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Strategies for the purification of laminin‐10 for studies on colon cancer metastasis
Author(s) -
Zamurs Laura,
Pouliot Normand,
Gibson Peter,
Hocking Glenn,
Nice Edouard
Publication year - 2003
Publication title -
biomedical chromatography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.4
H-Index - 65
eISSN - 1099-0801
pISSN - 0269-3879
DOI - 10.1002/bmc.248
Subject(s) - laminin , integrin , metastasis , colorectal cancer , epidermal growth factor , chemistry , receptor , immunohistochemistry , epidermal growth factor receptor , microbiology and biotechnology , cancer research , adhesion , cell adhesion , cell migration , cancer , cell , biology , biochemistry , immunology , medicine , organic chemistry
Abstract Signals from the epidermal growth factor (EGF) receptor family are thought to combine with integrin‐dependent adhesion to laminins to contribute to disease progression and metastasis in cancer. To date, little is known about the mechanisms by which these signals interact. Recently, we have shown that the colon cancer cell line LIM1215 secretes and adheres to laminin‐10 through multiple integrin receptors, and that EGF stimulates spreading and migration of these cells on the same substrate. Additionally laminin‐10/11 has been shown by immunohistochemistry to be present at the invasive edge of moderately differentiated colon cancers. To enable detailed structure–function studies to be undertaken, it is important to be able to rapidly obtain highly purified native laminin‐10 from bulk biological samples in reasonable yield. The development of a multidimensional micropurification scheme to achieve this is presented and compared with other reported methods for the purification of laminins. Copyright © 2003 John Wiley & Sons, Ltd.