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Published March 8, 2004 | public
Journal Article

Comparative Cell Response to Artificial Extracellular Matrix Proteins Containing the RGD and CS5 Cell-Binding Domains

Abstract

This study addresses endothelial cell adhesion and spreading on a family of artificial extracellular matrix (aECM) proteins designed for application in small-diameter vascular grafts. The aECM proteins contain domains derived from elastin and from fibronectin. aECM 1 contains the RGD sequence from the tenth type III domain of fibronectin; aECM 3 contains the fibronectin CS5 cell-binding domain. Negative control proteins aECM 2 and 4 are scrambled versions of aECM 1 and 3, respectively. Competitive peptide inhibition studies and comparisons of positive and negative control proteins confirm that adhesion of HUVECs to aECM proteins 1 and 3 is sequence specific. When subjected to a normal detachment force of 780 pN, 3-fold more HUVECs remained adherent to aECM 1 than to aECM 3. HUVECs also spread more rapidly on aECM 1 than on aECM 3. These results (i) indicate that cellular responses to aECM proteins can be modulated through choice of cell-binding domain and (ii) recommend the RGD sequence for applications that require rapid endothelial cell spreading and matrix adhesion.

Additional Information

Copyright © 2004 American Chemical Society. Published In Issue March 08, 2004. Publication Date (Web): January 24, 2004. Received September 4, 2003. Revised Manuscript Received December 8, 2003. Acknowledgment. We thank Kathleen Di Zio for helpful discussions regarding the DNA cloning and protein purification, Anand Asthagiri for helpful discussions regarding the cell spreading studies, and Scott Fraser and Carole Lu for help with the fluorescence microscopy. This work was supported by NIH Grant 5 RO1 HL59987-03, NSF Grant BES-9901648, and a Whitaker graduate fellowship.

Additional details

Created:
August 19, 2023
Modified:
October 19, 2023