Smooth muscle cell adhesion in surface-modified three-dimensional copolymer scaffolds prepared from co-continuous blends

2009 ◽  
Vol 91A (1) ◽  
pp. 305-315 ◽  
Author(s):  
Hanna Bramfeldt ◽  
Pierre Sarazin ◽  
Patrick Vermette
Keyword(s):  
Smooth Muscle ◽  
Cell Adhesion ◽  
Smooth Muscle Cell ◽  
Muscle Cell ◽  
Three Dimensional ◽  
Surface Modified

An In Vitro Study of Nano-fiber Polymers for Guided Vascular Regeneration

2001 ◽  
Vol 711 ◽  
Author(s):  
Derick C. Miller ◽  
Anil Thapa ◽  
Karen M. Haberstroh ◽  
Thomas J. Webster
Keyword(s):  
Smooth Muscle ◽  
Cell Adhesion ◽  
Smooth Muscle Cell ◽  
Muscle Cell ◽  
Surrounding Tissue ◽  
Arterial Smooth Muscle Cell ◽  
Arterial Smooth Muscle ◽  
Cell Functions ◽  
Fiber Dimensions

ABSTRACTBiomaterials that successfully integrate into surrounding tissue should match not only the tissue's mechanical properties, but also the dimensions of the associated nano-structured extra-cellular matrix (ECM) components. The goal of this research was to use these ideals to develop a synthetic, nano-structured, polymeric biomaterial that has cytocompatible and mechanical behaviors similar to that of natural vascular tissue. In a novel manner, poly-lactic acid/polyglycolic acid (PLGA) (50/50 wt.% mix) and polyurethane were separately synthesized to possess a range of fiber dimensions in the micron and nanometer regime. Preliminary results indicated that decreasing fiber diameter on both PLGA and PU enhanced arterial smooth muscle cell adhesion; specifically, arterial smooth muscle cell adhesion increased 23% when PLGA fiber dimensions decreased from 500 to 50 nm and increased 76% on nano-structured, compared to conventional structured, polyurethane. However, nano-structured PLGA decreased endothelial cell adhesion by 52%, whereas adhesion of these same cells was increased by 50% on polyurethane. For these reasons, the present in vitro study provides the first evidence that polymer fiber dimensions can be used to selectively control cell functions for vascular prosthesis.

scholarly journals Role of c-Abl tyrosine kinase in smooth muscle cell migration

2014 ◽  
Vol 306 (8) ◽  
pp. C753-C761 ◽  
Author(s):  
Rachel A. Cleary ◽  
Ruping Wang ◽  
Omar Waqar ◽  
Harold A. Singer ◽  
Dale D. Tang
Keyword(s):  
Smooth Muscle ◽  
Cell Migration ◽  
Cell Adhesion ◽  
Smooth Muscle Cell ◽  
Muscle Cell ◽  
Leading Edge ◽  
Actin Dynamics ◽  
Cell Edge ◽  
Smooth Muscle Cell Migration

c-Abl is a nonreceptor protein tyrosine kinase that has a role in regulating smooth muscle cell proliferation and contraction. The role of c-Abl in smooth muscle cell migration has not been investigated. In the present study, c-Abl was found in the leading edge of smooth muscle cells. Knockdown of c-Abl by RNA interference attenuated smooth muscle cell motility as evidenced by time-lapse microscopy. Furthermore, the actin-associated proteins cortactin and profilin-1 (Pfn-1) have been implicated in cell migration. In this study, cell adhesion induced cortactin phosphorylation at Tyr-421, an indication of cortactin activation. Phospho-cortactin and Pfn-1 were also found in the cell edge. Pfn-1 directly interacted with cortactin in vitro. Silencing of c-Abl attenuated adhesion-induced cortactin phosphorylation and Pfn-1 localization in the cell edge. To assess the role of cortactin/Pfn-1 coupling, we developed a cell-permeable peptide. Treatment with the peptide inhibited the interaction of cortactin with Pfn-1 without affecting cortactin phosphorylation. Moreover, treatment with the peptide impaired the recruitment of Pfn-1 to the leading edge and cell migration. Finally, β1-integrin was required for the recruitment of c-Abl to the cell edge. Inhibition of actin dynamics impaired the spatial distribution of c-Abl. These results suggest that β1-integrin may recruit c-Abl to the leading cell edge, which may regulate cortactin phosphorylation in response to cell adhesion. Phosphorylated cortactin may facilitate the recruitment of Pfn-1 to the cell edge, which promotes localized actin polymerization, leading edge formation, and cell movement. Conversely, actin dynamics may strengthen the recruitment of c-Abl to the leading edge.

Sign in / Sign up

Export Citation Format

Share Document