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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.
Pancreatic cancer is the currently most lethal malignancy. Toward an accurate diagnosis of the disease in body liquids, we studied the protein composition of the secretomes of 16 primary and establish...
Monocytes are a part of the innate immune system. Their differentiation into macrophages changes their cellular proteome and secretome. Particularly secretome components such as cytokines are crucial ...
Lectins are omnipresent in almost all life forms, being the proteins which specifically bind to carbohydrate moieties on the cell surface; they have been explored for their anti-tumour activities. In ...
Adipose tissue secretes a plethora of adipokines as evidenced by characterization of subcutaneous and visceral adipose tissue secretomes. However, adipose tissue composition and secretion pattern is d...
Brown algae have evolved complex multicellularity in the heterokont lineage. They are phylogenetically distant to land plants, fungi and animals. Especially, the members of Laminariales (so-called kel...
RATIONALE: Mistletoe lectin may slow the growth of cancer cells and be an effective treatment for solid tumors. PURPOSE: Phase I trial to study the effectiveness of mistletoe lectin in tr...
The aim of this study is to identify the protein secretion and consumption profile of the human blastocyst (secretome) and the implanted blastocyst (implantome) using the protein array tec...
This study includes comatose survivors of out-of-hospital cardiac arrest treated with 24 hours or 48 hours of targeted temperature management. The overall aim is to evaluate the importanc...
The pharmacokinetics, and clinical and biological effects of MBL replacement therapy in MBL-deficient children during chemotherapy-induced neutropenia were studied.
The investigators will collect samples of sputum from healthy volunteers and patients with cystic fibrosis for the purpose of: a) purifying airway mucins for plate-based binding studies an...
Strategy for the analysis of RANDOMIZED CONTROLLED TRIALS AS TOPIC that compares patients in the groups to which they were originally randomly assigned.
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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