File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Lectin capture strategy for effective analysis of cell secretome

TitleLectin capture strategy for effective analysis of cell secretome
Authors
KeywordsBreast cancer
Cell secretome
Conditioned medium
Lectin affinity capture
Technology
Issue Date2012
Citation
Proteomics, 2012, v. 12, n. 1, p. 32-36 How to Cite?
AbstractSecreted 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 study, 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, and 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 upregulated 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 the 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. © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Persistent Identifierhttp://hdl.handle.net/10722/342406
ISSN
2023 Impact Factor: 3.4
2023 SCImago Journal Rankings: 1.011
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorZhang, Yan-
dc.contributor.authorTang, Xiaorong-
dc.contributor.authorYao, Ling-
dc.contributor.authorChen, Keying-
dc.contributor.authorJia, Wei-
dc.contributor.authorHu, Xiaofang-
dc.contributor.authorXu, Lisa X.-
dc.date.accessioned2024-04-17T07:03:35Z-
dc.date.available2024-04-17T07:03:35Z-
dc.date.issued2012-
dc.identifier.citationProteomics, 2012, v. 12, n. 1, p. 32-36-
dc.identifier.issn1615-9853-
dc.identifier.urihttp://hdl.handle.net/10722/342406-
dc.description.abstractSecreted 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 study, 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, and 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 upregulated 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 the 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. © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.-
dc.languageeng-
dc.relation.ispartofProteomics-
dc.subjectBreast cancer-
dc.subjectCell secretome-
dc.subjectConditioned medium-
dc.subjectLectin affinity capture-
dc.subjectTechnology-
dc.titleLectin capture strategy for effective analysis of cell secretome-
dc.typeArticle-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1002/pmic.201100323-
dc.identifier.pmid22065611-
dc.identifier.scopuseid_2-s2.0-84855430076-
dc.identifier.volume12-
dc.identifier.issue1-
dc.identifier.spage32-
dc.identifier.epage36-
dc.identifier.eissn1615-9861-
dc.identifier.isiWOS:000298841000006-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats