메뉴 건너뛰기




Volumn 73, Issue 6, 2010, Pages 1219-1229

Isotope labeled internal standards (ILIS) as a basis for quality control in clinical studies using plasma samples

Author keywords

Clinical proteomics; Heavy isotope labeled peptides; Human blood plasma; Mass spectrometry

Indexed keywords

AMINO ACID; SYNTHETIC PEPTIDE; ISOTOPE; PEPTIDE; PLASMA PROTEIN; PROTEOME;

EID: 77950516712     PISSN: 18743919     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jprot.2010.02.012     Document Type: Article
Times cited : (5)

References (42)
  • 1
    • 0001644020 scopus 로고    scopus 로고
    • The human plasma proteome - history, character, and diagnostic prospects
    • Anderson N.L., and Anderson N.G. The human plasma proteome - history, character, and diagnostic prospects. Mol Cell Proteomics 1 (2002) 845-867
    • (2002) Mol Cell Proteomics , vol.1 , pp. 845-867
    • Anderson, N.L.1    Anderson, N.G.2
  • 2
    • 23944492134 scopus 로고    scopus 로고
    • Overview of the HUPO plasma proteome project: results from the pilot phase with 35 collaborating laboratories and multiple analytical groups, generating a core dataset of 3020 proteins and a publicly-available database
    • Omenn G.S., States D.J., Adamski M., Blackwell T.W., Menon R., Hermjakob H., et al. Overview of the HUPO plasma proteome project: results from the pilot phase with 35 collaborating laboratories and multiple analytical groups, generating a core dataset of 3020 proteins and a publicly-available database. Proteomics 5 (2005) 3226-3245
    • (2005) Proteomics , vol.5 , pp. 3226-3245
    • Omenn, G.S.1    States, D.J.2    Adamski, M.3    Blackwell, T.W.4    Menon, R.5    Hermjakob, H.6
  • 3
    • 34948876373 scopus 로고    scopus 로고
    • Contribution of protein fractionation to depth of analysis of the serum and plasma proteomes
    • Faca V., Pitteri S.J., Newcomb L., Glukhova V., Phanstiel D., Krasnoselsky A., et al. Contribution of protein fractionation to depth of analysis of the serum and plasma proteomes. J Proteome Res 6 (2007) 3558-3565
    • (2007) J Proteome Res , vol.6 , pp. 3558-3565
    • Faca, V.1    Pitteri, S.J.2    Newcomb, L.3    Glukhova, V.4    Phanstiel, D.5    Krasnoselsky, A.6
  • 4
    • 39749141692 scopus 로고    scopus 로고
    • Application of proteomics in the discovery of candidate protein biomarkers in a diabetes autoantibody standardization program sample subset
    • Metz T.O., Qian W.J., Jacobs J.M., Gritsenko M.A., Moore R.J., Polpitiya A.D., et al. Application of proteomics in the discovery of candidate protein biomarkers in a diabetes autoantibody standardization program sample subset. J Proteome Res 7 (2008) 698-707
    • (2008) J Proteome Res , vol.7 , pp. 698-707
    • Metz, T.O.1    Qian, W.J.2    Jacobs, J.M.3    Gritsenko, M.A.4    Moore, R.J.5    Polpitiya, A.D.6
  • 5
    • 46749145331 scopus 로고    scopus 로고
    • Performance characteristics of an FT MS-based workflow for label-free differential MS analysis of human plasma: standards, reproducibility, targeted feature investigation, and application to a model of controlled myocardial infarction
    • Sutton J., Richmond T., Shi X., Athanas M., Ptak C., Gerszten R., et al. Performance characteristics of an FT MS-based workflow for label-free differential MS analysis of human plasma: standards, reproducibility, targeted feature investigation, and application to a model of controlled myocardial infarction. Proteom Clin Appl 2 (2008) 862-881
    • (2008) Proteom Clin Appl , vol.2 , pp. 862-881
    • Sutton, J.1    Richmond, T.2    Shi, X.3    Athanas, M.4    Ptak, C.5    Gerszten, R.6
  • 7
    • 55049086987 scopus 로고    scopus 로고
    • Use of an immunoaffinity-mass spectrometry-based approach for the quantification of protein biomarkers from serum samples of lung cancer patients
    • Nicol G.R., Han M., Kim J., Birse C.E., Brand E., Nguyen A., et al. Use of an immunoaffinity-mass spectrometry-based approach for the quantification of protein biomarkers from serum samples of lung cancer patients. Mol Cell Proteomics 7 (2008) 1974-1982
    • (2008) Mol Cell Proteomics , vol.7 , pp. 1974-1982
    • Nicol, G.R.1    Han, M.2    Kim, J.3    Birse, C.E.4    Brand, E.5    Nguyen, A.6
  • 8
    • 61849105469 scopus 로고    scopus 로고
    • Mass spectrometry based targeted protein quantification: methods and applications
    • Pan S., Aebersold R., Chen R., Rush J., Goodlett D.R., McIntosh M.W., et al. Mass spectrometry based targeted protein quantification: methods and applications. J Proteome Res 8 (2009) 787-797
    • (2009) J Proteome Res , vol.8 , pp. 787-797
    • Pan, S.1    Aebersold, R.2    Chen, R.3    Rush, J.4    Goodlett, D.R.5    McIntosh, M.W.6
  • 9
    • 33645721632 scopus 로고    scopus 로고
    • Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins
    • Anderson L., and Hunter C.L. Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins. Mol Cell Proteomics 5 (2006) 573-588
    • (2006) Mol Cell Proteomics , vol.5 , pp. 573-588
    • Anderson, L.1    Hunter, C.L.2
  • 10
    • 71049137289 scopus 로고    scopus 로고
    • Multiple reaction monitoring-based, multiplexed, absolute quantitation of 45 proteins in human plasma
    • Kuzyk M.A., Smith D., Yang J.C., Cross T.J., Jackson A.M., Hardie D.B., et al. Multiple reaction monitoring-based, multiplexed, absolute quantitation of 45 proteins in human plasma. Mol Cell Proteomics 8 (2009) 1860-1877
    • (2009) Mol Cell Proteomics , vol.8 , pp. 1860-1877
    • Kuzyk, M.A.1    Smith, D.2    Yang, J.C.3    Cross, T.J.4    Jackson, A.M.5    Hardie, D.B.6
  • 11
    • 41549158639 scopus 로고    scopus 로고
    • A sequence-specific exopeptidase activity test (SSEAT) for "functional" biomarker discovery
    • Villanueva J., Nazarian A., Lawlor K., Yi S.S., Robbins R.J., and Temps P. A sequence-specific exopeptidase activity test (SSEAT) for "functional" biomarker discovery. Mol Cell Proteomics 7 (2008) 509-518
    • (2008) Mol Cell Proteomics , vol.7 , pp. 509-518
    • Villanueva, J.1    Nazarian, A.2    Lawlor, K.3    Yi, S.S.4    Robbins, R.J.5    Temps, P.6
  • 12
    • 45549099293 scopus 로고    scopus 로고
    • Combined experimental and statistical strategy for mass spectrometry based serum protein profiling for diagnosis of breast cancer: a case-control study
    • Callesen A.K., Vach W., Jorgensen P.E., Cold S., Tan Q., Christensen R.D., et al. Combined experimental and statistical strategy for mass spectrometry based serum protein profiling for diagnosis of breast cancer: a case-control study. J Proteome Res 7 (2008) 1419-1426
    • (2008) J Proteome Res , vol.7 , pp. 1419-1426
    • Callesen, A.K.1    Vach, W.2    Jorgensen, P.E.3    Cold, S.4    Tan, Q.5    Christensen, R.D.6
  • 14
    • 34948905277 scopus 로고    scopus 로고
    • Comparative profiling of serum glycoproteome by sequential purification of glycoproteins and 2-nitrobenzenesulfenyl (NBS) stable isotope labeling: a new approach for the novel biomarker discovery for cancer
    • Ueda K., Katagiri T., Shimada T., Irie S., Sato T.A., Nakamura Y., et al. Comparative profiling of serum glycoproteome by sequential purification of glycoproteins and 2-nitrobenzenesulfenyl (NBS) stable isotope labeling: a new approach for the novel biomarker discovery for cancer. J Proteome Res 6 (2007) 3475-3483
    • (2007) J Proteome Res , vol.6 , pp. 3475-3483
    • Ueda, K.1    Katagiri, T.2    Shimada, T.3    Irie, S.4    Sato, T.A.5    Nakamura, Y.6
  • 15
    • 12444330378 scopus 로고    scopus 로고
    • Processing of serum proteins underlies the mass spectral fingerprinting of myocardial infarction
    • Marshall J., Kupchak P., Zhu W.M., Yantha J., Vrees T., Furesz S., et al. Processing of serum proteins underlies the mass spectral fingerprinting of myocardial infarction. J Proteome Res 2 (2003) 361-372
    • (2003) J Proteome Res , vol.2 , pp. 361-372
    • Marshall, J.1    Kupchak, P.2    Zhu, W.M.3    Yantha, J.4    Vrees, T.5    Furesz, S.6
  • 17
    • 33748294174 scopus 로고    scopus 로고
    • Peptidomics for cancer diagnosis: present and future
    • Diamandis E.P. Peptidomics for cancer diagnosis: present and future. J Proteome Res 5 (2006) 2079-2082
    • (2006) J Proteome Res , vol.5 , pp. 2079-2082
    • Diamandis, E.P.1
  • 18
    • 38749086467 scopus 로고    scopus 로고
    • Preanalytical influences in clinical proteomic studies: raising awareness of fundamental issues in sample banking
    • Banks R.E. Preanalytical influences in clinical proteomic studies: raising awareness of fundamental issues in sample banking. Clin Chem 54 (2008) 6-7
    • (2008) Clin Chem , vol.54 , pp. 6-7
    • Banks, R.E.1
  • 19
    • 38749151898 scopus 로고    scopus 로고
    • SELDI-TOF MS whole serum proteomic profiling with IMAC surface does not reliably detect prostate cancer
    • McLerran D., Grizzle W.E., Feng Z.D., Thompson I.M., Bigbee W.L., Cazares L.H., et al. SELDI-TOF MS whole serum proteomic profiling with IMAC surface does not reliably detect prostate cancer. Clin Chem 54 (2008) 53-60
    • (2008) Clin Chem , vol.54 , pp. 53-60
    • McLerran, D.1    Grizzle, W.E.2    Feng, Z.D.3    Thompson, I.M.4    Bigbee, W.L.5    Cazares, L.H.6
  • 20
    • 55049130238 scopus 로고    scopus 로고
    • Banking of biological fluids for studies of disease-associated protein biomarkers
    • Schrohl A.S., Wurtz S., Kohn E., Banks R.E., Nielsen H.J., Sweep F., et al. Banking of biological fluids for studies of disease-associated protein biomarkers. Mol Cell Proteomics 7 (2008) 2061-2066
    • (2008) Mol Cell Proteomics , vol.7 , pp. 2061-2066
    • Schrohl, A.S.1    Wurtz, S.2    Kohn, E.3    Banks, R.E.4    Nielsen, H.J.5    Sweep, F.6
  • 21
    • 23944520883 scopus 로고    scopus 로고
    • HUPO plasma proteome project specimen collection and handling: towards the standardization of parameters for plasma proteome samples
    • Rai A.J., Gelfand C.A., Haywood B.C., Warunek D.J., Yi J.Z., Schuchard M.D., et al. HUPO plasma proteome project specimen collection and handling: towards the standardization of parameters for plasma proteome samples. Proteomics 5 (2005) 3262-3277
    • (2005) Proteomics , vol.5 , pp. 3262-3277
    • Rai, A.J.1    Gelfand, C.A.2    Haywood, B.C.3    Warunek, D.J.4    Yi, J.Z.5    Schuchard, M.D.6
  • 22
    • 41849087888 scopus 로고    scopus 로고
    • The UK Biobank sample handling and storage validation studies
    • Peakman T.C., and Elliott P. The UK Biobank sample handling and storage validation studies. Int J Epidemiol 37 (2008) 2-6
    • (2008) Int J Epidemiol , vol.37 , pp. 2-6
    • Peakman, T.C.1    Elliott, P.2
  • 23
    • 28844442934 scopus 로고    scopus 로고
    • Prerequisites for peptidomic analysis of blood samples: I. Evaluation of blood specimen qualities and determination of technical performance characteristics
    • Tammen H., Schulte I., Hess R., Menzel C., Kellmann M., and Schulz-Knappe P. Prerequisites for peptidomic analysis of blood samples: I. Evaluation of blood specimen qualities and determination of technical performance characteristics. Comb Chem High T Scr 8 (2005) 725-733
    • (2005) Comb Chem High T Scr , vol.8 , pp. 725-733
    • Tammen, H.1    Schulte, I.2    Hess, R.3    Menzel, C.4    Kellmann, M.5    Schulz-Knappe, P.6
  • 24
    • 24144432109 scopus 로고    scopus 로고
    • Influences of blood sample processing on low-molecular-weight proteome identified by surface-enhanced laser desorption/ionization mass spectrometry
    • Banks R.E., Stanley A.J., Cairns D.A., Barrett J.H., Clarke P., Thompson D., et al. Influences of blood sample processing on low-molecular-weight proteome identified by surface-enhanced laser desorption/ionization mass spectrometry. Clin Chem 51 (2005) 1637-1649
    • (2005) Clin Chem , vol.51 , pp. 1637-1649
    • Banks, R.E.1    Stanley, A.J.2    Cairns, D.A.3    Barrett, J.H.4    Clarke, P.5    Thompson, D.6
  • 25
    • 14644426471 scopus 로고    scopus 로고
    • Plasma storage at - 80 degrees C does not protect matrix metalloproteinase-9 from degradation
    • Rouy D., Ernens I., Jeanty C., and Wagner D.R. Plasma storage at - 80 degrees C does not protect matrix metalloproteinase-9 from degradation. Anal Biochem 338 (2005) 294-298
    • (2005) Anal Biochem , vol.338 , pp. 294-298
    • Rouy, D.1    Ernens, I.2    Jeanty, C.3    Wagner, D.R.4
  • 26
    • 41849144111 scopus 로고    scopus 로고
    • The UK Biobank sample handling and storage protocol for the collection, processing and archiving of human blood and urine
    • Elliott P., Peakman T.C., and Biobank U.K. The UK Biobank sample handling and storage protocol for the collection, processing and archiving of human blood and urine. Int J Epidemiol 37 (2008) 234-244
    • (2008) Int J Epidemiol , vol.37 , pp. 234-244
    • Elliott, P.1    Peakman, T.C.2    Biobank, U.K.3
  • 27
    • 67649511917 scopus 로고    scopus 로고
    • Isotope dilution strategies for absolute quantitative proteomics
    • Brun V., Masselon C., Garin J., and Dupuis A. Isotope dilution strategies for absolute quantitative proteomics. J Proteomics 72 (2009) 740-749
    • (2009) J Proteomics , vol.72 , pp. 740-749
    • Brun, V.1    Masselon, C.2    Garin, J.3    Dupuis, A.4
  • 28
    • 61349174658 scopus 로고    scopus 로고
    • Intrinsic Peptidase Activity Causes a Sequential Multi-Step Reaction (SMSR) in digestion of human plasma peptides
    • Yi J.Z., Liu Z.X., Craft D., O'Mullan P., Ju G., and Gelfand C.A. Intrinsic Peptidase Activity Causes a Sequential Multi-Step Reaction (SMSR) in digestion of human plasma peptides. J Proteome Res 7 (2008) 5112-5118
    • (2008) J Proteome Res , vol.7 , pp. 5112-5118
    • Yi, J.Z.1    Liu, Z.X.2    Craft, D.3    O'Mullan, P.4    Ju, G.5    Gelfand, C.A.6
  • 29
    • 33745005452 scopus 로고    scopus 로고
    • Analysis of the low molecular weight serum peptidome using ultrafiltration and a hybrid ion trap-Fourier transform mass spectrometer
    • Zheng X.Y., Baker H., and Hancock W.S. Analysis of the low molecular weight serum peptidome using ultrafiltration and a hybrid ion trap-Fourier transform mass spectrometer. J Chromatogr A 1120 (2006) 173-184
    • (2006) J Chromatogr A , vol.1120 , pp. 173-184
    • Zheng, X.Y.1    Baker, H.2    Hancock, W.S.3
  • 30
    • 23944470664 scopus 로고    scopus 로고
    • Peptidomic analysis of human blood specimens: comparison between plasma specimens and serum by differential peptide display
    • Tammen H., Schulte L., Hess R., Menzel C., Kellmann M., Mohring T., et al. Peptidomic analysis of human blood specimens: comparison between plasma specimens and serum by differential peptide display. Proteomics 5 (2005) 3414-3422
    • (2005) Proteomics , vol.5 , pp. 3414-3422
    • Tammen, H.1    Schulte, L.2    Hess, R.3    Menzel, C.4    Kellmann, M.5    Mohring, T.6
  • 31
    • 20844448187 scopus 로고    scopus 로고
    • Direct tandem mass spectrometry reveals limitations in protein profiling experiments for plasma biomarker discovery
    • Koomen J.M., Li D.H., Xiao L.C., Liu T.C., Coombes K.R., Abbruzzese J., et al. Direct tandem mass spectrometry reveals limitations in protein profiling experiments for plasma biomarker discovery. J Proteome Res 4 (2005) 972-981
    • (2005) J Proteome Res , vol.4 , pp. 972-981
    • Koomen, J.M.1    Li, D.H.2    Xiao, L.C.3    Liu, T.C.4    Coombes, K.R.5    Abbruzzese, J.6
  • 32
    • 33847360986 scopus 로고    scopus 로고
    • Evaluation of endogenous plasma peptide extraction methods for mass spectrometric biomarker discovery
    • Aristoteli L.P., Molloy M.P., and Baker M.S. Evaluation of endogenous plasma peptide extraction methods for mass spectrometric biomarker discovery. J Proteome Res 6 (2007) 571-581
    • (2007) J Proteome Res , vol.6 , pp. 571-581
    • Aristoteli, L.P.1    Molloy, M.P.2    Baker, M.S.3
  • 33
    • 11144353532 scopus 로고    scopus 로고
    • Organic solvent extraction of proteins and peptides from serum as an effective sample preparation for detection and identification of biomarkers by mass spectrometry
    • Chertov O., Biragyn A., Kwak L.W., Simpson J.T., Boronina T., Hoang V.M., et al. Organic solvent extraction of proteins and peptides from serum as an effective sample preparation for detection and identification of biomarkers by mass spectrometry. Proteomics 4 (2004) 1195-1203
    • (2004) Proteomics , vol.4 , pp. 1195-1203
    • Chertov, O.1    Biragyn, A.2    Kwak, L.W.3    Simpson, J.T.4    Boronina, T.5    Hoang, V.M.6
  • 34
    • 33646746601 scopus 로고    scopus 로고
    • Enrichment of low molecular weight fraction of serum for MS analysis of peptides associated with hepatocellular carcinoma
    • Orvisky E., Drake S.K., Martin B.M., Abdel-Hamid M., Ressom H.W., Varghese R.S., et al. Enrichment of low molecular weight fraction of serum for MS analysis of peptides associated with hepatocellular carcinoma. Proteomics 6 (2006) 2895-2902
    • (2006) Proteomics , vol.6 , pp. 2895-2902
    • Orvisky, E.1    Drake, S.K.2    Martin, B.M.3    Abdel-Hamid, M.4    Ressom, H.W.5    Varghese, R.S.6
  • 35
    • 63049101911 scopus 로고    scopus 로고
    • Serum protein profiling by solid phase extraction and mass spectrometry: a future diagnostics tool?
    • Callesen A.K., Madsen J.S., Vach W., Kruse T.A., Mogensen O., and Jensen O.N. Serum protein profiling by solid phase extraction and mass spectrometry: a future diagnostics tool?. Proteomics 9 (2009) 1428-1441
    • (2009) Proteomics , vol.9 , pp. 1428-1441
    • Callesen, A.K.1    Madsen, J.S.2    Vach, W.3    Kruse, T.A.4    Mogensen, O.5    Jensen, O.N.6
  • 37
    • 0036745551 scopus 로고    scopus 로고
    • Graphite powder as an alternative or supplement to reversed-phase material for desalting and concentration of peptide mixtures prior to matrix-assisted laser desorption/ionization-mass spectrometry
    • Larsen M.R., Cordwell S.J., and Roepstorff P. Graphite powder as an alternative or supplement to reversed-phase material for desalting and concentration of peptide mixtures prior to matrix-assisted laser desorption/ionization-mass spectrometry. Proteomics 2 (2002) 1277-1287
    • (2002) Proteomics , vol.2 , pp. 1277-1287
    • Larsen, M.R.1    Cordwell, S.J.2    Roepstorff, P.3
  • 38
    • 1542617944 scopus 로고    scopus 로고
    • Serum peptide profiling by magnetic particle-assisted, automated sample processing and MALDI-TOF mass spectrometry
    • Villanueva J., Philip J., Entenberg D., Chaparro C.A., Tanwar M.K., Holland E.C., et al. Serum peptide profiling by magnetic particle-assisted, automated sample processing and MALDI-TOF mass spectrometry. Anal Chem 76 (2004) 1560-1570
    • (2004) Anal Chem , vol.76 , pp. 1560-1570
    • Villanueva, J.1    Philip, J.2    Entenberg, D.3    Chaparro, C.A.4    Tanwar, M.K.5    Holland, E.C.6
  • 40
    • 33744473319 scopus 로고    scopus 로고
    • Systematical evaluation of the effects of sample collection procedures on low-molecular-weight serum/plasma proteome profiling
    • Hsieh S.Y., Chen R.K., Pan Y.H., and Lee H.L. Systematical evaluation of the effects of sample collection procedures on low-molecular-weight serum/plasma proteome profiling. Proteomics 6 (2006) 3189-3198
    • (2006) Proteomics , vol.6 , pp. 3189-3198
    • Hsieh, S.Y.1    Chen, R.K.2    Pan, Y.H.3    Lee, H.L.4
  • 41
    • 34249315396 scopus 로고    scopus 로고
    • Inhibition of intrinsic proteolytic activities moderates preanalytical variability and instability of human plasma
    • Yi J.Z., Kim C., and Gelfand C.A. Inhibition of intrinsic proteolytic activities moderates preanalytical variability and instability of human plasma. J Proteome Res 6 (2007) 1768-1781
    • (2007) J Proteome Res , vol.6 , pp. 1768-1781
    • Yi, J.Z.1    Kim, C.2    Gelfand, C.A.3
  • 42
    • 46749127737 scopus 로고    scopus 로고
    • Influence of variations in sample handling on SELDI-TOF MS serum protein profiles for colorectal cancer
    • Engwegen J., Alberts M., Knol J.C., Jimenez C.R., Depla A., Tuynman H., et al. Influence of variations in sample handling on SELDI-TOF MS serum protein profiles for colorectal cancer. Proteom Clin Appl 2 (2008) 936-945
    • (2008) Proteom Clin Appl , vol.2 , pp. 936-945
    • Engwegen, J.1    Alberts, M.2    Knol, J.C.3    Jimenez, C.R.4    Depla, A.5    Tuynman, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.