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An optimized isolation of biotinylated cell surface proteins reveals novel players in cancer metastasis.

Abstract：

:Details of metastasis, the deadliest aspect of cancer, are unclear. Cell surface proteins play central roles in adhesive contacts between the tumor cell and the stroma during metastasis. We optimized a fast, small-scale isolation of biotinylated cell surface proteins to reveal novel metastasis-associated players from an isogenic pair of human MDA-MB-435 cancer cells with opposite metastatic phenotypes. Isolated proteins were trypsin digested and analyzed using LC-MS/MS followed by quantitation with the Progenesis LC-MS software. Sixteen proteins displayed over twofold expression differences between the metastatic and non-metastatic cells. Interestingly, overexpression of most of them (14/16) in the metastatic cells indicates a gain of novel surface protein profile as compared to the non-metastatic ones. All five validated, differentially expressed proteins showed higher expression in the metastatic cells in culture, and four of these were further validated in vivo. Moreover, we analyzed expression of two of the identified proteins, CD109 and ITGA6 in 3-dimensional cultures of six melanoma cell lines. Both proteins marked the surface of cells derived from melanoma metastasis over cells derived from primary melanoma. The unbiased identification and validation of both known and novel metastasis-associated proteins indicate a reliable approach for the identification of differentially expressed surface proteins.

journal_name

J Proteomics

journal_title

Journal of proteomics

authors

Karhemo PR,Ravela S,Laakso M,Ritamo I,Tatti O,Mäkinen S,Goodison S,Stenman UH,Hölttä E,Hautaniemi S,Valmu L,Lehti K,Laakkonen P

doi

10.1016/j.jprot.2012.07.009

subject

Has Abstract

pub_date

2012-12-21 00:00:00

pages

87-100

eissn

1874-3919

issn

1876-7737

pii

S1874-3919(12)00539-8

journal_volume

77

pub_type

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