메뉴 건너뛰기




Volumn 829, Issue , 2014, Pages 40-47

Analysis of the human urine endogenous peptides by nanoparticle extraction and mass spectrometry identification

Author keywords

Biomarker; Human urine; Nanoparticle; Peptidomics; Proteomics; Two dimensional

Indexed keywords

BIOMARKERS; EXTRACTION; MASS SPECTROMETRY; MOLECULAR BIOLOGY; MOLECULAR WEIGHT; NANOPARTICLES; PEPTIDES; TWO DIMENSIONAL;

EID: 84900990297     PISSN: 00032670     EISSN: 18734324     Source Type: Journal    
DOI: 10.1016/j.aca.2014.04.040     Document Type: Article
Times cited : (15)

References (57)
  • 4
    • 23944436422 scopus 로고    scopus 로고
    • Proteomics: from basic research to diagnostic application. A review of requirements and needs
    • Vitzthum F., Behrens F., Anderson N.L., Shaw J.H. Proteomics: from basic research to diagnostic application. A review of requirements and needs. Journal of Proteome Research 2005, 4:1086-1097.
    • (2005) Journal of Proteome Research , vol.4 , pp. 1086-1097
    • Vitzthum, F.1    Behrens, F.2    Anderson, N.L.3    Shaw, J.H.4
  • 5
    • 33749264369 scopus 로고    scopus 로고
    • Proteomic profiling of human urinary proteome using nano-high performance liquid chromatography/electrospray ionization tandem mass spectrometry
    • Tyan Y.C., Guo H.R., Liu C.Y., Liao P.C. Proteomic profiling of human urinary proteome using nano-high performance liquid chromatography/electrospray ionization tandem mass spectrometry. Analytica Chimica Acta 2006, 579:158-176.
    • (2006) Analytica Chimica Acta , vol.579 , pp. 158-176
    • Tyan, Y.C.1    Guo, H.R.2    Liu, C.Y.3    Liao, P.C.4
  • 7
    • 15944364115 scopus 로고    scopus 로고
    • Profiling of urinary proteins by nano-high performance liquid chromatography/tandem mass spectrometry
    • Hong S.S., Kwon S.W. Profiling of urinary proteins by nano-high performance liquid chromatography/tandem mass spectrometry. Journal of Liquid Chromatography & Related Technologies 2005, 28:805-822.
    • (2005) Journal of Liquid Chromatography & Related Technologies , vol.28 , pp. 805-822
    • Hong, S.S.1    Kwon, S.W.2
  • 8
    • 33745252024 scopus 로고    scopus 로고
    • Solid-phase extraction and elution on diamond (SPEED): a fast and general platform for proteome analysis with mass spectrometry
    • Chen W.H., Lee S.C., Sabu S., Fang H.C., Chung S.C., Han C.C., Chang H.C. Solid-phase extraction and elution on diamond (SPEED): a fast and general platform for proteome analysis with mass spectrometry. Analytical Chemistry 2006, 78:4228-4234.
    • (2006) Analytical Chemistry , vol.78 , pp. 4228-4234
    • Chen, W.H.1    Lee, S.C.2    Sabu, S.3    Fang, H.C.4    Chung, S.C.5    Han, C.C.6    Chang, H.C.7
  • 10
    • 30744440918 scopus 로고    scopus 로고
    • Systematic evaluation of sample preparation methods for gel-based human urinary proteomics: quantity, quality, and variability
    • Thongboonkerd V., Chutipongtanate S., Kanlaya R. Systematic evaluation of sample preparation methods for gel-based human urinary proteomics: quantity, quality, and variability. Journal of Proteome Research 2006, 5:183-191.
    • (2006) Journal of Proteome Research , vol.5 , pp. 183-191
    • Thongboonkerd, V.1    Chutipongtanate, S.2    Kanlaya, R.3
  • 12
    • 11144356366 scopus 로고    scopus 로고
    • Characterization of the human urinary proteome: a method for high-resolution display of urinary proteins on two-dimensional electrophoresis gels with a yield of nearly 1400 distinct protein spots
    • Pieper R., Gatlin C.L., McGrath A.M., Makusky A.J., Mondal M., Seonarain M., Field E., Schatz C.R., Estock M.A., Ahmed N., Anderson N.G., Steiner S. Characterization of the human urinary proteome: a method for high-resolution display of urinary proteins on two-dimensional electrophoresis gels with a yield of nearly 1400 distinct protein spots. Proteomics 2004, 4:1159-1174.
    • (2004) Proteomics , vol.4 , pp. 1159-1174
    • Pieper, R.1    Gatlin, C.L.2    McGrath, A.M.3    Makusky, A.J.4    Mondal, M.5    Seonarain, M.6    Field, E.7    Schatz, C.R.8    Estock, M.A.9    Ahmed, N.10    Anderson, N.G.11    Steiner, S.12
  • 13
    • 33750364830 scopus 로고    scopus 로고
    • The human urinary proteome contains more than 1500 proteins, including a large proportion of membrane proteins
    • R80
    • Adachi J., Kumar C., Zhang Y.L., Olsen J.V., Mann M. The human urinary proteome contains more than 1500 proteins, including a large proportion of membrane proteins. Genome Biology 2006, 7(9). R80.
    • (2006) Genome Biology , vol.7 , Issue.9
    • Adachi, J.1    Kumar, C.2    Zhang, Y.L.3    Olsen, J.V.4    Mann, M.5
  • 16
    • 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., Schulz-Knappe P. Peptidomic analysis of human blood specimens: comparison between plasma specimens and serum by differential peptide display. Proteomics 2005, 5:3414-3422.
    • (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    Schulz-Knappe, P.7
  • 19
    • 32944482784 scopus 로고    scopus 로고
    • Peptidomics: bridging the gap between proteome and metabolome
    • Soloviev M., Finch P. Peptidomics: bridging the gap between proteome and metabolome. Proteomics 2006, 6:744-747.
    • (2006) Proteomics , vol.6 , pp. 744-747
    • Soloviev, M.1    Finch, P.2
  • 21
    • 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., Hancock W.S. Analysis of the low molecular weight serum peptidome using ultrafiltration and a hybrid ion trap-Fourier transform mass spectrometer. Journal of Chromatography A 2006, 1120:173-184.
    • (2006) Journal of Chromatography A , vol.1120 , pp. 173-184
    • Zheng, X.Y.1    Baker, H.2    Hancock, W.S.3
  • 23
    • 33644843647 scopus 로고    scopus 로고
    • Biomarkers: taking out the trash
    • Novak K. Biomarkers: taking out the trash. Nature Reviews Cancer 2006, 6:92.
    • (2006) Nature Reviews Cancer , vol.6 , pp. 92
    • Novak, K.1
  • 24
    • 33845267469 scopus 로고    scopus 로고
    • The blood peptidome: a higher dimension of information content for cancer biomarker discovery
    • Petricoin E.F., Belluco C., Araujo R.P., Liotta L.A. The blood peptidome: a higher dimension of information content for cancer biomarker discovery. Nature Reviews Cancer 2006, 6:961-967.
    • (2006) Nature Reviews Cancer , vol.6 , pp. 961-967
    • Petricoin, E.F.1    Belluco, C.2    Araujo, R.P.3    Liotta, L.A.4
  • 25
    • 31044448275 scopus 로고    scopus 로고
    • Serum peptidome for cancer detection: spinning biologic trash into diagnostic gold
    • Liotta L.A., Petricoin E.F. Serum peptidome for cancer detection: spinning biologic trash into diagnostic gold. Journal of Clinical Investigation 2006, 116:26-30.
    • (2006) Journal of Clinical Investigation , vol.116 , pp. 26-30
    • Liotta, L.A.1    Petricoin, E.F.2
  • 30
    • 0030800989 scopus 로고    scopus 로고
    • Mapping of peptides and protein fragments in human urine using liquid chromatography mass spectrometry
    • Heine G., Raida M., Forssmann W.G. Mapping of peptides and protein fragments in human urine using liquid chromatography mass spectrometry. Journal of Chromatography A 1997, 776:117-124.
    • (1997) Journal of Chromatography A , vol.776 , pp. 117-124
    • Heine, G.1    Raida, M.2    Forssmann, W.G.3
  • 31
    • 0038355369 scopus 로고    scopus 로고
    • Detection and analysis of urinary peptides by on-line liquid chromatography and mass spectrometry: application to patients with renal Fanconi syndrome
    • Cutillas P.R., Norden A.G.W., Cramer R., Burlingame A.L., Unwin R.J. Detection and analysis of urinary peptides by on-line liquid chromatography and mass spectrometry: application to patients with renal Fanconi syndrome. Clinical Science 2003, 104:483-490.
    • (2003) Clinical Science , vol.104 , pp. 483-490
    • Cutillas, P.R.1    Norden, A.G.W.2    Cramer, R.3    Burlingame, A.L.4    Unwin, R.J.5
  • 32
    • 0034877096 scopus 로고    scopus 로고
    • Protein fragments in urine have been considerably underestimated by various protein assays
    • Greive K.A., Balazs N.D.H., Comper W.D. Protein fragments in urine have been considerably underestimated by various protein assays. Clinical Chemistry 2001, 47:1717-1719.
    • (2001) Clinical Chemistry , vol.47 , pp. 1717-1719
    • Greive, K.A.1    Balazs, N.D.H.2    Comper, W.D.3
  • 36
    • 0026931265 scopus 로고
    • Ordered mesoporous molecular-sieves synthesized by a liquid-crystal template mechanism
    • Kresge C.T., Leonowicz M.E., Roth W.J., Vartuli J.C., Beck J.S. Ordered mesoporous molecular-sieves synthesized by a liquid-crystal template mechanism. Nature 1992, 359:710-712.
    • (1992) Nature , vol.359 , pp. 710-712
    • Kresge, C.T.1    Leonowicz, M.E.2    Roth, W.J.3    Vartuli, J.C.4    Beck, J.S.5
  • 38
  • 41
    • 35448965232 scopus 로고    scopus 로고
    • Optimization of filtering criterion for SEQUEST database searching to improve proteome coverage in shotgun proteomics
    • Jiang X.N., Ye M.L., Zou H.F. Optimization of filtering criterion for SEQUEST database searching to improve proteome coverage in shotgun proteomics. BMC Bioinformatics 2007, 8(323):1-12.
    • (2007) BMC Bioinformatics , vol.8 , Issue.323 , pp. 1-12
    • Jiang, X.N.1    Ye, M.L.2    Zou, H.F.3
  • 42
    • 2442690211 scopus 로고    scopus 로고
    • Degradation of albumin by the renal proximal tubule cells and the subsequent fate of its fragments
    • Gudehithlu K.P., Pegoraro A.A., Dunea G., Arruda J.A.L., Singh A.K. Degradation of albumin by the renal proximal tubule cells and the subsequent fate of its fragments. Kidney International 2004, 65:2113-2122.
    • (2004) Kidney International , vol.65 , pp. 2113-2122
    • Gudehithlu, K.P.1    Pegoraro, A.A.2    Dunea, G.3    Arruda, J.A.L.4    Singh, A.K.5
  • 44
    • 16244419727 scopus 로고    scopus 로고
    • Proteomic-based identification of cleaved urinary beta 2-microglobulin as a potential marker for acute tubular injury in renal allografts
    • Schaub S., Wilkins J.A., Antonovici M., Krokhin O., Weiler T., Rush D., Nickerson P. Proteomic-based identification of cleaved urinary beta 2-microglobulin as a potential marker for acute tubular injury in renal allografts. American Journal of Transplantation 2005, 5:729-738.
    • (2005) American Journal of Transplantation , vol.5 , pp. 729-738
    • Schaub, S.1    Wilkins, J.A.2    Antonovici, M.3    Krokhin, O.4    Weiler, T.5    Rush, D.6    Nickerson, P.7
  • 45
    • 84901004353 scopus 로고
    • Research development of urinary trypsin inhibitor
    • Shu Z.S., Jiang Y.S. Research development of urinary trypsin inhibitor. World Clinical Drugs 1991, 12:203-205.
    • (1991) World Clinical Drugs , vol.12 , pp. 203-205
    • Shu, Z.S.1    Jiang, Y.S.2
  • 47
    • 34848857003 scopus 로고    scopus 로고
    • Selective extraction of peptides in acidic human plasma by porous silica nanoparticles for peptidome analysis with 2-D LC-MS/MS
    • Tian R.J., Ye M.L., Hu L.H., Li X., Zou H.F. Selective extraction of peptides in acidic human plasma by porous silica nanoparticles for peptidome analysis with 2-D LC-MS/MS. Journal of Separation Science 2007, 30:2204-2209.
    • (2007) Journal of Separation Science , vol.30 , pp. 2204-2209
    • Tian, R.J.1    Ye, M.L.2    Hu, L.H.3    Li, X.4    Zou, H.F.5
  • 48
    • 33847397401 scopus 로고    scopus 로고
    • Comprehensive peptidome analysis of mouse livers by size exclusion chromatography prefractionation and nanoLC-MS/MS identification
    • Hu L.H., Li X., Jiang X.N., Jiang X.G., Zhou H.J., Kong L., Ye M.L., Zou H.F. Comprehensive peptidome analysis of mouse livers by size exclusion chromatography prefractionation and nanoLC-MS/MS identification. Journal of Proteome Research 2007, 6:801-808.
    • (2007) Journal of Proteome Research , vol.6 , pp. 801-808
    • Hu, L.H.1    Li, X.2    Jiang, X.N.3    Jiang, X.G.4    Zhou, H.J.5    Kong, L.6    Ye, M.L.7    Zou, H.F.8
  • 49
    • 14744276328 scopus 로고    scopus 로고
    • Top-down identification of endogenous peptides up to 9kDa in cerebrospinal fluid and brain tissue by nanoelectrospray quadrupole time-of-flight tandem mass spectrometry
    • Mohring T., Kellmann M., Jurgens M., Schrader M. Top-down identification of endogenous peptides up to 9kDa in cerebrospinal fluid and brain tissue by nanoelectrospray quadrupole time-of-flight tandem mass spectrometry. Journal of Mass Spectrometry 2005, 40:214-226.
    • (2005) Journal of Mass Spectrometry , vol.40 , pp. 214-226
    • Mohring, T.1    Kellmann, M.2    Jurgens, M.3    Schrader, M.4
  • 50
    • 4644262588 scopus 로고    scopus 로고
    • A new and sensitive on-line liquid chromatography/mass spectrometric approach for top-down protein analysis: the comprehensive analysis of human growth hormone in an E. coli lysate using a hybrid linear ion trap/Fourier transform ion cyclotron resonance mass spectrometer
    • Wu S.L., Jardine I., Hancock W.S., Karger B.L. A new and sensitive on-line liquid chromatography/mass spectrometric approach for top-down protein analysis: the comprehensive analysis of human growth hormone in an E. coli lysate using a hybrid linear ion trap/Fourier transform ion cyclotron resonance mass spectrometer. Rapid Communications in Mass Spectrometry 2004, 18:2201-2207.
    • (2004) Rapid Communications in Mass Spectrometry , vol.18 , pp. 2201-2207
    • Wu, S.L.1    Jardine, I.2    Hancock, W.S.3    Karger, B.L.4
  • 52
    • 84875908330 scopus 로고    scopus 로고
    • Proteasix: a tool for automated and large-scale prediction of proteases involved in naturally occurring peptide generation
    • Klein J., Eales J., Zuerbig P., Vlahou A., Mischak H., Stevens R. Proteasix: a tool for automated and large-scale prediction of proteases involved in naturally occurring peptide generation. Proteomics 2013, 13:1077-1082.
    • (2013) Proteomics , vol.13 , pp. 1077-1082
    • Klein, J.1    Eales, J.2    Zuerbig, P.3    Vlahou, A.4    Mischak, H.5    Stevens, R.6
  • 53
    • 0033887931 scopus 로고    scopus 로고
    • Probable involvement of cathepsin D in the degradation of beta(2)-microglobulin in acidic urine
    • Yamamoto H., Yamada T., Itoh Y. Probable involvement of cathepsin D in the degradation of beta(2)-microglobulin in acidic urine. Clinical Chemistry and Laboratory Medicine 2000, 38:495-499.
    • (2000) Clinical Chemistry and Laboratory Medicine , vol.38 , pp. 495-499
    • Yamamoto, H.1    Yamada, T.2    Itoh, Y.3
  • 54
    • 0022413812 scopus 로고
    • Uromodulin: a unique 85-kilodalton immunosuppressive glycoprotein isolated from urine of pregnant women
    • Muchmore A.V., Decker J.M. Uromodulin: a unique 85-kilodalton immunosuppressive glycoprotein isolated from urine of pregnant women. Science 1985, 229:479-481.
    • (1985) Science , vol.229 , pp. 479-481
    • Muchmore, A.V.1    Decker, J.M.2
  • 57
    • 33845566919 scopus 로고    scopus 로고
    • Increase in dermcidin-derived peptides in sweat of patients with atopic eczema caused by a humorous video
    • Kimata H. Increase in dermcidin-derived peptides in sweat of patients with atopic eczema caused by a humorous video. Journal of Psychosomatic Research 2007, 62:57-79.
    • (2007) Journal of Psychosomatic Research , vol.62 , pp. 57-79
    • Kimata, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.