Use of an Immobilized Monoclonal Antibody to Examine Integrin α5β1 Signaling Independent of Cell Spreading

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Author: Bao, W
Author: Strömblad, S
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Use of an Immobilized Monoclonal Antibody to Examine Integrin α5β1 Signaling Independent of Cell Spreading

Wenjie Bao¹^* and Staffan Strömblad¹

¹ Karolinska Institutet, Department of Microbiology, Pathology and Immunology. Huddinge University Hospital F46, SE-141 86 Huddinge. Sweden. Phone: 46-8-58581036 Fax: 46-8-58581020

* To whom correspondence should be addressed: Wenjie Bao, Karolinska Institutet, Department of Microbiology, Pathology and Immunology. Huddinge University Hospital F46, SE-141 86 Huddinge. Sweden. Phone: 46-8-58581036. Fax: 46-8-58581020. Email: wenjie.bao@impi.ki.se

Biol. Proced. Online 2002;4:81-87. doi:10.1251/bpo37
Submitted: September 12, 2002; Accepted: October 15, 2002; Published: November 11, 2002.

Indexing terms: cell adhesion; integrins; antibodies, monoclonal; fibronectins; protein kinases.

Figure 2 Enlarged

Fig. 2:

Immobilized anti-integrin mabs rapidly down-regulate protein levels of the Cdk2- inhibitors p21CIP1 and p27KIP1. ECV 304 cells were plated onto FN, anti-integrin mabs P4C10 (anti-β1), LM609 (anti-αvβ3) or JBS5 (anti-α5β1) or onto poly-L-lysine (P-L-L) that mediates integrin-independent cell attachment. The protein levels of the Cdk2-inhibitors p21CIP1 and p27KIP1 were determined by Western blotting. Actin levels were analyzed as a loading control.

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