| Fetuin-A ({alpha}2HS-glycoprotein) is a major serum adhesive protein that mediates growth signaling in breast tumor cells. | |
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MedLine Citation:
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PMID: 20956534 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The identity of the cell adhesive factors in fetal bovine serum, commonly used to supplement growth media, remains a mystery due to the plethora of serum proteins. In the present analyses, we showed that fetuin-A, whose function in cellular attachment in tissue culture has been debated for many years, is indeed a major serum cell attachment factor particularly for tumor cells. We are able to report this because of a new purification strategy that has for the first time given us a homogeneous protein band in colloidal Coomassie-stained gels that retains biological activity. The tumor cells adhered to immobilized fetuin-A and not α(2)-macroglobulin, its major contaminant. The interaction of cells with fetuin-A was driven mainly by Ca(2+) ions, and cells growing in regular medium supplemented with fetal bovine serum were just as sensitive to loss of extracellular Ca(2+) ions as cells growing in fetuin-A. Fractionation of human serum revealed that cell attachment was confined to the fractions that had fetuin-A. Interestingly, the tumor cells also took up fetuin-A and secreted it back to the medium using an unknown mechanism that can be observed in live cells. The attachment of tumor cells to fetuin-A was accompanied by phosphatidylinositol 3-kinase/Akt activation that was down-regulated in cells that lack annexin-A6, one of the cell surface receptors for fetuin-A. Taken together, our data show the significance of fetuin-A in tumor cell growth mechanisms in vitro and open new research vistas for this protein. |
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Authors:
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Amos M Sakwe; Rainelli Koumangoye; Shawn J Goodwin; Josiah Ochieng |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S. Date: 2010-10-18 |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 285 ISSN: 1083-351X ISO Abbreviation: J. Biol. Chem. Publication Date: 2010 Dec |
Date Detail:
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Created Date: 2010-12-27 Completed Date: 2011-02-09 Revised Date: 2013-05-27 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
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Languages: eng Pagination: 41827-35 Citation Subset: IM |
Affiliation:
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Department of Biochemistry and Cancer Biology, Meharry Medical College, Nashville, Tennessee 37208, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Blood Proteins
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chemistry* Breast Neoplasms / metabolism, pathology* Calcium / chemistry Cell Adhesion Cell Membrane / metabolism Cell Proliferation Gene Expression Regulation, Neoplastic* Glycerol / chemistry Green Fluorescent Proteins / chemistry Humans Ions MAP Kinase Signaling System Phosphatidylinositol 3-Kinases / metabolism Signal Transduction* alpha-2-HS-Glycoprotein alpha-Fetoproteins / chemistry* |
| Grant Support | |
ID/Acronym/Agency:
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1SC1CA134018-01/CA/NCI NIH HHS; 5U54NS041071/NS/NINDS NIH HHS; G12RR03032-19/RR/NCRR NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/AHSG protein, human; 0/Blood Proteins; 0/Ions; 0/alpha-2-HS-Glycoprotein; 0/alpha-Fetoproteins; 147336-22-9/Green Fluorescent Proteins; 56-81-5/Glycerol; 7440-70-2/Calcium; EC 2.7.1.-/Phosphatidylinositol 3-Kinases |
| Comments/Corrections | |
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