کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10159607 | 54 | 2013 | 12 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Artificial extracellular matrix composed of collagen I and highly sulfated hyaluronan interferes with TGFβ1 signaling and prevents TGFβ1-induced myofibroblast differentiation
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
بیو مهندسی (مهندسی زیستی)
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Artificial extracellular matrix composed of collagen I and highly sulfated hyaluronan interferes with TGFβ1 signaling and prevents TGFβ1-induced myofibroblast differentiation Artificial extracellular matrix composed of collagen I and highly sulfated hyaluronan interferes with TGFβ1 signaling and prevents TGFβ1-induced myofibroblast differentiation](/preview/png/10159607.png)
چکیده انگلیسی
Sulfated glycosaminoglycans are promising components for functional biomaterials since sulfate groups modulate the binding of growth factors and thereby influence wound healing. Here, we have investigated the influence of an artificial extracellular matrix (aECM) consisting of collagen I (coll) and hyaluronan (HA) or highly sulfated HA (hsHA) on dermal fibroblasts (dFb) with respect to their differentiation into myofibroblasts (MFb). Fibroblasts were cultured on aECM in the presence of aECM-adsorbed or soluble transforming growth factor β1 (TGFβ1). The synthesis of α-smooth muscle actin (αSMA), collagen and the ED-A splice variant of fibronectin (ED-A FN) were analyzed at the mRNA and protein levels. Furthermore, we investigated the bioactivity and signal transduction of TGFβ1 in the presence of aECM and finally made interaction studies of soluble HA or hsHA with TGFβ1. Artificial ECM composed of coll and hsHA prevents TGFβ1-stimulated αSMA, collagen and ED-A FN expression. Our data suggest an impaired TGFβ1 bioactivity and downstream signaling in the presence of aECM containing hsHA, shown by massively reduced Smad2/3 translocation to the nucleus. These data are explained by in silico docking experiments demonstrating the occupation of the TGFβ-receptor I binding site by hsHA. Possibly, HA sulfation has a strong impact on TGFβ1-driven differentiation of dFb and thus could be used to modulate the properties of biomaterials.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Acta Biomaterialia - Volume 9, Issue 8, August 2013, Pages 7775-7786
Journal: Acta Biomaterialia - Volume 9, Issue 8, August 2013, Pages 7775-7786
نویسندگان
Anja van der Smissen, Sergey Samsonov, Vera Hintze, Dieter Scharnweber, Stephanie Moeller, Matthias Schnabelrauch, M. Teresa Pisabarro, Ulf Anderegg,