Key result
Smooth muscle progenitor cells preferentially adhere to fibronectin and collagen over vitronectin via beta1 integrins.
BACKGROUND: Recently, we identified circulating smooth muscle progenitor cells (SPCs) in human peripheral blood. The integrin profile of such progenitors is currently unknown and may affect their in vivo homing characteristics. In this study, we determined the integrin profile of vascular progenitors and SPC adhesion to extracellular matrix (ECM) proteins in vitro and in vivo. METHODS AND RESULTS: SPCs and endothelial progenitor cells (EPCs) were isolated from peripheral blood of healthy human subjects, and expression of surface integrins and adhesion to several vascular ECM proteins were determined. Homing of SPCs in vivo to specific ECM protein was determined by intracoronary infusion of fluorescent SPCs into porcine coronary arteries containing a fibronectin-coated mesh stent. SPCs had high expression of beta1 integrin, moderate expression of alpha1, low levels of alpha(v)beta3, and did not express alpha(v)beta5, beta2, alpha2beta1, or alpha4beta1 integrins. In contrast, EPCs had high expression of alpha2beta1, alpha(v)beta3, alpha(v)beta5, beta1, and alpha1 and minimal expression of alpha4beta1. Moreover, SPCs showed increased adherence to fibronectin and collagen type I compared with vitronectin, consistent with their integrin profile, and demonstrated a similar degree of in vivo attachment to fibronectin-coated mesh. CONCLUSIONS: These data for the first time show a spectrum of integrin expression on vascular progenitors and suggest the potential importance of integrins in mediating adherence of SPCs to specific ECM both in vitro and in vivo.
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Deb et al. (2004) studied Healthy subjects. Smooth muscle progenitor cells (SPCs) vs. Endothelial progenitor cells (EPCs) was evaluated on Expression of surface integrins and adhesion to vascular extracellular matrix proteins. Smooth muscle progenitor cells exhibited high expression of beta1 integrins and increased adherence to fibronectin and collagen type I compared to vitronectin, distinct from endothelial progenitors.
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