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Status: Bibliographieeintrag

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Verfasst von:Stieß, Michael [VerfasserIn]   i
 Wegehingel, Sabine [VerfasserIn]   i
 Nguyen, Chuong [VerfasserIn]   i
 Nickel, Walter [VerfasserIn]   i
 Bradke, Frank [VerfasserIn]   i
 Cambridge, Sidney [VerfasserIn]   i
Titel:A dual SILAC proteomic labeling strategy for quantifying constitutive and cell-cell induced protein secretion
Verf.angabe:Michael Stiess, Sabine Wegehingel, Chuong Nguyen, Walter Nickel, Frank Bradke, and Sidney B. Cambridge
E-Jahr:2015
Jahr:July 20, 2015
Umfang:10 S.
Fussnoten:Gesehen am 23.06.2020
Titel Quelle:Enthalten in: Journal of proteome research
Ort Quelle:Washington, DC : ACS Publications, 2002
Jahr Quelle:2015
Band/Heft Quelle:14(2015), 8, Seite 3229-3238
ISSN Quelle:1535-3907
Abstract:Recent evidence suggests that the extracellular protein milieu is much more complex than previously assumed as various secretome analyses from different cell types described the release of hundreds to thousands of proteins. The extracellular function of many of these proteins has yet to be determined particularly in the context of three-dimensional tissues with abundant cell-cell contacts. Toward this goal, we developed a strategy of dual SILAC labeling astrocytic cultures for in silico exclusion of unlabeled proteins from serum or neurons used for stimulation. For constitutive secretion, this strategy allowed the precise quantification of the extra-to-intracellular protein ratio of more than 2000 identified proteins. Ratios covered 4 orders of magnitude indicating that the intracellular vs extracellular contributions of different proteins can be variable. Functionally, the secretome of labeled forebrain astrocytic cultures specifically changed within hours after adding unlabeled, “physiological” forebrain neurons. “Nonphysiological” cerebellar hindbrain neurons, however, elicited a different, highly repulsive secretory response. Our data also suggest a significant association of constitutive secretion with the classical secretion pathway and regulated secretion with unconventional pathways. We conclude that quantitative proteomics can help to elucidate general principles of cellular secretion and provide functional insight into the abundant extracellular presence of proteins.
DOI:doi:10.1021/acs.jproteome.5b00199
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext: https://doi.org/10.1021/acs.jproteome.5b00199
 DOI: https://doi.org/10.1021/acs.jproteome.5b00199
Datenträger:Online-Ressource
Sprache:eng
K10plus-PPN:1701957434
Verknüpfungen:→ Zeitschrift

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