메뉴 건너뛰기




Volumn 86, Issue , 2016, Pages 468-480

Development of glycan specific lectin based immunoassay for detection of prostate specific antigen

Author keywords

Biomarkers; Glycosylation; Lectin based immunoassay; Prostate cancer; Prostate specific antigen

Indexed keywords

CASEIN; GELATIN; GLYCAN; LECTIN; MONOCLONAL ANTIBODY; PROSTATE SPECIFIC ANTIGEN; PROTEINASE; POLYSACCHARIDE;

EID: 84956914930     PISSN: 01418130     EISSN: 18790003     Source Type: Journal    
DOI: 10.1016/j.ijbiomac.2016.01.110     Document Type: Article
Times cited : (17)

References (46)
  • 1
    • 77952299239 scopus 로고    scopus 로고
    • α1,2-Fucosylated and β-N-acetylgalactosaminylated prostate-specific antigen as an efficient marker of prostatic cancer
    • Fukushima K., Satoh T., Baba S., Yamashita K. α1,2-Fucosylated and β-N-acetylgalactosaminylated prostate-specific antigen as an efficient marker of prostatic cancer. Glycobiology 2010, 20:452-460.
    • (2010) Glycobiology , vol.20 , pp. 452-460
    • Fukushima, K.1    Satoh, T.2    Baba, S.3    Yamashita, K.4
  • 2
    • 0028840275 scopus 로고
    • Free and complexed prostate-specific antigen (PSA): in vitro stability, epitope map, and development of immunofluorometric assays for specific and sensitive detection of free PSA and PSA-alpha 1-antichymotrypsin complex
    • Pettersson K., Piironen T., Seppälä M., Liukkonen L., Christensson A., Matikainen M.T., Suonpää M., Lövgren T., Lilja H. Free and complexed prostate-specific antigen (PSA): in vitro stability, epitope map, and development of immunofluorometric assays for specific and sensitive detection of free PSA and PSA-alpha 1-antichymotrypsin complex. Clin. Chem. 1995, 41:1480-1488.
    • (1995) Clin. Chem. , vol.41 , pp. 1480-1488
    • Pettersson, K.1    Piironen, T.2    Seppälä, M.3    Liukkonen, L.4    Christensson, A.5    Matikainen, M.T.6    Suonpää, M.7    Lövgren, T.8    Lilja, H.9
  • 3
    • 0028865871 scopus 로고
    • Molecular mass and carbohydrate structure of prostate specific antigen: studies for establishment of an international PSA standard
    • Bélanger A., van Halbeek H., Graves H.C., Grandbois K., Stamey T.A., Huang L., Poppe I., Labrie F. Molecular mass and carbohydrate structure of prostate specific antigen: studies for establishment of an international PSA standard. Prostate 1995, 27:187-197.
    • (1995) Prostate , vol.27 , pp. 187-197
    • Bélanger, A.1    van Halbeek, H.2    Graves, H.C.3    Grandbois, K.4    Stamey, T.A.5    Huang, L.6    Poppe, I.7    Labrie, F.8
  • 4
    • 0038618896 scopus 로고    scopus 로고
    • Altered glycosylation pattern allows the distinction between prostate-specific antigen (PSA) from normal and tumor origins
    • Peracaula R., Tabarés G., Royle L., Harvey D.J., Dwek R.A., Rudd P.M., Llorens de R. Altered glycosylation pattern allows the distinction between prostate-specific antigen (PSA) from normal and tumor origins. Glycobiology 2003, 13:457-470.
    • (2003) Glycobiology , vol.13 , pp. 457-470
    • Peracaula, R.1    Tabarés, G.2    Royle, L.3    Harvey, D.J.4    Dwek, R.A.5    Rudd, P.M.6    Llorens, D.R.7
  • 5
    • 0030822246 scopus 로고    scopus 로고
    • Isolation and characterization of free form prostate specific antigen (f-PSA) in sera of men with prostate cancer
    • Noldus J., Chen Z., Stamey T.A. Isolation and characterization of free form prostate specific antigen (f-PSA) in sera of men with prostate cancer. J. Urol. 1997, 158:1606-1609.
    • (1997) J. Urol. , vol.158 , pp. 1606-1609
    • Noldus, J.1    Chen, Z.2    Stamey, T.A.3
  • 6
    • 0031815518 scopus 로고    scopus 로고
    • Free-to-total prostate-specific antigen (PSA) ratio improves the specificity for detecting prostate cancer in patients with prostatism and intermediate PSA levels
    • Recker F., Kwiatkowski M.K., Piironen T., Pettersson K., Goepe M., Tscholl R. Free-to-total prostate-specific antigen (PSA) ratio improves the specificity for detecting prostate cancer in patients with prostatism and intermediate PSA levels. Br. J. Urol. 1998, 81:532-538.
    • (1998) Br. J. Urol. , vol.81 , pp. 532-538
    • Recker, F.1    Kwiatkowski, M.K.2    Piironen, T.3    Pettersson, K.4    Goepe, M.5    Tscholl, R.6
  • 7
    • 4444231395 scopus 로고    scopus 로고
    • Carbohydrate structure and differential binding of prostate specific antigen to Maackia amurensis lectin between prostate cancer and benign prostate hypertrophy
    • Ohyama C., Hosono M., Nitta K., Oh-eda M., Yoshikawa K., Habuchi T., Arai Y., Fukuda M. Carbohydrate structure and differential binding of prostate specific antigen to Maackia amurensis lectin between prostate cancer and benign prostate hypertrophy. Glycobiology 2004, 14:671-679.
    • (2004) Glycobiology , vol.14 , pp. 671-679
    • Ohyama, C.1    Hosono, M.2    Nitta, K.3    Oh-eda, M.4    Yoshikawa, K.5    Habuchi, T.6    Arai, Y.7    Fukuda, M.8
  • 8
    • 37549016762 scopus 로고    scopus 로고
    • Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma: a glycopeptide approach
    • Tajiri M., Ohyama C., Wada Y. Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma: a glycopeptide approach. Glycobiology 2008, 18:2-8.
    • (2008) Glycobiology , vol.18 , pp. 2-8
    • Tajiri, M.1    Ohyama, C.2    Wada, Y.3
  • 9
    • 84956900256 scopus 로고    scopus 로고
    • Quantification of prostate cancer-associated aberrant glycosylation of prostate-specific antigen
    • Springer, Japan, T. Endo, P.H. Seeberger, G.W. Hart, C. Wong, N. Taniguchi (Eds.)
    • Ohyama C., Koie T., Yoneyama T., Tobisawa Y. Quantification of prostate cancer-associated aberrant glycosylation of prostate-specific antigen. Glycoscience: Biology and Medicine 2014, 1-6. Springer, Japan. T. Endo, P.H. Seeberger, G.W. Hart, C. Wong, N. Taniguchi (Eds.).
    • (2014) Glycoscience: Biology and Medicine , pp. 1-6
    • Ohyama, C.1    Koie, T.2    Yoneyama, T.3    Tobisawa, Y.4
  • 10
    • 41149166182 scopus 로고    scopus 로고
    • Prostate-specific antigen and prostate cancer: prediction, detection and monitoring
    • Lilja H., Ulmert D., Vickers A.J. Prostate-specific antigen and prostate cancer: prediction, detection and monitoring. Nat. Rev. Cancer 2008, 8:268-278.
    • (2008) Nat. Rev. Cancer , vol.8 , pp. 268-278
    • Lilja, H.1    Ulmert, D.2    Vickers, A.J.3
  • 12
    • 79960746535 scopus 로고    scopus 로고
    • CE methods for analysis of isoforms of prostate-specific antigen compatible with online derivatization for LIF detection
    • Garrido-Medina R., Díez-Masa J.C., Frutos de M. CE methods for analysis of isoforms of prostate-specific antigen compatible with online derivatization for LIF detection. Electrophoresis 2011, 32:2036-2043.
    • (2011) Electrophoresis , vol.32 , pp. 2036-2043
    • Garrido-Medina, R.1    Díez-Masa, J.C.2    Frutos, D.M.3
  • 13
    • 0020082066 scopus 로고
    • A simplified purification procedure for human prostate antigen
    • Wang M.C., Valenzuela L.A., Murphy G.P., Chu T.M. A simplified purification procedure for human prostate antigen. Oncology 1982, 39:1-5.
    • (1982) Oncology , vol.39 , pp. 1-5
    • Wang, M.C.1    Valenzuela, L.A.2    Murphy, G.P.3    Chu, T.M.4
  • 14
    • 0033952926 scopus 로고    scopus 로고
    • Molecular forms of prostate-specific antigen in malignant and benign prostatic tissue: biochemical and diagnostic implications
    • Jung K., Brux B., Lein M., Rudolph B., Kristiansen G., Hauptmann S., Schnorr D., Loening S.A., Sinha P. Molecular forms of prostate-specific antigen in malignant and benign prostatic tissue: biochemical and diagnostic implications. Clin. Chem. 2000, 46:47-54.
    • (2000) Clin. Chem. , vol.46 , pp. 47-54
    • Jung, K.1    Brux, B.2    Lein, M.3    Rudolph, B.4    Kristiansen, G.5    Hauptmann, S.6    Schnorr, D.7    Loening, S.A.8    Sinha, P.9
  • 16
    • 77954087867 scopus 로고    scopus 로고
    • Cell viability and PSA secretion assays in LNCaP cells: a tiered in vitro approach to screen chemicals with a prostate-mediated effect on male reproduction within the ReProTect project
    • Lorenzetti S., Marcoccia D., Narciso L., Mantovani A. Cell viability and PSA secretion assays in LNCaP cells: a tiered in vitro approach to screen chemicals with a prostate-mediated effect on male reproduction within the ReProTect project. Reprod. Toxicol. 2010, 30:25-35.
    • (2010) Reprod. Toxicol. , vol.30 , pp. 25-35
    • Lorenzetti, S.1    Marcoccia, D.2    Narciso, L.3    Mantovani, A.4
  • 17
    • 33745290404 scopus 로고    scopus 로고
    • Fast and novel purification method to obtain the prostate specific antigen (PSA) from human seminal plasma
    • Acevedo B., Perera Y., Torres E., Pentón D., Ayala M., Gavilondo J. Fast and novel purification method to obtain the prostate specific antigen (PSA) from human seminal plasma. Prostate 2006, 66:1029-1036.
    • (2006) Prostate , vol.66 , pp. 1029-1036
    • Acevedo, B.1    Perera, Y.2    Torres, E.3    Pentón, D.4    Ayala, M.5    Gavilondo, J.6
  • 18
    • 84898902599 scopus 로고    scopus 로고
    • Immunoaffinity chromatographic isolation of prostate-specific antigen from seminal plasma for capillary electrophoresis analysis of its isoforms
    • Garrido-Medina R., Farina-Gomez N., Diez-Masa J.C., Frutos de M. Immunoaffinity chromatographic isolation of prostate-specific antigen from seminal plasma for capillary electrophoresis analysis of its isoforms. Anal. Chim. Acta 2014, 820:47-55.
    • (2014) Anal. Chim. Acta , vol.820 , pp. 47-55
    • Garrido-Medina, R.1    Farina-Gomez, N.2    Diez-Masa, J.C.3    Frutos, D.M.4
  • 19
    • 0022239505 scopus 로고
    • The predominant protein in human seminal coagulate
    • Lilja H., Laurell C.B. The predominant protein in human seminal coagulate. Scand. J. Clin. Lab. Invest. 1985, 45:635-641.
    • (1985) Scand. J. Clin. Lab. Invest. , vol.45 , pp. 635-641
    • Lilja, H.1    Laurell, C.B.2
  • 21
    • 0025350689 scopus 로고
    • Increased monoclonal antibody ascites production in mice primed with Freund's incomplete adjuvant
    • Jones S.L., Cox J.C., Pearson J.E. Increased monoclonal antibody ascites production in mice primed with Freund's incomplete adjuvant. J. Immunol. Methods 1990, 129:227-231.
    • (1990) J. Immunol. Methods , vol.129 , pp. 227-231
    • Jones, S.L.1    Cox, J.C.2    Pearson, J.E.3
  • 22
    • 0020559474 scopus 로고
    • The effect of pre-injection of mice with pristane on ascites tumour formation and monoclonal antibody production
    • Hoogenraad N., Helman T., Hoogenraad J. The effect of pre-injection of mice with pristane on ascites tumour formation and monoclonal antibody production. J. Immunol. Methods 1983, 61:317-320.
    • (1983) J. Immunol. Methods , vol.61 , pp. 317-320
    • Hoogenraad, N.1    Helman, T.2    Hoogenraad, J.3
  • 23
    • 0022600453 scopus 로고
    • Monoclonal antibody production by hybridoma growth in Freund's adjuvant primed mice
    • Mueller U.W., Hawes C.S., Jones W.R. Monoclonal antibody production by hybridoma growth in Freund's adjuvant primed mice. J. Immunol. Methods 1986, 87:193-196.
    • (1986) J. Immunol. Methods , vol.87 , pp. 193-196
    • Mueller, U.W.1    Hawes, C.S.2    Jones, W.R.3
  • 24
    • 33847660116 scopus 로고    scopus 로고
    • Protein A chromatography for antibody purification
    • Hober S., Nord K., Linhult M. Protein A chromatography for antibody purification. J. Chromatogr. B 2007, 848:40-47.
    • (2007) J. Chromatogr. B , vol.848 , pp. 40-47
    • Hober, S.1    Nord, K.2    Linhult, M.3
  • 25
    • 77449156540 scopus 로고    scopus 로고
    • Antibody purification: affinity chromatography-protein A and protein G Sepharose
    • Grodzki A.C., Berenstein E. Antibody purification: affinity chromatography-protein A and protein G Sepharose. Methods Mol. Biol. 2010, 588:33-41.
    • (2010) Methods Mol. Biol. , vol.588 , pp. 33-41
    • Grodzki, A.C.1    Berenstein, E.2
  • 27
    • 0037083495 scopus 로고    scopus 로고
    • Thiophilic interaction chromatography facilitates detection of various molecular complexes of prostate-specific antigen in biological fluids
    • Kawinski E., Levine E., Chadha K. Thiophilic interaction chromatography facilitates detection of various molecular complexes of prostate-specific antigen in biological fluids. Prostate 2002, 50:145-153.
    • (2002) Prostate , vol.50 , pp. 145-153
    • Kawinski, E.1    Levine, E.2    Chadha, K.3
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 84867688308 scopus 로고    scopus 로고
    • A protocol for stripping and reprobing of Western blots originally developed with colorimetric substrate TMB
    • Kar P., Agnihotri S.K., Sharma A., Sachan R., Bhatt M.L., Sachdev M. A protocol for stripping and reprobing of Western blots originally developed with colorimetric substrate TMB. Electrophoresis 2012, 33:3062-3065.
    • (2012) Electrophoresis , vol.33 , pp. 3062-3065
    • Kar, P.1    Agnihotri, S.K.2    Sharma, A.3    Sachan, R.4    Bhatt, M.L.5    Sachdev, M.6
  • 31
    • 0018854046 scopus 로고
    • Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulphate and copolymerized substrates
    • Heussen C., Dowdle E.B. Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulphate and copolymerized substrates. Anal. Biochem. 1980, 102:196-202.
    • (1980) Anal. Biochem. , vol.102 , pp. 196-202
    • Heussen, C.1    Dowdle, E.B.2
  • 32
    • 0026706930 scopus 로고
    • Weighing naked proteins: practical, high-accuracy mass measurement of peptides and proteins
    • Chait B.T., Kent S.B.H. Weighing naked proteins: practical, high-accuracy mass measurement of peptides and proteins. Science 1992, 257:1885-1894.
    • (1992) Science , vol.257 , pp. 1885-1894
    • Chait, B.T.1    Kent, S.B.H.2
  • 34
    • 59749089917 scopus 로고    scopus 로고
    • Comparative analysis of oligosaccharide specificities of fucose-specific lectins from Aspergillus oryzae and Aleuria aurantia using frontal affinity chromatography
    • Matsumura K., Higashida K., Hata Y., Kominami J., Nakamura-Tsuruta S., Hirabayashi J. Comparative analysis of oligosaccharide specificities of fucose-specific lectins from Aspergillus oryzae and Aleuria aurantia using frontal affinity chromatography. Anal. Biochem. 2009, 386:217-221.
    • (2009) Anal. Biochem. , vol.386 , pp. 217-221
    • Matsumura, K.1    Higashida, K.2    Hata, Y.3    Kominami, J.4    Nakamura-Tsuruta, S.5    Hirabayashi, J.6
  • 36
    • 0026020575 scopus 로고
    • Characterization of the carbohydrate binding specificity of the leukoagglutinating lectin from Maackia amurensis. Comparison with other sialic acid-specific lectins
    • Knibbs R.N., Goldstein I.J., Ratcliffe R.M., Shibuya N. Characterization of the carbohydrate binding specificity of the leukoagglutinating lectin from Maackia amurensis. Comparison with other sialic acid-specific lectins. J. Biol. Chem. 1991, 266:83-88.
    • (1991) J. Biol. Chem. , vol.266 , pp. 83-88
    • Knibbs, R.N.1    Goldstein, I.J.2    Ratcliffe, R.M.3    Shibuya, N.4
  • 37
    • 79960223187 scopus 로고    scopus 로고
    • Effective glycoanalysis with Maackia amurensis lectins requires a clear understanding of their binding specificities
    • Christoph G., Donald L.J. Effective glycoanalysis with Maackia amurensis lectins requires a clear understanding of their binding specificities. Glycobiology 2011, 21:988-993.
    • (2011) Glycobiology , vol.21 , pp. 988-993
    • Christoph, G.1    Donald, L.J.2
  • 39
    • 0030990262 scopus 로고    scopus 로고
    • Prostate specific antigen in benign prostatic hyperplasia: purification and characterization
    • Chen Z., Chen H., Stamey T.A. Prostate specific antigen in benign prostatic hyperplasia: purification and characterization. J. Urol. 1997, 157:2166-2170.
    • (1997) J. Urol. , vol.157 , pp. 2166-2170
    • Chen, Z.1    Chen, H.2    Stamey, T.A.3
  • 40
    • 0030728733 scopus 로고    scopus 로고
    • Specific and efficient peptide substrates for assaying the proteolytic activity of prostate-specific antigen
    • Denmeade S.R., Lou W., Lovgren J., Malm J., Lilja H., Isaacs J.T. Specific and efficient peptide substrates for assaying the proteolytic activity of prostate-specific antigen. Cancer Res. 1997, 57:4924-4930.
    • (1997) Cancer Res. , vol.57 , pp. 4924-4930
    • Denmeade, S.R.1    Lou, W.2    Lovgren, J.3    Malm, J.4    Lilja, H.5    Isaacs, J.T.6
  • 41
    • 0030070722 scopus 로고    scopus 로고
    • Complex formation between PSA isoenzymes and protease inhibitors
    • Leinonen J., Zhang W.M., Stenman U.H. Complex formation between PSA isoenzymes and protease inhibitors. J. Urol. 1996, 155:1099-1103.
    • (1996) J. Urol. , vol.155 , pp. 1099-1103
    • Leinonen, J.1    Zhang, W.M.2    Stenman, U.H.3
  • 42
    • 0037218414 scopus 로고    scopus 로고
    • Inhibition of the enzymatic activity of prostate-specific antigen by boric acid and 3-nitrophenyl boronic acid
    • Gallardo-Williams M.T., Maronpot R.R., Wine R.N., Brunssen S.H., Chapin R.E. Inhibition of the enzymatic activity of prostate-specific antigen by boric acid and 3-nitrophenyl boronic acid. Prostate 2003, 54:44-49.
    • (2003) Prostate , vol.54 , pp. 44-49
    • Gallardo-Williams, M.T.1    Maronpot, R.R.2    Wine, R.N.3    Brunssen, S.H.4    Chapin, R.E.5
  • 43
    • 77950518665 scopus 로고    scopus 로고
    • Identification of prostate specific antigen (psa) isoforms in complex biological samples utilizing complementary platforms
    • Végvári A., Rezeli M., Welinder C., Malm J., Lilja H., Marko-Varga G., Laurell T. Identification of prostate specific antigen (psa) isoforms in complex biological samples utilizing complementary platforms. J. Proteom. 2010, 73:1137-1147.
    • (2010) J. Proteom. , vol.73 , pp. 1137-1147
    • Végvári, A.1    Rezeli, M.2    Welinder, C.3    Malm, J.4    Lilja, H.5    Marko-Varga, G.6    Laurell, T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.