Enhanced smooth muscle cell adhesion and proliferation on protein-modified polycaprolactone-based copolymers

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.

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Corrigendum: “Polymers with nano‐dimensional surface features enhance bladder smooth muscle cell adhesion”

Journal of Biomedical Materials Research Part A ◽

10.1002/jbm.a.37054 ◽

2020 ◽

Vol 109 (1) ◽

pp. 123-123

Author(s):

Anil Thapa ◽

Thomas J. Webster ◽

Karen M. Haberstroh

Keyword(s):

Smooth Muscle ◽

Cell Adhesion ◽

Smooth Muscle Cell ◽

Muscle Cell ◽

Bladder Smooth Muscle ◽

Surface Features ◽

Bladder Smooth Muscle Cell ◽

Dimensional Surface

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Rare Copy Number Variants Disrupt Genes Regulating Vascular Smooth Muscle Cell Adhesion and Contractility in Sporadic Thoracic Aortic Aneurysms and Dissections

The American Journal of Human Genetics ◽

10.1016/j.ajhg.2010.09.015 ◽

2010 ◽

Vol 87 (6) ◽

pp. 743-756 ◽

Cited By ~ 52

Author(s):

Siddharth K. Prakash ◽

Scott A. LeMaire ◽

Dong-Chuan Guo ◽

Ludivine Russell ◽

Ellen S. Regalado ◽

...

Keyword(s):

Smooth Muscle ◽

Cell Adhesion ◽

Vascular Smooth Muscle ◽

Smooth Muscle Cell ◽

Muscle Cell ◽

Vascular Smooth Muscle Cell ◽

Copy Number ◽

Copy Number Variants ◽

Aortic Aneurysms ◽

Thoracic Aortic Aneurysms

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

AJP Cell Physiology ◽

10.1152/ajpcell.00327.2013 ◽

2014 ◽

Vol 306 (8) ◽

pp. C753-C761 ◽

Cited By ~ 25

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.

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