Proteomics

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Proteome analysis of NGF stimulated PC12 cells

ABSTRACT: We used quantitative mass spectrometry-based proteomics to unravel global nerve growth factor (NGF)-induced changes in protein abundance using the rat PC12 cell line. Cells were stimulated with NGF for 0, 24 and 48 h in a triple SILAC setup (Light: Lys0,Arg0; Medium: Lys4,Arg6; and Heavy: Lys8,Arg10). All experiments were performed as biological replicates.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Rattus Norvegicus (rat)

TISSUE(S): Adrenal Medulla Chromaffin Cell, Adrenal Medulla

DISEASE(S): Adrenal Gland Pheochromocytoma

SUBMITTER: Kristina Bennet Emdal  

LAB HEAD: Jesper Velgaard Olsen

PROVIDER: PXD001478 | Pride | 2015-05-06

REPOSITORIES: Pride

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Dataset's files

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20120323_QE4_KBE_SA_PC12_NGF15S_ingel_A10_10.raw Raw
20120323_QE4_KBE_SA_PC12_NGF15S_ingel_A1_01.raw Raw
20120323_QE4_KBE_SA_PC12_NGF15S_ingel_A2_02.raw Raw
20120323_QE4_KBE_SA_PC12_NGF15S_ingel_A3_03.raw Raw
20120323_QE4_KBE_SA_PC12_NGF15S_ingel_A4_04.raw Raw
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Publications

Temporal proteomics of NGF-TrkA signaling identifies an inhibitory role for the E3 ligase Cbl-b in neuroblastoma cell differentiation.

Emdal Kristina B KB   Pedersen Anna-Kathrine AK   Bekker-Jensen Dorte B DB   Tsafou Kalliopi P KP   Horn Heiko H   Lindner Sven S   Schulte Johannes H JH   Eggert Angelika A   Jensen Lars J LJ   Francavilla Chiara C   Olsen Jesper V JV  

Science signaling 20150428 374

SH-SY5Y neuroblastoma cells respond to nerve growth factor (NGF)-mediated activation of the tropomyosin-related kinase A (TrkA) with neurite outgrowth, thereby providing a model to study neuronal differentiation. We performed a time-resolved analysis of NGF-TrkA signaling in neuroblastoma cells using mass spectrometry-based quantitative proteomics. The combination of interactome, phosphoproteome, and proteome data provided temporal insights into the molecular events downstream of NGF binding to  ...[more]

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