe3+ as a reducing agent.
MeSH term(s)	Animals ; Cattle ; Cell Line, Tumor ; Enzyme Activation ; Female ; Ferrous Compounds/chemistry ; Ferrous Compounds/metabolism ; Ligands ; Male ; Mastocytoma/enzymology ; Mice ; Mice, Inbred C57BL ; Mice, Inbred DBA ; Sulfhydryl Compounds/chemistry ; Sulfhydryl Compounds/metabolism ; Tryptophan Hydroxylase/chemistry ; Tryptophan Hydroxylase/metabolism
Chemical Substances	Ferrous Compounds ; Ligands ; Sulfhydryl Compounds ; Tph1 protein, mouse (EC 1.14.16.4) ; Tryptophan Hydroxylase (EC 1.14.16.4)
Language	English
Publishing date	2005-12-09
Publishing country	United States
Document type	Comparative Study ; Journal Article
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2005.09.045
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Article: Primary hyperoxaluria type 1 in Japan.

Takayama, Tatsuya / Nagata, Masao / Ichiyama, Arata / Ozono, Seiichiro

American journal of nephrology

2005 Volume 25, Issue 3, Page(s) 297–302

Abstract: Background/aims: Current status of primary hyperoxaluria (PH) has not been surveyed in Japan.: Methods: Japanese patients with PH were reviewed in the published literature.: Results: Fifty-nine patients were diagnosed as PH from 1962 to 2003. The ... ...

Abstract	Background/aims: Current status of primary hyperoxaluria (PH) has not been surveyed in Japan. Methods: Japanese patients with PH were reviewed in the published literature. Results: Fifty-nine patients were diagnosed as PH from 1962 to 2003. The median ages both at diagnosis and at the onset of initial symptoms were 17 (range: 0.02-63) and 13 (range: 0-58) years, respectively. Twenty-nine (49%) patients were older than 20 years at diagnosis, among whom 26 (90%) already presented end-stage renal failure (ESRF) or soon evolved into ESRF. Among 30 (51%) diagnosed as PH under 20 years old, only 13 (43%) were already in a terminal stage of renal insufficiency. Ten patients were diagnosed as PH1 by liver biopsy. We identified two types of enzymatic phenotypes in 3 of those patients examined. In 1 case, immunoreactive SPT/AGT protein level was very low due to accelerated proteolysis, while in other 2 cases, the immunoreactivity was detected on mitochondria due to mistargeting. Of 9 cases having been subjected to kidney transplantation at a median age of 20 years (range 7.3-40.0), it was only 2 cases that were reported to be successful, while the median survival time of the kidney grafts being 1.4 years (range 0-7). Of 4 patients having undergone combined liver/kidney transplantations (at the ages of 1.3, 1.4, 9 and 41 years, respectively), the surgery was successful in 3 cases; in the remaining one case, however, rejection required removal of the transplanted kidney was observed. The overall survival ratio of all the 59 PH cases accounted for 77, 71 and 55% at 5, 10 and 20 years, respectively. Conclusion: Assuming that the majority of the 59 patients with PH reported was classified as PH1, it is postulated that morbidity of violent infantile PH1 in Japan might be less than those in the USA and Europe, and symptoms of elderly Japanese PH1 patients seem to be milder than those of Western patients. Establishment of an early detection system of PH1 and more popular application of combined liver/kidney transplantation deserve further study.
MeSH term(s)	Adolescent ; Adult ; Age of Onset ; Child ; Child, Preschool ; Female ; Graft Survival ; Humans ; Hyperoxaluria, Primary/complications ; Hyperoxaluria, Primary/enzymology ; Hyperoxaluria, Primary/epidemiology ; Incidence ; Infant ; Infant, Newborn ; Japan/epidemiology ; Kidney Failure, Chronic/etiology ; Kidney Failure, Chronic/surgery ; Kidney Transplantation ; Liver/enzymology ; Liver Transplantation ; Male ; Middle Aged ; Survival Analysis ; Transaminases/metabolism
Chemical Substances	Transaminases (EC 2.6.1.-) ; glutamate-glyoxylate aminotransferase (EC 2.6.1.-) ; Alanine-glyoxylate transaminase (EC 2.6.1.44) ; serine-pyruvate aminotransferase (EC 2.6.1.51)
Language	English
Publishing date	2005-05
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	604540-6
ISSN	0250-8095
ISSN	0250-8095
DOI	10.1159/000086361
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Article ; Online: Assay of alanine:glyoxylate aminotransferase in human liver by its serine: glyoxylate aminotransferase activity.

Nagata, Masao / Ichiyama, Arata / Takayama, Tatsuya / Oda, Toshiaki / Mugiya, Soichi / Ozono, Seiichiro

Biomedical research (Tokyo, Japan)

2009 Volume 30, Issue 5, Page(s) 295–301

Abstract: We have examined assay methods and conditions for human liver alanine:glyoxylate aminotransferase (AGT). This enzyme shows not only the AGT activity but also serine:pyruvate and serine: glyoxylate aminotransferase (SPT and SGT) activities. In the assay ... ...

Abstract	We have examined assay methods and conditions for human liver alanine:glyoxylate aminotransferase (AGT). This enzyme shows not only the AGT activity but also serine:pyruvate and serine: glyoxylate aminotransferase (SPT and SGT) activities. In the assay of AGT activity using crude enzyme preparations, there is the complication that glutamate:glyoxylate aminotransferase (GGT) also contributes to AGT activity, but at present no other enzyme is known to catalyze transamination between L-serine and glyoxylate or pyruvate. Therefore, an assay for AGT using its SGT activity was investigated in which hydroxypyruvate formed from L-serine in the enzymic reaction with glyoxylate was determined by lactate dehydrogenase (LDH) in the presence of tris(hydroxym ethyl)aminomethane (Tris) at pH 8.4. A possible obstacle to this assay is that pyruvate formed from L-serine by serine dehydratase (SDH) interferes with SGT assay as an additional substrate of LDH and AGT. However, the SDH activity in human liver is very low, and by performing the SGT reaction in the presence and absence of glyoxylate the SGT activity was represented as the glyoxylate-dependent hydroxypyruvate formation from L-serine. There was a combined good correlation between the AGT, SGT and SPT activities, and the activity ratio, AGT : SGT : SPT was about 1.0 : 0.17 : 0.13.
MeSH term(s)	Alanine/metabolism ; Animals ; Biological Assay/methods ; Humans ; Liver/enzymology ; Pyridoxal Phosphate/metabolism ; Serine/metabolism ; Tissue Extracts/metabolism ; Transaminases/metabolism
Chemical Substances	Tissue Extracts ; Serine (452VLY9402) ; Pyridoxal Phosphate (5V5IOJ8338) ; Transaminases (EC 2.6.1.-) ; Alanine-glyoxylate transaminase (EC 2.6.1.44) ; serine-glyoxylate aminotransferase (EC 2.6.1.45) ; serine-pyruvate aminotransferase (EC 2.6.1.51) ; Alanine (OF5P57N2ZX)
Language	English
Publishing date	2009-09-23
Publishing country	Japan
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	604561-3
ISSN	1880-313X ; 0388-6107
ISSN (online)	1880-313X
ISSN	0388-6107
DOI	10.2220/biomedres.30.295
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Article: Primary Hyperoxaluria Type 1 in Japan

Takayama, Tatsuya / Nagata, Masao / Ichiyama, Arata / Ozono, Seiichiro

American Journal of Nephrology

2005 Volume 25, Issue 3, Page(s) 297–302

Abstract: Background/Aims: Current status of primary hyperoxaluria (PH) has not been surveyed in Japan. Methods: Japanese patients with PH were reviewed in the published literature. Results: Fifty-nine patients were diagnosed as PH from 1962 to 2003. The median ... ...

Institution	Department of Urology, Hamamatsu University School of Medicine, Shizuoka, Japan
Abstract	Background/Aims: Current status of primary hyperoxaluria (PH) has not been surveyed in Japan. Methods: Japanese patients with PH were reviewed in the published literature. Results: Fifty-nine patients were diagnosed as PH from 1962 to 2003. The median ages both at diagnosis and at the onset of initial symptoms were 17 (range: 0.02–63) and 13 (range: 0–58) years, respectively. Twenty-nine (49%) patients were older than 20 years at diagnosis, among whom 26 (90%) already presented end-stage renal failure (ESRF) or soon evolved into ESRF. Among 30 (51%) diagnosed as PH under 20 years old, only 13 (43%) were already in a terminal stage of renal insufficiency. Ten patients were diagnosed as PH1 by liver biopsy. We identified two types of enzymatic phenotypes in 3 of those patients examined. In 1 case, immunoreactive SPT/AGT protein level was very low due to accelerated proteolysis, while in other 2 cases, the immunoreactivity was detected on mitochondria due to mistargeting. Of 9 cases having been subjected to kidney transplantation at a median age of 20 years (range 7.3–40.0), it was only 2 cases that were reported to be successful, while the median survival time of the kidney grafts being 1.4 years (range 0–7). Of 4 patients having undergone combined liver/kidney transplantations (at the ages of 1.3, 1.4, 9 and 41 years, respectively), the surgery was successful in 3 cases; in the remaining one case, however, rejection required removal of the transplanted kidney was observed. The overall survival ratio of all the 59 PH cases accounted for 77, 71 and 55% at 5, 10 and 20 years, respectively. Conclusion: Assuming that the majority of the 59 patients with PH reported was classified as PH1, it is postulated that morbidity of violent infantile PH1 in Japan might be less than those in the USA and Europe, and symptoms of elderly Japanese PH1 patients seem to be milder than those of Western patients. Establishment of an early detection system of PH1 and more popular application of combined liver/kidney transplantation deserve further study.
Keywords	Serine:pyruvate/alanine:glyoxylate aminotransferase ; Alanine:glyoxylate aminotransferase ; Primary hyperoxaluria
Language	English
Publishing date	2005-07-01
Publisher	S. Karger AG
Publishing place	Basel, Switzerland
Document type	Article
Note	In-Depth Topic Review
ZDB-ID	604540-6
ISSN	1421-9670 ; 0250-8095
ISSN (online)	1421-9670
ISSN	0250-8095
DOI	10.1159/000086361
Database	Karger publisher's database

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Article: The role of Sp1 and AP-2 in basal and protein kinase A--induced expression of mitochondrial serine:pyruvate aminotransferase in hepatocytes.

Uchida, Chiharu / Oda, Toshiaki / Sugiyama, Tsuyoshi / Otani, Sunao / Kitagawa, Masatoshi / Ichiyama, Arata

The Journal of biological chemistry

2002 Volume 277, Issue 42, Page(s) 39082–39092

Abstract: Transcription of mitochondrial serine:pyruvate aminotransferase (SPT) mRNA (SPTm-mRNA) in rat liver is unique in that it occurs from the upstream site of the two transcription start sites within the first exon of the SPT gene and is selectively enhanced ... ...

Abstract	Transcription of mitochondrial serine:pyruvate aminotransferase (SPT) mRNA (SPTm-mRNA) in rat liver is unique in that it occurs from the upstream site of the two transcription start sites within the first exon of the SPT gene and is selectively enhanced by cAMP via the protein kinase A (PKA) signaling pathway. In this study, we identified the DNA elements and nuclear factors responsible for the basal and PKA-induced activities of the upstream promoter. By using a luciferase reporter assay with HepG2 cells, DNase I footprinting analysis, and gel shift experiments, we identified the binding sites for Sp1 and AP-2 within the regions -125 to -89 and -14 to +10, respectively. Mutational analyses indicated that these regions are essential for the transcription factor binding and the SPT promoter activity. Expression of AP-2 caused a marked increase in the basal promoter activity to about the same level as that achieved by PKA. On the other hand, both the basal and PKA-induced activities were elevated by overexpression of Sp1, its effect on PKA-induced activity being more pronounced with coexpression of CBP and repressed by E1A oncoprotein. These results suggest that AP-2 and Sp1 regulate basal promoter activity, and Sp1 is also involved in PKA-mediated expression of the rat SPT gene in concert with the transcriptional coactivator CBP.
MeSH term(s)	Animals ; Binding Sites ; Cells, Cultured ; Cyclic AMP ; Cyclic AMP-Dependent Protein Kinases/metabolism ; DNA Mutational Analysis ; DNA-Binding Proteins/physiology ; Deoxyribonuclease I/metabolism ; Gene Expression Regulation, Enzymologic ; Genetic Vectors ; Hepatocytes/enzymology ; Humans ; Luciferases/metabolism ; Mitochondria/enzymology ; Plasmids/metabolism ; Promoter Regions, Genetic ; Protein Binding ; RNA, Messenger/metabolism ; Rats ; Signal Transduction ; Sp1 Transcription Factor/physiology ; Thymidine Kinase/metabolism ; Transaminases/metabolism ; Transcription Factor AP-2 ; Transcription Factors/physiology ; Transcriptional Activation ; Transfection
Chemical Substances	DNA-Binding Proteins ; RNA, Messenger ; Sp1 Transcription Factor ; Transcription Factor AP-2 ; Transcription Factors ; Cyclic AMP (E0399OZS9N) ; Luciferases (EC 1.13.12.-) ; Transaminases (EC 2.6.1.-) ; serine-pyruvate aminotransferase (EC 2.6.1.51) ; Thymidine Kinase (EC 2.7.1.21) ; Cyclic AMP-Dependent Protein Kinases (EC 2.7.11.11) ; Deoxyribonuclease I (EC 3.1.21.1)
Language	English
Publishing date	2002-08-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M201380200
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Article: Control of oxalate formation from L-hydroxyproline in liver mitochondria.

Takayama, Tatsuya / Fujita, Kimio / Suzuki, Kazuo / Sakaguchi, Michiko / Fujie, Michio / Nagai, Erina / Watanabe, Shinya / Ichiyama, Arata / Ogawa, Yoshihide

Journal of the American Society of Nephrology : JASN

2003 Volume 14, Issue 4, Page(s) 939–946

Abstract: Serine:pyruvate/alanine:glyoxylate aminotransferase (SPT/AGT) is largely located in mitochondria in carnivores, whereas it is entirely found within peroxisomes in herbivores and humans. In rat liver, SPT/AGT is found in both of these organelles, and only ...

Abstract	Serine:pyruvate/alanine:glyoxylate aminotransferase (SPT/AGT) is largely located in mitochondria in carnivores, whereas it is entirely found within peroxisomes in herbivores and humans. In rat liver, SPT/AGT is found in both of these organelles, and only the mitochondrial enzyme is markedly induced by glucagon. Although SPT/AGT is a bifunctional enzyme involved in the metabolism of both L-serine and glyoxylate, its contribution to L-serine metabolism is independent of mitochondrial or peroxisomal localization (Xue HH et al., J Biol Chem 274: 16028-16033, 1999). Therefore, the species-specific and food habit-dependent organelle distribution might be required for proper metabolism of glyoxylate at the subcellular site of its formation. Glyoxylate formation from glycolate and that from L-hydroxyproline have been shown to occur in peroxisomes and mitochondria, respectively. The present study found that urinary excretion of oxalate was markedly increased when a large dose of L-hydroxyproline or glycolate was administered to rats. Oxalate formation from L-hydroxyproline but not that from glycolate was significantly reduced when mitochondrial SPT/AGT had been induced by glucagon. The hydroxyproline content of collagen is 10 to 13%, and collagen accounts for about 30% of total animal protein; therefore, these results suggest that an important role of mitochondrial SPT/AGT in carnivores is to convert L-hydroxyproline-derived glyoxylate into glycine in situ, preventing undesirable overflow into the production of oxalate.
MeSH term(s)	Animals ; Glucagon/metabolism ; Glyoxylates/metabolism ; Glyoxylates/urine ; Hydroxyproline/metabolism ; Liver/enzymology ; Male ; Mitochondria, Liver/metabolism ; Oxalates/metabolism ; Rats ; Rats, Wistar ; Transaminases/metabolism
Chemical Substances	Glyoxylates ; Oxalates ; Glucagon (9007-92-5) ; Transaminases (EC 2.6.1.-) ; Alanine-glyoxylate transaminase (EC 2.6.1.44) ; serine-pyruvate aminotransferase (EC 2.6.1.51) ; glyoxylic acid (JQ39C92HH6) ; Hydroxyproline (RMB44WO89X)
Language	English
Publishing date	2003-02-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1085942-1
ISSN	1533-3450 ; 1046-6673
ISSN (online)	1533-3450
ISSN	1046-6673
DOI	10.1097/01.asn.0000059310.67812.4f
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Article: Analyses in transfected cells and in vitro of a putative peroxisomal targeting signal of rat liver serine:pyruvate aminotransferase.

Mizuno, Takuji / Ito, Kouichi / Uchida, Chiharu / Kitagawa, Masatoshi / Ichiyama, Arata / Miura, Satoshi / Fujita, Kimio / Oda, Toshiaki

Histochemistry and cell biology

2002 Volume 118, Issue 4, Page(s) 321–328

Abstract: Serine:pyruvate aminotransferase (SPT; EC 2.6.1.51) of rat liver is a unique enzyme in that it is located in both mitochondria and peroxisomes. To analyze a peroxisomal targeting signal (PTS) of SPT, we constructed in this study various peroxisomal SPT ... ...

Abstract	Serine:pyruvate aminotransferase (SPT; EC 2.6.1.51) of rat liver is a unique enzyme in that it is located in both mitochondria and peroxisomes. To analyze a peroxisomal targeting signal (PTS) of SPT, we constructed in this study various peroxisomal SPT clones having mutations at the C-terminal 20-amino acid region in which a putative PTS is located, and we examined subcellular localization of mutated products expressed in transfected COS-1 cells. When the mutant SPTs were unstable in transfected COS-1 cells, their translocation into peroxisomes was examined using an in vitro peroxisomal import system. Deletion of the C-terminal tripeptide, NKL, and amino acid substitution of K2 (the second lysine from the C-terminus), K4, or E15 abolished or impaired the peroxisomal import of the translated product, resulting in cytosolic accumulation in the cell. In the cases of mutation of R18G, D19A, or K2Q and the conversion to proline of L9, L13, V17, or A20, no products were detected in transfected cells. However, the results of an in vitro peroxisomal import experiment showed that the mutation of L9P, L13P, V17P, and A20P caused loss of the PTS function. When serine was introduced instead of N3 to generate a typical PTS1, the SKL motif, at the C-terminus, all of the proteins having mutations at P5, E11, R12, or E15 showed extensive localization in peroxisomes. These results suggest that the putative C-terminal PTS of SPT is not equivalent to the typical PTS1 shown in acyl-CoA oxidase and urate oxidase, because the PTS of SPT is not restricted to the C-terminal tripeptide. The results also suggest that the alpha-helical structure of the C-terminal region of SPT is important for the stable conformation of the enzyme and the peroxisomal targeting function of its PTS.
MeSH term(s)	Animals ; COS Cells ; DNA Primers/chemistry ; Immunohistochemistry ; Liver/enzymology ; Mutagenesis, Site-Directed ; Peroxisomes/enzymology ; Point Mutation ; Protein Sorting Signals ; Transaminases/genetics ; Transaminases/metabolism ; Transfection
Chemical Substances	DNA Primers ; Protein Sorting Signals ; Transaminases (EC 2.6.1.-) ; serine-pyruvate aminotransferase (EC 2.6.1.51)
Language	English
Publishing date	2002-10
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1222930-1
ISSN	1432-119X ; 0948-6143 ; 0301-5564
ISSN (online)	1432-119X
ISSN	0948-6143 ; 0301-5564
DOI	10.1007/s00418-002-0455-6
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Article: Radioreceptor assay of methionine-enkephalin-like substance in human cerebrospinal fluid.

Furui, Tomoo / Kageyama, Naoki / Haga, Tatsuya / Ichiyama, Arata / Fukushima, Masanori

Pain

1980 Volume 9, Issue 1, Page(s) 63–72

Abstract: A sensitive and simple radioreceptor assay system for measuring methionine(met)-enkephalin-like substance in human cerebrospinal fluid (CSF) was developed using a particulate fraction of rat brain as a receptor preparation and [3H]dihydromorphine as a ... ...

Abstract	A sensitive and simple radioreceptor assay system for measuring methionine(met)-enkephalin-like substance in human cerebrospinal fluid (CSF) was developed using a particulate fraction of rat brain as a receptor preparation and [3H]dihydromorphine as a radiolabeled ligand in the presence of 1 mM ethylenediamine tetracetate (EDTA) and 2 mM magnesium acetate. Metenkephalin-like substance was purified from CSF by the combination of Sephadex G-10 and SP-Sephadex (H+) column chromatographies to be free of sodium and large molecular weight substance such as beta-endorphin. The assays were carried out on samples obtained from normal subjects and patients with the disease of the brain or pituitary by lumbar or ventricular puncture. Mean level in samples obtained from normal subjects by lumbar puncture was 2.6 +/- 1.0 pmoles/ml.
MeSH term(s)	Animals ; Brain Chemistry ; Endorphins/cerebrospinal fluid ; Enkephalins/cerebrospinal fluid ; Humans ; Methionine/cerebrospinal fluid ; Radioligand Assay ; Rats
Chemical Substances	Endorphins ; Enkephalins ; Methionine (AE28F7PNPL)
Language	English
Publishing date	1980-08
Publishing country	United States
Document type	Journal Article
ZDB-ID	193153-2
ISSN	1872-6623 ; 0304-3959
ISSN (online)	1872-6623
ISSN	0304-3959
DOI	10.1016/0304-3959(80)90029-9
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Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

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