Publication

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., Mannaa, A., Bussmann, T., Bartkowiak, K., Kruber, S., Uschold, S., Steffen, P., Luebberstedt, J., Kuepker, N., Petersen, H., Knecht, R., Hansen, N. O., Zarrine-Afsar, A., Robertson, W. D., Miller, R. J. D. & Schlueter, H., 16-Feb-2016, In : Journal of proteomics. 134, p. 193-202 10 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Kwiatkowski, M., Wurlitzer, M., Krutilin, A., Kiani, P., Nimer, R., Omidi, M., ... Schlueter, H. (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. https://doi.org/10.1016/j.jprot.2015.12.029

Author

Kwiatkowski, M. ; Wurlitzer, M. ; Krutilin, A. ; Kiani, P. ; Nimer, R. ; Omidi, M. ; Mannaa, A. ; Bussmann, T. ; Bartkowiak, K. ; Kruber, S. ; Uschold, S. ; Steffen, P. ; Luebberstedt, J. ; Kuepker, N. ; Petersen, H. ; Knecht, R. ; Hansen, N. O. ; Zarrine-Afsar, A. ; Robertson, W. D. ; Miller, R. J. D. ; Schlueter, H. / 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. In: Journal of proteomics. 2016 ; Vol. 134. pp. 193-202.

Harvard

Kwiatkowski, M, Wurlitzer, M, Krutilin, A, Kiani, P, Nimer, R, Omidi, M, Mannaa, A, Bussmann, T, Bartkowiak, K, Kruber, S, Uschold, S, Steffen, P, Luebberstedt, J, Kuepker, N, Petersen, H, Knecht, R, Hansen, NO, Zarrine-Afsar, A, Robertson, WD, Miller, RJD & Schlueter, H 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, vol. 134, pp. 193-202. https://doi.org/10.1016/j.jprot.2015.12.029

Standard

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.; Mannaa, A.; Bussmann, T.; Bartkowiak, K.; Kruber, S.; Uschold, S.; Steffen, P.; Luebberstedt, J.; Kuepker, N.; Petersen, H.; Knecht, R.; Hansen, N. O.; Zarrine-Afsar, A.; Robertson, W. D.; Miller, R. J. D.; Schlueter, H.

In: Journal of proteomics, Vol. 134, 16.02.2016, p. 193-202.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Kwiatkowski M, Wurlitzer M, Krutilin A, Kiani P, Nimer R, Omidi M et al. 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. 2016 Feb 16;134:193-202. https://doi.org/10.1016/j.jprot.2015.12.029


BibTeX

@article{5d544741a0f74f39983dfbe14f24bd17,
title = "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",
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. (C) 2016 The Authors. Published by Elsevier B.V.",
keywords = "Tissue homogenization, Protein species, Proteolysis, PIRL-DIVE, Mass spectrometry, POSTTRANSLATIONAL MODIFICATIONS, 2-DIMENSIONAL ELECTROPHORESIS, PREANALYTICAL VARIABILITY, SAMPLE PREPARATION, IDENTIFICATION, EXTRACTION, PROTEOMICS, MASS, QUANTIFICATION, STATE",
author = "M. Kwiatkowski and M. Wurlitzer and A. Krutilin and P. Kiani and R. Nimer and M. Omidi and A. Mannaa and T. Bussmann and K. Bartkowiak and S. Kruber and S. Uschold and P. Steffen and J. Luebberstedt and N. Kuepker and H. Petersen and R. Knecht and Hansen, {N. O.} and A. Zarrine-Afsar and Robertson, {W. D.} and Miller, {R. J. D.} and H. Schlueter",
year = "2016",
month = "2",
day = "16",
doi = "10.1016/j.jprot.2015.12.029",
language = "English",
volume = "134",
pages = "193--202",
journal = "Journal of proteomics",
issn = "1874-3919",
publisher = "ELSEVIER SCIENCE BV",

}

RIS

TY - JOUR

T1 - Homogenization of tissues via picosecond-infrared laser (PIRL) ablation

T2 - Giving a closer view on the in-vivo composition of protein species as compared to mechanical homogenization

AU - Kwiatkowski, M.

AU - Wurlitzer, M.

AU - Krutilin, A.

AU - Kiani, P.

AU - Nimer, R.

AU - Omidi, M.

AU - Mannaa, A.

AU - Bussmann, T.

AU - Bartkowiak, K.

AU - Kruber, S.

AU - Uschold, S.

AU - Steffen, P.

AU - Luebberstedt, J.

AU - Kuepker, N.

AU - Petersen, H.

AU - Knecht, R.

AU - Hansen, N. O.

AU - Zarrine-Afsar, A.

AU - Robertson, W. D.

AU - Miller, R. J. D.

AU - Schlueter, H.

PY - 2016/2/16

Y1 - 2016/2/16

N2 - 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. (C) 2016 The Authors. Published by Elsevier B.V.

AB - 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. (C) 2016 The Authors. Published by Elsevier B.V.

KW - Tissue homogenization

KW - Protein species

KW - Proteolysis

KW - PIRL-DIVE

KW - Mass spectrometry

KW - POSTTRANSLATIONAL MODIFICATIONS

KW - 2-DIMENSIONAL ELECTROPHORESIS

KW - PREANALYTICAL VARIABILITY

KW - SAMPLE PREPARATION

KW - IDENTIFICATION

KW - EXTRACTION

KW - PROTEOMICS

KW - MASS

KW - QUANTIFICATION

KW - STATE

U2 - 10.1016/j.jprot.2015.12.029

DO - 10.1016/j.jprot.2015.12.029

M3 - Article

VL - 134

SP - 193

EP - 202

JO - Journal of proteomics

JF - Journal of proteomics

SN - 1874-3919

ER -

ID: 48887923