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Volumn 13, Issue 6, 2004, Pages 1627-1635

Identification of the N-glycosylation sites on glutamate carboxypeptidase II necessary for proteolytic activity

Author keywords

Enzyme kinetics; GCPII; Glycosylation; NAALADase; Proteolytic activity; PSMA

Indexed keywords

GAMMA GLUTAMYL HYDROLASE; GAMMA GLUTAMYL HYDROLASE 2; N ACETYLASPARTYLGLUTAMIC ACID; PEPTIDE DERIVATIVE; PROSTATE SPECIFIC MEMBRANE ANTIGEN; UNCLASSIFIED DRUG;

EID: 2442663919     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.04622104     Document Type: Article
Times cited : (91)

References (35)
  • 1
    • 0035121494 scopus 로고    scopus 로고
    • Cloning, expression, genomic localization, and enzymatic activities of the mouse homolog of prostate-specific membrane antigen/NAALADase/folate hydrolase
    • Bacich, D.J., Pinto, J.T., Tong, W.P., and Heston, W.D. 2001 . Cloning, expression, genomic localization, and enzymatic activities of the mouse homolog of prostate-specific membrane antigen/NAALADase/folate hydrolase. Mamm. Genome 12: 117-123.
    • (2001) Mamm. Genome , vol.12 , pp. 117-123
    • Bacich, D.J.1    Pinto, J.T.2    Tong, W.P.3    Heston, W.D.4
  • 2
    • 0036488137 scopus 로고    scopus 로고
    • Substrate specificity, inhibition and enzymological analysis of recombinant human glutamate carboxypeptidase II
    • Barinka, C., Rinnova, M., Šácha, P., Rojas, C., Majer, P., Slusher, B.S., and Konvalinka, J. 2002. Substrate specificity, inhibition and enzymological analysis of recombinant human glutamate carboxypeptidase II. J. Neurochem. 80: 477-487.
    • (2002) J. Neurochem. , vol.80 , pp. 477-487
    • Barinka, C.1    Rinnova, M.2    Šácha, P.3    Rojas, C.4    Majer, P.5    Slusher, B.S.6    Konvalinka, J.7
  • 3
    • 0028985483 scopus 로고
    • N-acetylated α-linked acidic dipeptidase is expressed by non-myelinating Schwann cells in the peripheral nervous system
    • Berger, U.V., Carter, R.E., McKee, M., and Coyle, J.T. 1995. N-acetylated α-linked acidic dipeptidase is expressed by non-myelinating Schwann cells in the peripheral nervous system. J. Neurocytol. 24: 99-109.
    • (1995) J. Neurocytol. , vol.24 , pp. 99-109
    • Berger, U.V.1    Carter, R.E.2    McKee, M.3    Coyle, J.T.4
  • 4
    • 0043225730 scopus 로고    scopus 로고
    • Determination of the complete covalent structure of the major glycoform of DQH sperm surface protein, a novel trypsin-resistant boar seminal plasma O-glycoprotein related to pB1 protein
    • Bezouska, K. Sklenář, J., Novák, P., Halada, P., Havlicek, V., Kraus, M., Ticha, M., and Jonakova, V. 1999. Determination of the complete covalent structure of the major glycoform of DQH sperm surface protein, a novel trypsin-resistant boar seminal plasma O-glycoprotein related to pB1 protein. Protein Sci. 8: 1551-1556.
    • (1999) Protein Sci. , vol.8 , pp. 1551-1556
    • Bezouska, K.1    Sklenář, J.2    Novák, P.3    Halada, P.4    Havlicek, V.5    Kraus, M.6    Ticha, M.7    Jonakova, V.8
  • 5
    • 0030658978 scopus 로고    scopus 로고
    • Molecular cloning of a peptidase against N-acetylaspartylglutamate from a rat hippocampal cDNA library
    • Bzdega, T., Turi, T., Wroblewska, B., She, D., Chung, H.S., Kim, H., and Neale, J.H. 1997. Molecular cloning of a peptidase against N-acetylaspartylglutamate from a rat hippocampal cDNA library. J. Neurochem. 69: 2270-2277.
    • (1997) J. Neurochem. , vol.69 , pp. 2270-2277
    • Bzdega, T.1    Turi, T.2    Wroblewska, B.3    She, D.4    Chung, H.S.5    Kim, H.6    Neale, J.H.7
  • 6
    • 0033168844 scopus 로고    scopus 로고
    • Five different anti-prostate-specific membrane antigen (PSMA) antibodies confirm PSMA expression in tumor-associated neovasculature
    • Chang, S.S., Reuter, V.E., Heston, W.D., Bander, N.H., Grauer, L.S., and Gaudin, P.B. 1999. Five different anti-prostate-specific membrane antigen (PSMA) antibodies confirm PSMA expression in tumor-associated neovasculature. Cancer Res. 59: 3192-3198.
    • (1999) Cancer Res. , vol.59 , pp. 3192-3198
    • Chang, S.S.1    Reuter, V.E.2    Heston, W.D.3    Bander, N.H.4    Grauer, L.S.5    Gaudin, P.B.6
  • 7
    • 0028773280 scopus 로고
    • Crystal structure of Aeromonas proteolytica aminopeptidase: A prototypical member of the co-catalytic zinc enzyme family
    • Chevrier, B., Schalk, C., D'Orchymont, H., Rondeau, J.M., Moras, D., and Tarnus, C. 1994. Crystal structure of Aeromonas proteolytica aminopeptidase: A prototypical member of the co-catalytic zinc enzyme family. Structure 2: 283-291.
    • (1994) Structure , vol.2 , pp. 283-291
    • Chevrier, B.1    Schalk, C.2    D'Orchymont, H.3    Rondeau, J.M.4    Moras, D.5    Tarnus, C.6
  • 8
    • 0035001341 scopus 로고    scopus 로고
    • Glutamate uptake
    • Danbolt, N.C. 2001. Glutamate uptake. Prog. Neurobiol. 65: 1-105.
    • (2001) Prog. Neurobiol. , vol.65 , pp. 1-105
    • Danbolt, N.C.1
  • 9
    • 0032967382 scopus 로고    scopus 로고
    • The role of excitotoxicity in neurodegenerative disease: Implications for therapy
    • Doble, A. 1999. The role of excitotoxicity in neurodegenerative disease: Implications for therapy. Pharmacol. Ther. 81: 163-221.
    • (1999) Pharmacol. Ther. , vol.81 , pp. 163-221
    • Doble, A.1
  • 10
    • 0025367812 scopus 로고
    • Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implications for protein engineering
    • Gavel, Y. and von Heijne, G. 1990. Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implications for protein engineering. Protein Eng. 3: 433-442.
    • (1990) Protein Eng. , vol.3 , pp. 433-442
    • Gavel, Y.1    Von Heijne, G.2
  • 11
    • 0141788026 scopus 로고    scopus 로고
    • Effect of carbohydrate moieties on the folate hydrolysis activity of the prostate specific membrane antigen
    • Ghosh, A. and Heston, W.D. 2003. Effect of carbohydrate moieties on the folate hydrolysis activity of the prostate specific membrane antigen. Prostate 57: 140-151.
    • (2003) Prostate , vol.57 , pp. 140-151
    • Ghosh, A.1    Heston, W.D.2
  • 12
    • 0026698693 scopus 로고
    • A method for determination of N-glycosylation sites in glycoproteins by collision-induced dissociation analysis in fast atom bombardment mass spectrometry: Identification of the positions of carbohydrate-linked asparagine in recombinant α-amylase by treatment with peptide-N-glycosidase F in 180-labeled water
    • Gonzalez, J., Takao, T., Hori, H., Besada, V., Rodriguez, R., Padron, G., and Shimonishi, Y. 1992. A method for determination of N-glycosylation sites in glycoproteins by collision-induced dissociation analysis in fast atom bombardment mass spectrometry: Identification of the positions of carbohydrate-linked asparagine in recombinant α-amylase by treatment with peptide-N-glycosidase F in 180-labeled water. Anal. Biochem. 205: 151-158.
    • (1992) Anal. Biochem. , vol.205 , pp. 151-158
    • Gonzalez, J.1    Takao, T.2    Hori, H.3    Besada, V.4    Rodriguez, R.5    Padron, G.6    Shimonishi, Y.7
  • 13
    • 0032211331 scopus 로고    scopus 로고
    • Identification, purification, and subcellular localization of prostate-specific membrane antigen PSM' protein in the LNCaP prostatic carcinoma cell line
    • Grauer, L.S., Lawler, K.D., Marignac, J.L., Kumar, A., Goel, A.S., and Wolfert, R.L. 1998. Identification, purification, and subcellular localization of prostate-specific membrane antigen PSM' protein in the LNCaP prostatic carcinoma cell line. Cancer Res. 58: 4787-4789.
    • (1998) Cancer Res. , vol.58 , pp. 4787-4789
    • Grauer, L.S.1    Lawler, K.D.2    Marignac, J.L.3    Kumar, A.4    Goel, A.S.5    Wolfert, R.L.6
  • 14
    • 0031933907 scopus 로고    scopus 로고
    • Prostate-specific membrane antigen: Current and future utility
    • Gregorakis, A.K., Holmes, E.H., and Murphy, G.P. 1998. Prostate-specific membrane antigen: Current and future utility. Semin. Urol. Oncol. 16: 2-12.
    • (1998) Semin. Urol. Oncol. , vol.16 , pp. 2-12
    • Gregorakis, A.K.1    Holmes, E.H.2    Murphy, G.P.3
  • 15
    • 0032493644 scopus 로고    scopus 로고
    • Folylpoly-gamma-glutamate carboxypeptidase from pig jejunum. Molecular characterization and relation to glutamate carboxypeptidase II
    • Halsted, C.H., Ling, E.H., Lutbi-Carter, R., Villanueva, J.A., Gardner, J.M., and Coyle, J.T. 1998. Folylpoly-gamma-glutamate carboxypeptidase from pig jejunum. Molecular characterization and relation to glutamate carboxypeptidase II. J. Biol. Chem. 273: 20417-20424.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20417-20424
    • Halsted, C.H.1    Ling, E.H.2    Lutbi-Carter, R.3    Villanueva, J.A.4    Gardner, J.M.5    Coyle, J.T.6
  • 16
    • 0033218504 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry of carbohydrates
    • Harvey, D.J. 1999. Matrix-assisted laser desorption/ionization mass spectrometry of carbohydrates. Mass Spectrom. Rev. 18: 349-450.
    • (1999) Mass Spectrom. Rev. , vol.18 , pp. 349-450
    • Harvey, D.J.1
  • 17
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • Helenius, A. and Aebi, M. 2001. Intracellular functions of N-linked glycans. Science 291: 2364-2369.
    • (2001) Science , vol.291 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 18
    • 0030341967 scopus 로고    scopus 로고
    • Analysis of glycosylation of prostate-specific membrane antigen derived from LNCaP cells, prostatic carcinoma tumors, and serum from prostate cancer patients
    • Holmes, E.H., Greene, T.G., Tino, W.T., Boynton, A.L., Aldape, H.C., Misrock, S.L., and Murphy, G.P. 1996. Analysis of glycosylation of prostate-specific membrane antigen derived from LNCaP cells, prostatic carcinoma tumors, and serum from prostate cancer patients. Prostate Suppl. 7: 25-29.
    • (1996) Prostate Suppl. , vol.7 , pp. 25-29
    • Holmes, E.H.1    Greene, T.G.2    Tino, W.T.3    Boynton, A.L.4    Aldape, H.C.5    Misrock, S.L.6    Murphy, G.P.7
  • 19
    • 0027500319 scopus 로고
    • Molecular cloning of a complementary DNA encoding a prostate-specific membrane antigen
    • Israeli, R.S., Powell, C.T., Fair, W.R., and Heston, W.D. 1993. Molecular cloning of a complementary DNA encoding a prostate-specific membrane antigen. Cancer Res. 53: 227-230.
    • (1993) Cancer Res. , vol.53 , pp. 227-230
    • Israeli, R.S.1    Powell, C.T.2    Fair, W.R.3    Heston, W.D.4
  • 20
    • 0034682814 scopus 로고    scopus 로고
    • N-Linked oligosaccharides on the meprin A metalloprotease are important for secretion and enzymatic activity, but not for apical targeting
    • Kadowaki, T., Tsukuba, T., Bertenshaw, G.P., and Bond, J.S. 2000. N-Linked oligosaccharides on the meprin A metalloprotease are important for secretion and enzymatic activity, but not for apical targeting. J. Biol. Chem. 275: 25577-25584.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25577-25584
    • Kadowaki, T.1    Tsukuba, T.2    Bertenshaw, G.P.3    Bond, J.S.4
  • 21
    • 0033674466 scopus 로고    scopus 로고
    • Prostate-specific membrane antigen (PSMA) enzyme activity is elevated in prostate cancer cells
    • Lapidus, R.G., Tiffany, C.W., Isaacs, J.T., and Slusher, B.S. 2000. Prostate-specific membrane antigen (PSMA) enzyme activity is elevated in prostate cancer cells [In Process Citation]. Prostate 45: 350-354.
    • (2000) Prostate , vol.45 , pp. 350-354
    • Lapidus, R.G.1    Tiffany, C.W.2    Isaacs, J.T.3    Slusher, B.S.4
  • 22
  • 23
    • 0031734879 scopus 로고    scopus 로고
    • A general approach to desalting oligosaccharides released from glycoproteins
    • Packer, N.H., Lawson, M.A., Jardine, D.R., and Redmond, J.W. 1998. A general approach to desalting oligosaccharides released from glycoproteins. Glycoconj. J. 15: 737-747.
    • (1998) Glycoconj. J. , vol.15 , pp. 737-747
    • Packer, N.H.1    Lawson, M.A.2    Jardine, D.R.3    Redmond, J.W.4
  • 24
    • 0030940306 scopus 로고    scopus 로고
    • Structure of membrane glutamate carboxypeptidase
    • Rawlings, N.D. and Barrett, A.J. 1997. Structure of membrane glutamate carboxypeptidase. Biochim. Biophys. Acta 1339: 247-252.
    • (1997) Biochim. Biophys. Acta , vol.1339 , pp. 247-252
    • Rawlings, N.D.1    Barrett, A.J.2
  • 25
    • 0023232412 scopus 로고
    • Hydrolysis of the brain dipeptide N-acetyl-L-aspartyl-L-glutamate. Identification and characterization of a novel N-acetylated α-linked acidic dipeptidase activity from rat brain
    • Robinson, M.B., Blakely, R.D., Couto, R., and Coyle, J.T. 1987. Hydrolysis of the brain dipeptide N-acetyl-L-aspartyl-L-glutamate. Identification and characterization of a novel N-acetylated α-linked acidic dipeptidase activity from rat brain. J. Biol. Chem. 262: 14498-14506.
    • (1987) J. Biol. Chem. , vol.262 , pp. 14498-14506
    • Robinson, M.B.1    Blakely, R.D.2    Couto, R.3    Coyle, J.T.4
  • 26
    • 0037068438 scopus 로고    scopus 로고
    • Molecular modeling of the interactions of glutamate carboxypeptidase II with its potent NAAG-based inhibitors
    • Rong, S.B., Zhang, J., Neale, J.H., Wroblewski, J.T., Wang, S., and Kozikowski, A.P. 2002. Molecular modeling of the interactions of glutamate carboxypeptidase II with its potent NAAG-based inhibitors. J. Med. Chem. 45: 4140-4152.
    • (2002) J. Med. Chem. , vol.45 , pp. 4140-4152
    • Rong, S.B.1    Zhang, J.2    Neale, J.H.3    Wroblewski, J.T.4    Wang, S.5    Kozikowski, A.P.6
  • 28
    • 0141857763 scopus 로고    scopus 로고
    • Expression of prostate specific membrane antigen and three alternatively spliced variants of PSMA in prostate cancer patients
    • Schmittgen, T.D., Teske, S., Vessella, R.L., True, L.D., and Zakrajsek, B.A. 2003. Expression of prostate specific membrane antigen and three alternatively spliced variants of PSMA in prostate cancer patients. Int. J. Cancer 107: 323-329.
    • (2003) Int. J. Cancer , vol.107 , pp. 323-329
    • Schmittgen, T.D.1    Teske, S.2    Vessella, R.L.3    True, L.D.4    Zakrajsek, B.A.5
  • 30
    • 0028933376 scopus 로고
    • Alter natively spliced variants of prostate-specific membrane antigen RNA: Ratio of expression as a potential measurement of progression
    • Su, S.L., Huang, I.P., Fair, W.R., Powell, C.T., and Heston, W.D. 1995. Alter natively spliced variants of prostate-specific membrane antigen RNA: Ratio of expression as a potential measurement of progression. Cancer Res. 55: 1441-1443.
    • (1995) Cancer Res. , vol.55 , pp. 1441-1443
    • Su, S.L.1    Huang, I.P.2    Fair, W.R.3    Powell, C.T.4    Heston, W.D.5
  • 31
    • 0033560036 scopus 로고    scopus 로고
    • Characterization of the enzymatic activity of PSM: Comparison with brain NAALADase
    • Tiffany, C.W., Lapidus, R.G., Merion, A., Calvin, D.C., and Slusher, B.S. 1999. Characterization of the enzymatic activity of PSM: Comparison with brain NAALADase. Prostate 39: 28-35.
    • (1999) Prostate , vol.39 , pp. 28-35
    • Tiffany, C.W.1    Lapidus, R.G.2    Merion, A.3    Calvin, D.C.4    Slusher, B.S.5
  • 32
    • 0016757289 scopus 로고
    • Tunicamycin inhibition of polyisoprenyl N-acetylglucosaminyl pyrophosphate formation in calf-liver microsomes
    • Tkacz, J.S. and Lampen, O. 1975. Tunicamycin inhibition of polyisoprenyl N-acetylglucosaminyl pyrophosphate formation in calf-liver microsomes. Biochem. Biophys. Res. Commun. 65: 248-257.
    • (1975) Biochem. Biophys. Res. Commun. , vol.65 , pp. 248-257
    • Tkacz, J.S.1    Lampen, O.2
  • 33
    • 0035808437 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis-linked glutamate transporter mutant has impaired glutamate clearance capacity
    • Trotti, D., Aoki, M., Pasinelli, P., Berger, U.V., Danbolt, N.C., Brown Jr., R.H., and Hediger, M.A. 2001. Amyotrophic lateral sclerosis-linked glutamate transporter mutant has impaired glutamate clearance capacity. J. Biol. Chem. 276: 576-582.
    • (2001) J. Biol. Chem. , vol.276 , pp. 576-582
    • Trotti, D.1    Aoki, M.2    Pasinelli, P.3    Berger, U.V.4    Danbolt, N.C.5    Brown Jr., R.H.6    Hediger, M.A.7
  • 34
    • 0036451229 scopus 로고    scopus 로고
    • Characterization of the lectin from females of Phlebotomus duboscqi sand flies
    • Volf, P., Skarupova, S., and Man, P. 2002. Characterization of the lectin from females of Phlebotomus duboscqi sand flies. Eur. J. Biochem. 269: 6294-6301.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 6294-6301
    • Volf, P.1    Skarupova, S.2    Man, P.3
  • 35
    • 0030881717 scopus 로고    scopus 로고
    • Quality control in the secretory pathway: The role of calreticulin, calnexin and BiP in the retention of glycoproteins with C-terminal truncations
    • Zhang, J.X., Braakman, I., Matlack, K.E., and Helenius, A. 1997. Quality control in the secretory pathway: The role of calreticulin, calnexin and BiP in the retention of glycoproteins with C-terminal truncations. Mol. Biol. Cell 8: 1943-1954.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1943-1954
    • Zhang, J.X.1    Braakman, I.2    Matlack, K.E.3    Helenius, A.4


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