메뉴 건너뛰기




Volumn 382, Issue 2, 2009, Pages 415-418

Occurrence of phosphatidyl-d-serine in the rat cerebrum

Author keywords

Brain; Cerebrum; d Serine; Phosphatidylserine; Phospholipids; Rat

Indexed keywords

DEXTRO SERINE; DIVALENT CATION; EDETIC ACID; PHOSPHATIDYLSERINE; PHOSPHOLIPASE C; PHOSPHOLIPASE D; PHOSPHOSERINE;

EID: 63349108294     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.03.035     Document Type: Article
Times cited : (4)

References (36)
  • 1
    • 0345374586 scopus 로고    scopus 로고
    • Phosphatidylserine receptor is required for clearance of apoptotic cells
    • Li M.O., Sarkisian M.R., Mehal W.Z., Rakic P., and Flavell R.A. Phosphatidylserine receptor is required for clearance of apoptotic cells. Science 302 (2003) 1560-1563
    • (2003) Science , vol.302 , pp. 1560-1563
    • Li, M.O.1    Sarkisian, M.R.2    Mehal, W.Z.3    Rakic, P.4    Flavell, R.A.5
  • 2
    • 0021227676 scopus 로고
    • The role of protein kinase C in cell surface signal transduction and tumour promotion
    • Nishizuka Y. The role of protein kinase C in cell surface signal transduction and tumour promotion. Nature 308 (1984) 693-698
    • (1984) Nature , vol.308 , pp. 693-698
    • Nishizuka, Y.1
  • 3
    • 0025804529 scopus 로고
    • Lipid activation of protein kinase C
    • Bell R.M., and Burns D.J. Lipid activation of protein kinase C. J. Biol. Chem. 266 (1991) 4661-4664
    • (1991) J. Biol. Chem. , vol.266 , pp. 4661-4664
    • Bell, R.M.1    Burns, D.J.2
  • 4
    • 0011803402 scopus 로고
    • An amino acid constituent of brain cephalin
    • Folch J., and Schneider H.A. An amino acid constituent of brain cephalin. J. Biol. Chem. 137 (1941) 51-62
    • (1941) J. Biol. Chem. , vol.137 , pp. 51-62
    • Folch, J.1    Schneider, H.A.2
  • 5
    • 32644480982 scopus 로고
    • The isolation of phosphatidyl serine from brain cepharin, and identification of the serine component
    • Folch J. The isolation of phosphatidyl serine from brain cepharin, and identification of the serine component. J. Biol. Chem. 139 (1941) 973-974
    • (1941) J. Biol. Chem. , vol.139 , pp. 973-974
    • Folch, J.1
  • 6
    • 33645335557 scopus 로고
    • The chemical structure of phosphatidyl serine
    • Folch J. The chemical structure of phosphatidyl serine. J. Biol. Chem. 174 (1947) 439-450
    • (1947) J. Biol. Chem. , vol.174 , pp. 439-450
    • Folch, J.1
  • 9
    • 0029156742 scopus 로고
    • Anatomical distribution and postnatal changes in endogenous free d-aspartate and d-serine in rat brain and periphery
    • Hashimoto A., Oka T., and Nishikawa T. Anatomical distribution and postnatal changes in endogenous free d-aspartate and d-serine in rat brain and periphery. Eur. J. Neurosci. 7 (1995) 1657-1663
    • (1995) Eur. J. Neurosci. , vol.7 , pp. 1657-1663
    • Hashimoto, A.1    Oka, T.2    Nishikawa, T.3
  • 11
    • 0028988978 scopus 로고
    • d-Serine, an endogenous synaptic modulator: localization to astrocytes and glutamate-stimulated release
    • Schell M.J., Molliver M.E., and Snyder S.H. d-Serine, an endogenous synaptic modulator: localization to astrocytes and glutamate-stimulated release. Proc. Natl. Acad. Sci. USA 92 (1995) 3948-3952
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3948-3952
    • Schell, M.J.1    Molliver, M.E.2    Snyder, S.H.3
  • 13
    • 0017893962 scopus 로고
    • Characterization of phosphatidylthreonine in polyoma virus transformed fibroblasts
    • Mark-Malchoff D., Marinetti G.V., Hare G.D., and Meisler A. Characterization of phosphatidylthreonine in polyoma virus transformed fibroblasts. Biochemistry 17 (1978) 2684-2688
    • (1978) Biochemistry , vol.17 , pp. 2684-2688
    • Mark-Malchoff, D.1    Marinetti, G.V.2    Hare, G.D.3    Meisler, A.4
  • 14
    • 0017378048 scopus 로고
    • The enzymatic synthesis of phosphatidylserine and purification by CM-cellulose column chromatography
    • Comfurius P., and Zwaal R.F. The enzymatic synthesis of phosphatidylserine and purification by CM-cellulose column chromatography. Biochim. Biophys. Acta 488 (1977) 36-42
    • (1977) Biochim. Biophys. Acta , vol.488 , pp. 36-42
    • Comfurius, P.1    Zwaal, R.F.2
  • 15
    • 51649179265 scopus 로고
    • Quantitative analysis of phospholipids by thin-layer chromatography and phosphorus analysis of spots
    • Rouser G., Siakotos A.N., and Fleischer S. Quantitative analysis of phospholipids by thin-layer chromatography and phosphorus analysis of spots. Lipids 1 (1966) 85-86
    • (1966) Lipids , vol.1 , pp. 85-86
    • Rouser, G.1    Siakotos, A.N.2    Fleischer, S.3
  • 16
    • 85004570887 scopus 로고
    • Purification and properties of phospholipase D from Actinomadura sp. strain No. 362
    • Kokusho Y., Kato S., Machida H., and Iwasaki S. Purification and properties of phospholipase D from Actinomadura sp. strain No. 362. Agric. Biol. Chem. 51 (1987) 2515-2524
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 2515-2524
    • Kokusho, Y.1    Kato, S.2    Machida, H.3    Iwasaki, S.4
  • 17
    • 0016361463 scopus 로고
    • Phospholipase C (phosphatidylcholine cholinephosphohydrolase, EC 3.1.4.3) from Bacillus cereus
    • Zwaal R.F., and Roelofsen B. Phospholipase C (phosphatidylcholine cholinephosphohydrolase, EC 3.1.4.3) from Bacillus cereus. Methods Enzymol. 32 (1974) 154-161
    • (1974) Methods Enzymol. , vol.32 , pp. 154-161
    • Zwaal, R.F.1    Roelofsen, B.2
  • 18
    • 0026455011 scopus 로고
    • Determination of free amino acid enantiomers in rat brain and serum by high-performance liquid chromatography after derivatization with N-tert-butyloxycarbonyl-l-cysteine and o-phthaldialdehyde
    • Hashimoto A., Nishikawa T., Oka T., Takahashi K., and Hayashi T. Determination of free amino acid enantiomers in rat brain and serum by high-performance liquid chromatography after derivatization with N-tert-butyloxycarbonyl-l-cysteine and o-phthaldialdehyde. J. Chromatogr. 582 (1992) 41-48
    • (1992) J. Chromatogr. , vol.582 , pp. 41-48
    • Hashimoto, A.1    Nishikawa, T.2    Oka, T.3    Takahashi, K.4    Hayashi, T.5
  • 19
    • 0028820805 scopus 로고
    • Separation and quantification of d- and l-phosphoserine in rat brain using Nα-(2, 4-dinitro-5-fluorophenyl)-l-alaninamide (Marfey's reagent) by high-performance liquid chromatography with ultraviolet detection
    • Goodnough D.B., Lutz M.P., and Wood P.L. Separation and quantification of d- and l-phosphoserine in rat brain using Nα-(2, 4-dinitro-5-fluorophenyl)-l-alaninamide (Marfey's reagent) by high-performance liquid chromatography with ultraviolet detection. J. Chromatogr. B Biomed. Appl. 672 (1995) 290-294
    • (1995) J. Chromatogr. B Biomed. Appl. , vol.672 , pp. 290-294
    • Goodnough, D.B.1    Lutz, M.P.2    Wood, P.L.3
  • 20
    • 0014516141 scopus 로고
    • The distribution of phospholipase D in developing and mature plants
    • Quarles R.H., and Dawson R.M. The distribution of phospholipase D in developing and mature plants. Biochem. J. 112 (1969) 787-794
    • (1969) Biochem. J. , vol.112 , pp. 787-794
    • Quarles, R.H.1    Dawson, R.M.2
  • 21
    • 0016814451 scopus 로고
    • Phosphatidohydrolase activity in a solubilized preparation from rat brain particulate fraction
    • Saito M., and Kanfer J. Phosphatidohydrolase activity in a solubilized preparation from rat brain particulate fraction. Arch. Biochem. Biophys. 169 (1975) 318-323
    • (1975) Arch. Biochem. Biophys. , vol.169 , pp. 318-323
    • Saito, M.1    Kanfer, J.2
  • 22
    • 0021846710 scopus 로고
    • Isolation of a somatic-cell mutant defective in phosphatidylserine biosynthesis
    • Kuge O., Nishijima M., and Akamatsu Y. Isolation of a somatic-cell mutant defective in phosphatidylserine biosynthesis. Proc. Natl. Acad. Sci. USA 82 (1985) 1926-1930
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 1926-1930
    • Kuge, O.1    Nishijima, M.2    Akamatsu, Y.3
  • 23
    • 0022636810 scopus 로고
    • Isolation and characterization of a Chinese hamster ovary cell line requiring ethanolamine or phosphatidylserine for growth and exhibiting defective phosphatidylserine synthase activity
    • Voelker D.R., and Frazier J.L. Isolation and characterization of a Chinese hamster ovary cell line requiring ethanolamine or phosphatidylserine for growth and exhibiting defective phosphatidylserine synthase activity. J. Biol. Chem. 261 (1986) 1002-1008
    • (1986) J. Biol. Chem. , vol.261 , pp. 1002-1008
    • Voelker, D.R.1    Frazier, J.L.2
  • 24
    • 0032479436 scopus 로고    scopus 로고
    • Genetic evidence that phosphatidylserine synthase II catalyzes the conversion of phosphatidylethanolamine to phosphatidylserine in Chinese hamster ovary cells
    • Saito K., Nishijima M., and Kuge O. Genetic evidence that phosphatidylserine synthase II catalyzes the conversion of phosphatidylethanolamine to phosphatidylserine in Chinese hamster ovary cells. J. Biol. Chem. 273 (1998) 17199-17205
    • (1998) J. Biol. Chem. , vol.273 , pp. 17199-17205
    • Saito, K.1    Nishijima, M.2    Kuge, O.3
  • 26
    • 19444379562 scopus 로고    scopus 로고
    • Regio- and stereospecific analysis of glycerolipids
    • Kuksis A., and Itabashi Y. Regio- and stereospecific analysis of glycerolipids. Methods 36 (2005) 172-185
    • (2005) Methods , vol.36 , pp. 172-185
    • Kuksis, A.1    Itabashi, Y.2
  • 28
    • 0024427970 scopus 로고
    • Phospholipid functional groups involved in protein kinase C activation, phorbol ester binding, and binding to mixed micelles
    • Lee M.H., and Bell R.M. Phospholipid functional groups involved in protein kinase C activation, phorbol ester binding, and binding to mixed micelles. J. Biol. Chem. 264 (1989) 14797-14805
    • (1989) J. Biol. Chem. , vol.264 , pp. 14797-14805
    • Lee, M.H.1    Bell, R.M.2
  • 29
    • 0032168891 scopus 로고    scopus 로고
    • The chirality of phosphatidylserine and the activation of protein kinase C
    • Epand R.M., Stevenson C., Bruins R., Schram V., and Glaser M. The chirality of phosphatidylserine and the activation of protein kinase C. Biochemistry 37 (1998) 12068-12073
    • (1998) Biochemistry , vol.37 , pp. 12068-12073
    • Epand, R.M.1    Stevenson, C.2    Bruins, R.3    Schram, V.4    Glaser, M.5
  • 30
    • 22144463880 scopus 로고    scopus 로고
    • Metabolism and functions of phosphatidylserine
    • Vance J.E., and Steenbergen R. Metabolism and functions of phosphatidylserine. Prog. Lipid Res. 44 (2005) 207-234
    • (2005) Prog. Lipid Res. , vol.44 , pp. 207-234
    • Vance, J.E.1    Steenbergen, R.2
  • 31
    • 0029025347 scopus 로고
    • Extracellular concentration of endogenous free d-serine in the rat brain as revealed by in vivo microdialysis
    • Hashimoto A., Oka T., and Nishikawa T. Extracellular concentration of endogenous free d-serine in the rat brain as revealed by in vivo microdialysis. Neuroscience 66 (1995) 635-643
    • (1995) Neuroscience , vol.66 , pp. 635-643
    • Hashimoto, A.1    Oka, T.2    Nishikawa, T.3
  • 32
    • 0027473657 scopus 로고
    • Endogenous d-serine in rat brain: N-methyl-d-aspartate receptor-related distribution and aging
    • Hashimoto A., Nishikawa T., Oka T., and Takahashi K. Endogenous d-serine in rat brain: N-methyl-d-aspartate receptor-related distribution and aging. J. Neurochem. 60 (1993) 783-786
    • (1993) J. Neurochem. , vol.60 , pp. 783-786
    • Hashimoto, A.1    Nishikawa, T.2    Oka, T.3    Takahashi, K.4
  • 34
    • 0033539510 scopus 로고    scopus 로고
    • Serine racemase: a glial enzyme synthesizing d-serine to regulate glutamate-N-methyl-d-aspartate neurotransmission
    • Wolosker H., Blackshaw S., and Snyder S.H. Serine racemase: a glial enzyme synthesizing d-serine to regulate glutamate-N-methyl-d-aspartate neurotransmission. Proc. Natl. Acad. Sci. USA 96 (1999) 13409-13414
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13409-13414
    • Wolosker, H.1    Blackshaw, S.2    Snyder, S.H.3
  • 36
    • 52049087606 scopus 로고    scopus 로고
    • PLG72 modulates intracellular d-serine levels through its interaction with d-amino acid oxidase: effect on schizophrenia susceptibility
    • Sacchi S., Bernasconi M., Martineau M., Mothet J.P., Ruzzene M., Pilone M.S., Pollegioni L., and Molla G. PLG72 modulates intracellular d-serine levels through its interaction with d-amino acid oxidase: effect on schizophrenia susceptibility. J. Biol. Chem. 283 (2008) 22244-22256
    • (2008) J. Biol. Chem. , vol.283 , pp. 22244-22256
    • Sacchi, S.1    Bernasconi, M.2    Martineau, M.3    Mothet, J.P.4    Ruzzene, M.5    Pilone, M.S.6    Pollegioni, L.7    Molla, G.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.