An Examination of Endothelial Cell Function on Substrates Modified with Immobilized Bioactive Peptides

  • Sean M. Carroll
  • Kay C. Dee
  • R. Bizios
  • Thomas T. Anderson
Part of the NATO ASI Series book series (NSSA, volume 281)

Abstract

Recent advances in molecular/cellular biology and biochemistry have elucidated the role that functional domains of adhesive proteins (such as Arginine-Glycine-Aspartic Acid-Serine (RGDS) of fibronectin, and Tyrosine-Isoleucine-Glycine-Serine-Arginine-Glycine (YIGSRG) of laminin) play in mediating cell adhesion to substrates. Interaction of anchorage-dependent cells (via integrin receptors) with adhesive peptides of chemical components of the extracellular matrix trigger intracellular signal pathways which, subsequently, promote specific cellular functions such as motility and proliferation, which are crucial to endothelialization of a vascular implant material. Biomaterials for implantation should promote, maintain and, generally simulate the critical, beneficial conditions of the physiological milieu present during the wound healing process. A vascular implant, for example, should be designed to promote cellular functions which synergistically lead to the desirable end result of complete endothelialization within a clinically acceptable time period while remaining free of thrombotic complications.

Keywords

Integrin Laminin 

Copyright information

© Plenum Press, New York 1996

Authors and Affiliations

  • Sean M. Carroll
    • 1
  • Kay C. Dee
    • 1
  • R. Bizios
    • 1
  • Thomas T. Anderson
    • 2
  1. 1.Department of Biomedical EngineeringRensselaer Polytechnic InstituteTroyUSA
  2. 2.Department of BiochemistryAlbany Medical CollegeAlbanyUSA

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