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1.
Figure 6

Figure 6. Western blot analysis for a subset of differentially expressed proteins. From: Temporal profiling of the adipocyte proteome during differentiation using a 5-plex SILAC based strategy.

The left panel shows Western blot results with the right panel showing MS/MS spectra of a peptide from the corresponding protein.

Henrik Molina, et al. J Proteome Res. ;8(1):48-58.
2.
Figure 5

Figure 5. Heat map of quantitated secreted proteins. From: Temporal profiling of the adipocyte proteome during differentiation using a 5-plex SILAC based strategy.

The heat map shows the temporal profile of each protein identified and quantitated in the secretome by 5-plex SILAC based MS analysis. Relative expression abundance for each protein is indicated in each frame using Day 0 as a reference. For reference, a color intensity scale is included in the right side.

Henrik Molina, et al. J Proteome Res. ;8(1):48-58.
3.
Figure 4

Figure 4. Heat map of quantitated nuclear proteins. From: Temporal profiling of the adipocyte proteome during differentiation using a 5-plex SILAC based strategy.

The heat map shows the temporal profile of each protein identified and quantitated in nuclear fraction by 5-plex SILAC based MS analysis. Relative expression abundance for each protein is indicated in each frame using Day 0 as a reference. For reference, a color intensity scale is included in the right side.

Henrik Molina, et al. J Proteome Res. ;8(1):48-58.
4.
Figure 3

Figure 3. Gene Ontology and cellular component analysis. From: Temporal profiling of the adipocyte proteome during differentiation using a 5-plex SILAC based strategy.

Gene Ontology analysis for identified nuclear and secreted proteins was performed using ProteinCenter version 1.2 (Proxeon A/S, Odense, Denmark). Panel A shows the analysis for the 581 proteins identified in the nuclear enriched fraction, while panel B shows the corresponding analysis for the proteins identified from the secretome. Approximately half (284) of the proteins found in the nuclear fraction were previously known nuclear proteins. For the secreted proteins, the analysis revealed 149 proteins were membrane or cell surface proteins.

Henrik Molina, et al. J Proteome Res. ;8(1):48-58.
5.
Figure 1

Figure 1. 5-plex SILAC strategy and Oil red O staining for adipocyte differentiation. From: Temporal profiling of the adipocyte proteome during differentiation using a 5-plex SILAC based strategy.

A) Preadipocytes were grown in different cell culture media containing 5 different isotopic forms of arginine as shown until complete isotopic amino acid incorporation. After the induction of differentiation, cells were harvested on Day 0, Day 1, Day 3, Day 5 and Day 7 of the differentiation process and combined after protein normalization. In parallel, serum free media from five different cell populations were collected at the indicated time points and combined. The nuclear fraction and the secretome were processed and analyzed by LC-MS/MS. B) Differentiation of adipocytes was confirmed by Oil red O staining. Cells on Day 3, Day 5 and Day 7 show a progressive increase in red staining for fat droplets, indicating the extent of adipocyte differentiation.

Henrik Molina, et al. J Proteome Res. ;8(1):48-58.
6.

Figure 2. Mass spectra and elution profiles for SILAC labeled peptide sets. From: Temporal profiling of the adipocyte proteome during differentiation using a 5-plex SILAC based strategy.

Upper panels show the mass spectra and lower panels show elution profiles. The color code of the peptide elution profiles are: red: Day 0, blue: Day 1, green: Day 3, violet: Day 5 and black: Day 7, represented by the isotopes: normal, 13C4, 13C6, 13C615N4, and 13C615N42H7, respectively. The mass differences between the isotopic labeled peptides are shown in each upper panel. The sequence and charge states of the depicted peptides are as following. Figure 2 A: The peptides from secreted fraction. A: APILIATDVASR, doubly charged (DEAD box polypeptide 5), B: LGVEFDEITADDRK, triply charged (Fatty acid binding protein 2) and C: WISIMTER, doubly charged (Annexin A2). Figure 2 B: the peptides from nuclear fraction. A: IETIEVMEDR, doubly charged (similar to heterogeneous nuclear ribonucleoprotein A3 isoform 7), B: AAAITSDLLESLGR, doubly charged (osteoblast specific factor 2, fasciclin I-like), C: FGVEQDVDMVFASFIR, triply charged (pyruvate kinase 3).

Henrik Molina, et al. J Proteome Res. ;8(1):48-58.

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