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  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

Kwiatkowski, M., Wurlitzer, M., Krutilin, A., Kiani, P., Nimer, R., Omidi, M., et al. (2016). 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. Journal of Proteomics, 134, 193-202. doi:10.1016/j.jprot.2015.12.029.

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2016
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© Kwiatkowski et al.

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http://dx.doi.org/10.1016/j.jprot.2015.12.029 (Verlagsversion)
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 Urheber:
Kwiatkowski, M.1, Autor
Wurlitzer, M.1, Autor
Krutilin, A.1, Autor
Kiani, P.1, Autor
Nimer, R.1, Autor
Omidi, M.1, Autor
Mannaa, A.1, Autor
Bussmann, T.2, Autor
Bartkowiak, K.3, Autor
Kruber, Sebastian4, Autor           
Uschold, Stephanie4, Autor           
Steffen, P.1, Autor
Lübberstedt, J.1, Autor
Küpker, N.1, Autor
Petersen, H.5, Autor
Knecht, R.5, Autor
Hansen, N.-O.4, Autor           
Zarrine-Afsar, A.6, Autor
Robertson, W.4, Autor           
Miller, R. J. Dwayne4, Autor           
Schlüter, H.1, Autor mehr..
Affiliations:
1University Medical Centre Hamburg-Eppendorf, Institute for Clinical Chemistry, Department for Mass Spectrometric Proteomics, Martinistraße 52, 20246 Hamburg, Germany, ou_persistent22              
2Beiersdorf AG, Research & Development, Unnastrasse 48, 20245, Hamburg, Germany, ou_persistent22              
3University Medical Centre Hamburg-Eppendorf, Department of Tumor Biology, Martinistraße 52, 20246 Hamburg, Germany, ou_persistent22              
4Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society, ou_1938288              
5University Medical Centre Hamburg-Eppendorf, Department of Otorhinolaryngology, Head and Neck Surgery and Oncology, Martinistraße 52, 20246 Hamburg, Germany, ou_persistent22              
6Techna Institute for the Advancement of Technology for Health, University Health Network, Toronto, ON M5G-1P5, Canada & Department of Medical Biophysics, University of Toronto, 101 College Street Suite 15-701, Toronto, ON M5G 1L7, Canada, ou_persistent22              

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Schlagwörter: Tissue homogenization; Protein species; Proteolysis; PIRL-DIVE; Mass spectrometry
 Zusammenfassung: Abstract Posttranslational modifications and proteolytic processing regulate almost all physiological processes. Dysregulation can potentially result in pathologic protein species causing diseases. Thus, tissue species proteomes of diseased individuals provide diagnostic information. Since the composition of tissue proteomes can rapidly change during tissue homogenization by the action of enzymes released from their compartments, disease specific protein species patterns can vanish. Recently, we described a novel, ultrafast and soft method for cold vaporization of tissue via desorption by impulsive vibrational excitation (DIVE) using a picosecond-infrared-laser (PIRL). Given that DIVE extraction may provide improved access to the original composition of protein species in tissues, we compared the proteome composition of tissue protein homogenates after DIVE homogenization with conventional homogenizations. A higher number of intact protein species was observed in DIVE homogenates. Due to the ultrafast transfer of proteins from tissues via gas phase into frozen condensates of the aerosols, intact protein species were exposed to a lesser extent to enzymatic degradation reactions compared with conventional protein extraction. In addition, total yield of the number of proteins is higher in DIVE homogenates, because they are very homogenous and contain almost no insoluble particles, allowing direct analysis with subsequent analytical methods without the necessity of centrifugation. Biological significance Enzymatic protein modifications during tissue homogenization are responsible for changes of the in-vivo protein species composition. Cold vaporization of tissues by PIRL-DIVE is comparable with taking a snapshot at the time of the laser irradiation of the dynamic changes that occur continuously under in-vivo conditions. At that time point all biomolecules are transferred into an aerosol, which is immediately frozen.

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Sprache(n): eng - English
 Datum: 2015-12-222015-07-302015-12-312016-01-082016-02-16
 Publikationsstatus: Erschienen
 Seiten: 10
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1016/j.jprot.2015.12.029
BibTex Citekey: Kwiatkowski2016
 Art des Abschluß: -

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Titel: Journal of Proteomics
  Kurztitel : J. Proteome
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Amsterdam, The Netherlands : European Proteomics Association & Elsevier
Seiten: - Band / Heft: 134 Artikelnummer: - Start- / Endseite: 193 - 202 Identifikator: ISSN: 1874-3919
CoNE: https://pure.mpg.de/cone/journals/resource/1874-3919