ResearchFunctional Binding of Human Adipose-Derived Stromal Cells Effects of Extraction Method and Hypoxia PretreatmentAmos, Peter J. BS*‡; Bailey, Alexander M. BS*‡; Shang, Hulan PhD†; Katz, Adam J. MD†; Lawrence, Michael B. PhD*; Peirce, Shayn M. PhD*Author Information From the *Department of Biomedical Engineering, University of Virginia, Health System, Charlottesville, VA; and the †Department of Plastic and Reconstructive Surgery, University of Virginia, Charlottesville, VA. This work was supported by the University of Virginia Department of Biomedical Engineering. ‡These authors contributed equally to this paper. Reprints: Shayn M. Peirce, PhD, Department of Biomedical Engineering, PO Box 800759, Health System, Charlottesville, VA 22908. E-mail: [email protected]. Annals of Plastic Surgery: April 2008 - Volume 60 - Issue 4 - p 437-444 doi: 10.1097/SAP.0b013e318095a771 Buy Metrics Abstract Human adipose-derived stromal cells (hASCs) were evaluated in vitro for their ability to bind vascular adhesion and extracellular matrix proteins to arrest (firmly adhere) under physiological flow conditions. hASCs were flowed through a parallel plate flow chamber containing substrates presenting immobilized type I collagen, fibronectin, E-selectin, L-selectin, P-selectin, vascular cell adhesion molecule-1 (VCAM-1), or intercellular adhesion molecule-1 (ICAM-1) under static and laminar flow conditions (wall shear stress = 1 dyn/cm2). hASCs were able to firmly adhere to type I collagen, fibronectin, VCAM-1, and ICAM-1 substrates, but not to any of the selectins. Pretreatment with hypoxia increased the ability of hASCs isolated by liposuction to adhere to VCAM-1 and ICAM-1, but this effect was not seen in cells isolated by tissue excision. These results indicate that hASCs possess the ability to adhere key adhesion proteins, illustrate the importance of hASC harvest procedure, and suggest mechanisms for homing in a setting where interaction with inflamed or injured tissue is necessary. © 2008 Lippincott Williams & Wilkins, Inc.