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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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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-6C78-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-C9A5-8
Genre: Journal Article

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1-s2.0-S1874391916300045-main.pdf (Publisher version), 2MB
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Copyright Date:
2016
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© Kwiatkowski et al.

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http://dx.doi.org/10.1016/j.jprot.2015.12.029 (Publisher version)
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 Creators:
Kwiatkowski, M.1, Author
Wurlitzer, M.1, Author
Krutilin, A.1, Author
Kiani, P.1, Author
Nimer, R.1, Author
Omidi, M.1, Author
Mannaa, A.1, Author
Bussmann, T.2, Author
Bartkowiak, K.3, Author
Kruber, Sebastian4, Author              
Uschold, Stephanie4, Author              
Steffen, P.1, Author
Lübberstedt, J.1, Author
Küpker, N.1, Author
Petersen, H.5, Author
Knecht, R.5, Author
Hansen, N.-O.4, Author              
Zarrine-Afsar, A.6, Author
Robertson, W.4, Author              
Miller, R. J. Dwayne4, Author              
Schlüter, H.1, Author more..
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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Free keywords: Tissue homogenization; Protein species; Proteolysis; PIRL-DIVE; Mass spectrometry
 Abstract: 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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Language(s): eng - English
 Dates: 2015-12-222015-07-302015-12-312016-01-082016-02-16
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.jprot.2015.12.029
BibTex Citekey: Kwiatkowski2016
 Degree: -

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Title: Journal of Proteomics
  Abbreviation : J. Proteome
Source Genre: Journal
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Publ. Info: Amsterdam, The Netherlands : European Proteomics Association & Elsevier
Pages: - Volume / Issue: 134 Sequence Number: - Start / End Page: 193 - 202 Identifier: ISSN: 1874-3919
CoNE: /journals/resource/1874-3919