Proteomics

Dataset Information

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SWATH proteomics reveals that reductants selectively disrupt collagen homeostasis in human dermal fibroblasts and modify growth factor-independent signalling through the MAPK/Akt pathway


ABSTRACT: We have used an unbiased, label-free SWATH proteomic approach to quantitate the response of skin fibroblast cells to the reductant DTT in the presence or absence of the growth factor PDGF. Of the 4487 proteins that were identified, only 47 proteins showed a statistically significant change of 2-fold or more with reducing stress. Our data demonstrates that reducing stress results in the loss of a small subset of reductant-sensitive proteins, including the fibrillar collagens (COL1A1/2 and COL3A1) and the myopathy-associated bundling collagen COL6A1/2/3.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture, Fibroblast

SUBMITTER: Adrian Brown  

LAB HEAD: Adrian Paul Brown

PROVIDER: PXD010747 | Pride | 2019-03-25

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
IonsPeakareas.csv Csv
NC_CONTROL_1_A.wiff.zip Wiff
NC_CONTROL_1_B.wiff.zip Wiff
NC_CONTROL_1_C.wiff.zip Wiff
NC_CONTROL_2_A.wiff.zip Wiff
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Publications

Reductive Stress Selectively Disrupts Collagen Homeostasis and Modifies Growth Factor-independent Signaling Through the MAPK/Akt Pathway in Human Dermal Fibroblasts.

Carne Naomi A NA   Bell Steven S   Brown Adrian P AP   Määttä Arto A   Flagler Michael J MJ   Benham Adam M AM  

Molecular & cellular proteomics : MCP 20190319 6


Redox stress is a well-known contributor to aging and diseases in skin. Reductants such as dithiothreitol (DTT) can trigger a stress response by disrupting disulfide bonds. However, the quantitative response of the cellular proteome to reductants has not been explored, particularly in cells such as fibroblasts that produce extracellular matrix proteins. Here, we have used a robust, unbiased, label-free SWATH-MS proteomic approach to quantitate the response of skin fibroblast cells to DTT in the  ...[more]

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