» Articles » PMID: 23162466

Metastasis-associated Cell Surface Oncoproteomics

Overview
Journal Front Pharmacol
Date 2012 Nov 20
PMID 23162466
Citations 8
Authors
Affiliations
Soon will be listed here.
Abstract

Oncoproteomics aims to the discovery of molecular markers, drug targets, and pathways by studying cancer specific protein expression, localization, modification, and interaction. Cell surface proteins play a central role in several pathological conditions, including cancer and its metastatic spread. However, cell surface proteins are underrepresented in proteomics analyses performed from the whole cell extracts due to their hydrophobicity and low abundance. Different methods have been developed to enrich and isolate the cell surface proteins to reduce sample complexity. Despite the method selected, the primary difficulty encountered is the solubilization of the hydrophobic transmembrane proteins from the lipid bilayer. This review focuses on proteomic analyses of metastasis-associated proteins identified using the cell surface biotinylation method. Interestingly, also certain intracellular proteins were identified from the cell surface samples. The function of these proteins at the cell surface might well differ from their function inside the cell.

Citing Articles

Current and Future Trends of Colorectal Cancer Treatment: Exploring Advances in Immunotherapy.

Nikolouzakis T, Chrysos E, Docea A, Fragkiadaki P, Souglakos J, Tsiaoussis J Cancers (Basel). 2024; 16(11).

PMID: 38893120 PMC: 11171065. DOI: 10.3390/cancers16111995.


Extracellular Vesicles as Next-Generation Biomarkers in Lung Cancer Patients: A Case Report on Adenocarcinoma and Squamous Cell Carcinoma.

Ruzycka-Ayoush M, Prochorec-Sobieszek M, Cieszanowski A, Glogowski M, Szumera-Cieckiewicz A, Podgorska J Life (Basel). 2024; 14(3).

PMID: 38541732 PMC: 10971644. DOI: 10.3390/life14030408.


Current Methods for Identifying Plasma Membrane Proteins as Cancer Biomarkers.

de Jong E, Kocer A Membranes (Basel). 2023; 13(4).

PMID: 37103836 PMC: 10142483. DOI: 10.3390/membranes13040409.


MUC16 promotes triple-negative breast cancer lung metastasis by modulating RNA-binding protein ELAVL1/HUR.

Chaudhary S, Appadurai M, Maurya S, Nallasamy P, Marimuthu S, Shah A Breast Cancer Res. 2023; 25(1):25.

PMID: 36918912 PMC: 10012760. DOI: 10.1186/s13058-023-01630-7.


Proteomic Approach for Searching for Universal, Tissue-Specific, and Line-Specific Markers of Extracellular Vesicles in Lung and Colorectal Adenocarcinoma Cell Lines.

Novikova S, Shushkova N, Farafonova T, Tikhonova O, Kamyshinsky R, Zgoda V Int J Mol Sci. 2020; 21(18).

PMID: 32916986 PMC: 7555231. DOI: 10.3390/ijms21186601.


References
1.
Zhang B . CD73: a novel target for cancer immunotherapy. Cancer Res. 2010; 70(16):6407-11. PMC: 2922475. DOI: 10.1158/0008-5472.CAN-10-1544. View

2.
Sastry S, Elferink L . Checks and balances: interplay of RTKs and PTPs in cancer progression. Biochem Pharmacol. 2011; 82(5):435-40. DOI: 10.1016/j.bcp.2011.06.016. View

3.
Fogel M, Altevogt P, Schirrmacher V . Metastatic potential severely altered by changes in tumor cell adhesiveness and cell-surface sialylation. J Exp Med. 1983; 157(1):371-6. PMC: 2186915. DOI: 10.1084/jem.157.1.371. View

4.
Wang Y, Ao X, Vuong H, Konanur M, Miller F, Goodison S . Membrane glycoproteins associated with breast tumor cell progression identified by a lectin affinity approach. J Proteome Res. 2008; 7(10):4313-25. PMC: 2630886. DOI: 10.1021/pr8002547. View

5.
Dowling P, Walsh N, Clynes M . Membrane and membrane-associated proteins involved in the aggressive phenotype displayed by highly invasive cancer cells. Proteomics. 2008; 8(19):4054-65. DOI: 10.1002/pmic.200800098. View