메뉴 건너뛰기




Volumn 134, Issue , 2016, Pages 193-202

Homogenization of tissues via picosecond-infrared laser (PIRL) ablation: Giving a closer view on the in-vivo composition of protein species as compared to mechanical homogenization

Author keywords

Mass spectrometry; PIRL DIVE; Protein species; Proteolysis; Tissue homogenization

Indexed keywords

ANIMAL TISSUE; ARTICLE; DESORPTION BY IMPULSIVE VIBRATIONAL EXCITATION; HISTOLOGY; HUMAN; HUMAN TISSUE; IMAGE ANALYSIS; LASER; NONHUMAN; PANCREAS; PICOSECOND INFRARED LASER; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN PROCESSING; RAT; TISSUE HOMOGENATE; TONSIL; TWO DIMENSIONAL GEL ELECTROPHORESIS; VAPORIZATION; ANIMAL; CHEMISTRY; DEVICES; INFRARED RADIATION; MOUSE; PALATINE TONSIL; PROCEDURES; PROTEOMICS; SPECIMEN HANDLING; WISTAR RAT;

EID: 84958169667     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2015.12.029     Document Type: Article
Times cited : (37)

References (38)
  • 1
    • 84864000455 scopus 로고    scopus 로고
    • Small changes huge impact: the role of protein posttranslational modifications in cellular homeostasis and disease
    • Karve T.M., Cheema A.K. Small changes huge impact: the role of protein posttranslational modifications in cellular homeostasis and disease. J. Amino Acids 2011, 2011:207691.
    • (2011) J. Amino Acids , vol.2011 , pp. 207691
    • Karve, T.M.1    Cheema, A.K.2
  • 2
    • 84859265031 scopus 로고    scopus 로고
    • Amino acids: chemistry, functionality and selected non-enzymatic post-translational modifications
    • Bischoff R., Schluter H. Amino acids: chemistry, functionality and selected non-enzymatic post-translational modifications. J. Proteome 2012, 75:2275-2296.
    • (2012) J. Proteome , vol.75 , pp. 2275-2296
    • Bischoff, R.1    Schluter, H.2
  • 3
    • 84893781709 scopus 로고    scopus 로고
    • Protein post-translational modifications and regulation of pluripotency in human stem cells
    • Wang Y.C., Peterson S.E., Loring J.F. Protein post-translational modifications and regulation of pluripotency in human stem cells. Cell Res. 2014, 24:143-160.
    • (2014) Cell Res. , vol.24 , pp. 143-160
    • Wang, Y.C.1    Peterson, S.E.2    Loring, J.F.3
  • 5
    • 78650178328 scopus 로고    scopus 로고
    • Reactive oxygen and nitrogen species induce protein and DNA modifications driving arthrofibrosis following total knee arthroplasty
    • Freeman T.A., Parvizi J., Della Valle C.J., Steinbeck M.J. Reactive oxygen and nitrogen species induce protein and DNA modifications driving arthrofibrosis following total knee arthroplasty. Fibrogenesis Tissue Repair 2009, 2:5.
    • (2009) Fibrogenesis Tissue Repair , vol.2 , pp. 5
    • Freeman, T.A.1    Parvizi, J.2    Della Valle, C.J.3    Steinbeck, M.J.4
  • 7
    • 77955455232 scopus 로고    scopus 로고
    • Proteomic identification of carbonylated proteins and their oxidation sites
    • Madian A.G., Regnier F.E. Proteomic identification of carbonylated proteins and their oxidation sites. J. Proteome Res. 2010, 9:3766-3780.
    • (2010) J. Proteome Res. , vol.9 , pp. 3766-3780
    • Madian, A.G.1    Regnier, F.E.2
  • 10
    • 84887063785 scopus 로고    scopus 로고
    • Back to the future-the value of single protein species investigations
    • Jungblut P.R. Back to the future-the value of single protein species investigations. Proteomics 2013, 13:3103-3105.
    • (2013) Proteomics , vol.13 , pp. 3103-3105
    • Jungblut, P.R.1
  • 12
    • 34248598796 scopus 로고    scopus 로고
    • Trends in sample preparation for classical and second generation proteomics
    • Canas B., Pineiro C., Calvo E., Lopez-Ferrer D., Gallardo J.M. Trends in sample preparation for classical and second generation proteomics. J. Chromatogr. A 2007, 1153:235-258.
    • (2007) J. Chromatogr. A , vol.1153 , pp. 235-258
    • Canas, B.1    Pineiro, C.2    Calvo, E.3    Lopez-Ferrer, D.4    Gallardo, J.M.5
  • 13
    • 78549284015 scopus 로고    scopus 로고
    • Clinical application for the preservation of phospho-proteins through in-situ tissue stabilization
    • Rountree C.B., Van Kirk C.A., You H., Ding W., Dang H., VanGuilder H.D., et al. Clinical application for the preservation of phospho-proteins through in-situ tissue stabilization. Proteome Sci. 2010, 8:61.
    • (2010) Proteome Sci. , vol.8 , pp. 61
    • Rountree, C.B.1    Van Kirk, C.A.2    You, H.3    Ding, W.4    Dang, H.5    VanGuilder, H.D.6
  • 14
    • 79953032976 scopus 로고    scopus 로고
    • Neuropeptide profiling of the bovine hypothalamus: thermal stabilization is an effective tool in inhibiting post-mortem degradation
    • Colgrave M.L., Xi L., Lehnert S.A., Flatscher-Bader T., Wadensten H., Nilsson A., et al. Neuropeptide profiling of the bovine hypothalamus: thermal stabilization is an effective tool in inhibiting post-mortem degradation. Proteomics 2011, 11:1264-1276.
    • (2011) Proteomics , vol.11 , pp. 1264-1276
    • Colgrave, M.L.1    Xi, L.2    Lehnert, S.A.3    Flatscher-Bader, T.4    Wadensten, H.5    Nilsson, A.6
  • 15
    • 84902106529 scopus 로고    scopus 로고
    • Uncovering effects of ex vivo protease activity during proteomics and peptidomics sample extraction in rat brain tissue by oxygen-18 labeling
    • Stingl C., Soderquist M., Karlsson O., Boren M., Luider T.M. Uncovering effects of ex vivo protease activity during proteomics and peptidomics sample extraction in rat brain tissue by oxygen-18 labeling. J. Proteome Res. 2014, 13:2807-2817.
    • (2014) J. Proteome Res. , vol.13 , pp. 2807-2817
    • Stingl, C.1    Soderquist, M.2    Karlsson, O.3    Boren, M.4    Luider, T.M.5
  • 17
    • 61849162815 scopus 로고    scopus 로고
    • Heat stabilization of the tissue proteome: a new technology for improved proteomics
    • Svensson M., Boren M., Skold K., Falth M., Sjogren B., Andersson M., et al. Heat stabilization of the tissue proteome: a new technology for improved proteomics. J. Proteome Res. 2009, 8:974-981.
    • (2009) J. Proteome Res. , vol.8 , pp. 974-981
    • Svensson, M.1    Boren, M.2    Skold, K.3    Falth, M.4    Sjogren, B.5    Andersson, M.6
  • 18
    • 34249315396 scopus 로고    scopus 로고
    • Inhibition of intrinsic proteolytic activities moderates preanalytical variability and instability of human plasma
    • Yi J., Kim C., Gelfand C.A. Inhibition of intrinsic proteolytic activities moderates preanalytical variability and instability of human plasma. J. Proteome Res. 2007, 6:1768-1781.
    • (2007) J. Proteome Res. , vol.6 , pp. 1768-1781
    • Yi, J.1    Kim, C.2    Gelfand, C.A.3
  • 19
    • 70350215650 scopus 로고    scopus 로고
    • Tissue is alive: new technologies are needed to address the problems of protein biomarker pre-analytical variability
    • Espina V., Mueller C., Edmiston K., Sciro M., Petricoin E.F., Liotta L.A. Tissue is alive: new technologies are needed to address the problems of protein biomarker pre-analytical variability. Proteomics Clin. Appl. 2009, 3:874-882.
    • (2009) Proteomics Clin. Appl. , vol.3 , pp. 874-882
    • Espina, V.1    Mueller, C.2    Edmiston, K.3    Sciro, M.4    Petricoin, E.F.5    Liotta, L.A.6
  • 20
    • 77958595956 scopus 로고    scopus 로고
    • Ultrafast mid-IR laser scalpel: protein signals of the fundamental limits to minimally invasive surgery
    • Amini-Nik S., Kraemer D., Cowan M.L., Gunaratne K., Nadesan P., Alman B.A., et al. Ultrafast mid-IR laser scalpel: protein signals of the fundamental limits to minimally invasive surgery. PLoS ONE 2010, 5.
    • (2010) PLoS ONE , vol.5
    • Amini-Nik, S.1    Kraemer, D.2    Cowan, M.L.3    Gunaratne, K.4    Nadesan, P.5    Alman, B.A.6
  • 21
    • 84920074417 scopus 로고    scopus 로고
    • Ultrafast extraction of proteins from tissues using desorption by impulsive vibrational excitation
    • Kwiatkowski M., Wurlitzer M., Omidi M., Ren L., Kruber S., Nimer R., et al. Ultrafast extraction of proteins from tissues using desorption by impulsive vibrational excitation. Angew. Chem. 2015, 54:285-288.
    • (2015) Angew. Chem. , vol.54 , pp. 285-288
    • Kwiatkowski, M.1    Wurlitzer, M.2    Omidi, M.3    Ren, L.4    Kruber, S.5    Nimer, R.6
  • 22
    • 72049112858 scopus 로고    scopus 로고
    • Laser selective cutting of biological tissues by impulsive heat deposition through ultrafast vibrational excitations
    • Franjic K., Cowan M.L., Kraemer D., Miller R.J. Laser selective cutting of biological tissues by impulsive heat deposition through ultrafast vibrational excitations. Opt. Express 2009, 17:22937-22959.
    • (2009) Opt. Express , vol.17 , pp. 22937-22959
    • Franjic, K.1    Cowan, M.L.2    Kraemer, D.3    Miller, R.J.4
  • 23
    • 77952360659 scopus 로고    scopus 로고
    • Vibrationally excited ultrafast thermodynamic phase transitions at the water/air interface
    • Franjic K., Miller D. Vibrationally excited ultrafast thermodynamic phase transitions at the water/air interface. Phys. Chem. Chem. Phys. 2010, 12:5225-5239.
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 5225-5239
    • Franjic, K.1    Miller, D.2
  • 24
    • 84925278303 scopus 로고    scopus 로고
    • Reduction of thermocoagulative injury via use of a picosecond infrared laser (PIRL) in laryngeal tissues
    • Bottcher A., Kucher S., Knecht R., Jowett N., Krotz P., Reimer R., et al. Reduction of thermocoagulative injury via use of a picosecond infrared laser (PIRL) in laryngeal tissues. Eur. Arch. Otorhinolaryngol. 2015, 272:941-948.
    • (2015) Eur. Arch. Otorhinolaryngol. , vol.272 , pp. 941-948
    • Bottcher, A.1    Kucher, S.2    Knecht, R.3    Jowett, N.4    Krotz, P.5    Reimer, R.6
  • 25
    • 84937111155 scopus 로고    scopus 로고
    • Towards instantaneous cellular level bio diagnosis: laser extraction and imaging of biological entities with conserved integrity and activity
    • Ren L., Robertson W.D., Reimer R., Heinze C., Schneider C., Eggert D., et al. Towards instantaneous cellular level bio diagnosis: laser extraction and imaging of biological entities with conserved integrity and activity. Nanotechnology 2015, 26:284001.
    • (2015) Nanotechnology , vol.26 , pp. 284001
    • Ren, L.1    Robertson, W.D.2    Reimer, R.3    Heinze, C.4    Schneider, C.5    Eggert, D.6
  • 27
    • 0029020259 scopus 로고
    • Two-dimensional electrophoresis of proteins: an updated protocol and implications for a functional analysis of the genome
    • Klose J., Kobalz U. Two-dimensional electrophoresis of proteins: an updated protocol and implications for a functional analysis of the genome. Electrophoresis 1995, 16:1034-1059.
    • (1995) Electrophoresis , vol.16 , pp. 1034-1059
    • Klose, J.1    Kobalz, U.2
  • 28
    • 34648834050 scopus 로고    scopus 로고
    • The state of the art in the analysis of two-dimensional gel electrophoresis images
    • Berth M., Moser F.M., Kolbe M., Bernhardt J. The state of the art in the analysis of two-dimensional gel electrophoresis images. Appl. Microbiol. Biotechnol. 2007, 76:1223-1243.
    • (2007) Appl. Microbiol. Biotechnol. , vol.76 , pp. 1223-1243
    • Berth, M.1    Moser, F.M.2    Kolbe, M.3    Bernhardt, J.4
  • 29
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko A., Tomas H., Havlis J., Olsen J.V., Mann M. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protoc. 2006, 1:2856-2860.
    • (2006) Nat. Protoc. , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 30
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox J., Mann M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 2008, 26:1367-1372.
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 31
    • 84907197082 scopus 로고    scopus 로고
    • Accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction, termed MaxLFQ
    • Cox J., Hein M.Y., Luber C.A., Paron I., Nagaraj N., Mann M. Accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction, termed MaxLFQ. Mol. Cell. Proteomics 2014, 13:2513-2526.
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 2513-2526
    • Cox, J.1    Hein, M.Y.2    Luber, C.A.3    Paron, I.4    Nagaraj, N.5    Mann, M.6
  • 32
    • 58549112996 scopus 로고    scopus 로고
    • Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists
    • Huang da W., Sherman B.T., Lempicki R.A. Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists. Nucleic Acids Res. 2009, 37:1-13.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 1-13
    • Huang da, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 33
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang da W., Sherman B.T., Lempicki R.A. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat. Protoc. 2009, 4:44-57.
    • (2009) Nat. Protoc. , vol.4 , pp. 44-57
    • Huang da, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 34
    • 39749099462 scopus 로고    scopus 로고
    • Strategy for comprehensive identification of post-translational modifications in cellular proteins, including low abundant modifications: application to glyceraldehyde-3-phosphate dehydrogenase
    • Seo J., Jeong J., Kim Y.M., Hwang N., Paek E., Lee K.J. Strategy for comprehensive identification of post-translational modifications in cellular proteins, including low abundant modifications: application to glyceraldehyde-3-phosphate dehydrogenase. J. Proteome Res. 2008, 7:587-602.
    • (2008) J. Proteome Res. , vol.7 , pp. 587-602
    • Seo, J.1    Jeong, J.2    Kim, Y.M.3    Hwang, N.4    Paek, E.5    Lee, K.J.6
  • 35
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., et al. Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 2009, 325:834-840.
    • (2009) Science , vol.325 , pp. 834-840
    • Choudhary, C.1    Kumar, C.2    Gnad, F.3    Nielsen, M.L.4    Rehman, M.5    Walther, T.C.6
  • 36
    • 84890300195 scopus 로고    scopus 로고
    • An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome
    • Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., et al. An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J. Proteome 2014, 96:253-262.
    • (2014) J. Proteome , vol.96 , pp. 253-262
    • Bian, Y.1    Song, C.2    Cheng, K.3    Dong, M.4    Wang, F.5    Huang, J.6
  • 37
    • 84922386015 scopus 로고    scopus 로고
    • Proteomic challenges: sample preparation techniques for microgram-quantity protein analysis from biological samples
    • Feist P., Hummon A.B. Proteomic challenges: sample preparation techniques for microgram-quantity protein analysis from biological samples. Int. J. Mol. Sci. 2015, 16:3537-3563.
    • (2015) Int. J. Mol. Sci. , vol.16 , pp. 3537-3563
    • Feist, P.1    Hummon, A.B.2
  • 38
    • 0023092732 scopus 로고
    • Dynamic state of collagen: pathways of collagen degradation in vivo and their possible role in regulation of collagen mass
    • Laurent G.J. Dynamic state of collagen: pathways of collagen degradation in vivo and their possible role in regulation of collagen mass. Am. J. Physiol. 1987, 252:C1-C9.
    • (1987) Am. J. Physiol. , vol.252 , pp. C1-C9
    • Laurent, G.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.