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Secreted proteins play important roles in physiological and pathological processes. However, effective proteomic detection of low abundant secreted proteins is often shielded by the presence of a large amount of intracellular proteins released from unavoidable dead cells during cell culture. In the present work, we applied lectin affinity capture approach to enrich the secreted proteins in the conditioned media (CM) of three human breast cell lines (MCF-10A, MCF-7, MDA-MB-231). Lectin capture showed efficient enrichment of the secreted proteins in CM of all three cell lines and significantly increased the number of secreted proteins detected: from 183 to 292 for MCF-10A, 196 to 325 for MCF-7, and 194 to 368 for MDA-MB-231. Based on more comprehensive profiling of the secreted proteins, we identified 92 secreted proteins which were both up-regulated in MCF-7 and MDA-MB-231, with 82 only found in lectin captured samples. It should be noted that among these 82 potential biomarkers, 59 were not reported in previous proteomic studies of breast cancer. These data indicate that the lectin capture approach is a powerful means to move toward more comprehensive analysis and comparison of secretomes.
School of Biomedical Engineering and Med-X Research Institute, Shanghai Jiao Tong University, Shanghai, China.
This article was published in the following journal.
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A subclass of NK cell lectin-like receptors that associates with a variety of members of NK CELL LECTIN-LIKE RECEPTOR SUBFAMILY C to form heterodimeric receptors for HLA-E antigen.
A subclass of NK cell lectin-like receptors that associates with members of NK CELL LECTIN-LIKE RECEPTOR SUBFAMILY D to form heterodimeric receptors for HLA-E antigen.
A subclass of NK cell lectin-like receptors that includes both inhibitory and stimulatory members.
An inhibitory subclass of NK cell lectin-like receptors that interacts with CLASS I MAJOR HISTOCOMPATIBILITY ANTIGENS and prevents the activation of NK CELLS.
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