Proteomics

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Quantitative proteomics analysis of paired colorectal cancer and non-tumorigenic tissues reveal proteins and pathways perturbed in colorectal cancer


ABSTRACT: Proteomics is a dynamic field emerged dramatically the post genomic era which has been extensively employed to study altered protein expression to gain insight into the development process and pathways involved in cancer and uncover potential protein markers. Membrane proteomes of an expanded cohort of paired CRC and adjacent non-tumorigenic tissues (1 female and 7 males) were profiled using high resolution nanoLC-MS/MS-based proteomics, which identified 1,000-1,300 proteins in each of the two tissue types. 184 proteins were differentially expressed (P < 0.05, fold change > 1.5); 69 proteins were up- regulated and 115 proteins were down-regulated in the CRC tissues relative to non-tumorigenic tissues.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Colon

DISEASE(S): Colon Cancer

SUBMITTER: Manveen Sethi  

LAB HEAD: Dr. Susan Fanayan

PROVIDER: PXD001676 | Pride | 2016-06-15

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
Non-tumor-1_mzXML.zip Other
Non-tumor-1_raw.zip Other
Non-tumor-1_xml.xml Xml
Non-tumor-2_mzXML.zip Other
Non-tumor-2_raw.zip Other
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Publications

Quantitative proteomic analysis of paired colorectal cancer and non-tumorigenic tissues reveals signature proteins and perturbed pathways involved in CRC progression and metastasis.

Sethi Manveen K MK   Thaysen-Andersen Morten M   Kim Hoguen H   Park Cheol Keun CK   Baker Mark S MS   Packer Nicolle H NH   Paik Young-Ki YK   Hancock William S WS   Fanayan Susan S  

Journal of proteomics 20150606


Modern proteomics has proven instrumental in our understanding of the molecular deregulations associated with the development and progression of cancer. Herein, we profile membrane-enriched proteome of tumor and adjacent normal tissues from eight CRC patients using label-free nanoLC-MS/MS-based quantitative proteomics and advanced pathway analysis. Of the 948 identified proteins, 184 proteins were differentially expressed (P<0.05, fold change>1.5) between the tumor and non-tumor tissue (69 up-re  ...[more]

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