scholarly journals The bioactivity of composite Fmoc-RGDS-collagen gels

2014 ◽  
Vol 2 (9) ◽  
pp. 1222-1229 ◽  
Author(s):  
Ricardo M. Gouveia ◽  
Roanne R. Jones ◽  
Ian W. Hamley ◽  
Che J. Connon
Keyword(s):  
Structural Properties ◽  
Collagen Type ◽  
Cell Attachment ◽  
Collagen Type I ◽  
Type I ◽  
Collagen Gels ◽  
Mechanical And Structural Properties ◽  
Self Assembled

Collagen type-I gels incorporating self-assembled Fmoc-RGDS during polymerisation become functionalised, providing a scaffold for enhanced cell attachment and survival, and with improved mechanical and structural properties.

Bacterial Endotoxin Inhibits Migration, Attachment, and Orientation of Human Gingival Fibroblasts in vitro and Delays Collagen Gel Contraction

1987 ◽  
Vol 66 (9) ◽  
pp. 1449-1455 ◽  
Author(s):  
S. Pitaru ◽  
M. Soldinger ◽  
D. Madgar ◽  
Z. Metzger
Keyword(s):  
Collagen Type ◽  
Cell Attachment ◽  
Collagen Gel ◽  
Collagen Type I ◽  
Human Gingival Fibroblasts ◽  
Bacterial Endotoxin ◽  
Type I ◽  
Gingival Fibroblasts ◽  
Collagen Gels

The purpose of this study was to assess the effect of endotoxin adsorbed to dental surfaces and to collagen type I on the migration, attachment, and orientation of human gingival fibroblasts (HGF). Transversely cut porcine tooth root slices (RS), 200 μm thick, were prepared. Half of the RS obtained were partially demineralized in EDTA. Half of the demineralized and non-demineralized RS were incubated with 400 μg/mL of endotoxin for 24 hr, whereas the other half were maintained in PBS and served as controls. Experimental and control RS were placed on confluent layers of HFG and cultured for six days. Cell migration toward and cell attachment to the periphery of the RS and the formation of oriented cell sheets were assessed by means of photographic techniques. Additionally, six-day-old cultures were fixed and processed for SEM observation. In separate experiments, the effect of endotoxin on cell attachment to collagen type I and on contraction of three-dimensional collagen gels was assessed. It was found that: (i) bacterial endotoxin inhibited migration and attachment of HGF to both demineralized and non-demineralized cementum and interfered with the development of oriented cellular structure ; (ii) the inhibitory effect was significantly more pronounced for non-demineralized than for demineralized cementum; (iii) the morphology of HGF attached to endotoxin-treated dental surfaces was altered compared with that of their controls; and (iv) bacterial endotoxin inhibited cell attachment to collagen type I and delayed the contraction of collagen gel.

scholarly journals Collagen microarchitecture mechanically controls myofibroblast differentiation

2020 ◽  
Vol 117 (21) ◽  
pp. 11387-11398 ◽  
Author(s):  
Bo Ri Seo ◽  
Xingyu Chen ◽  
Lu Ling ◽  
Young Hye Song ◽  
Adrian A. Shimpi ◽  
...  
Keyword(s):  
Collagen Type ◽  
Collagen Type I ◽  
Type I ◽  
Myofibroblast Differentiation ◽  
Dependent Manner ◽  
Fibrillar Collagen ◽  
Collagen Gels ◽  
Gelation Temperature ◽  
Rheological Characterization ◽  
Fiber Thickness

Altered microarchitecture of collagen type I is a hallmark of wound healing and cancer that is commonly attributed to myofibroblasts. However, it remains unknown which effect collagen microarchitecture has on myofibroblast differentiation. Here, we combined experimental and computational approaches to investigate the hypothesis that the microarchitecture of fibrillar collagen networks mechanically regulates myofibroblast differentiation of adipose stromal cells (ASCs) independent of bulk stiffness. Collagen gels with controlled fiber thickness and pore size were microfabricated by adjusting the gelation temperature while keeping their concentration constant. Rheological characterization and simulation data indicated that networks with thicker fibers and larger pores exhibited increased strain-stiffening relative to networks with thinner fibers and smaller pores. Accordingly, ASCs cultured in scaffolds with thicker fibers were more contractile, expressed myofibroblast markers, and deposited more extended fibronectin fibers. Consistent with elevated myofibroblast differentiation, ASCs in scaffolds with thicker fibers exhibited a more proangiogenic phenotype that promoted endothelial sprouting in a contractility-dependent manner. Our findings suggest that changes of collagen microarchitecture regulate myofibroblast differentiation and fibrosis independent of collagen quantity and bulk stiffness by locally modulating cellular mechanosignaling. These findings have implications for regenerative medicine and anticancer treatments.

scholarly journals In vitro production of human dermal equivalent

2010 ◽  
Vol 63 (7-8) ◽  
pp. 459-464 ◽  
Author(s):  
Zoran Milosavljevic ◽  
Biljana Ljujic
Keyword(s):  
Vitamin C ◽  
Collagen Type ◽  
Collagen Type I ◽  
Type I ◽  
Collagen Gels ◽  
In Vitro Production ◽  
Dermal Equivalent ◽  
Enzymatic Dissociation ◽  
Vitro Production

Introduction. Human dermal tissue is composed of loose and dense connective tissue. Main cell populations are fibroblasts and the dominant fibers are built from collagen type I. The aim of our study was to determine the precise method and time frame for the in vitro production of human dermal equivalent and to investigate the effects of ratio of structural elements and vitamin C on characteristics of the engineered tissue. Material and methods. Primary isolation of the foreskin fibroblasts was performed by explant method and enzymatic dissociation. Various collagen gels were obtained by mixing cells (from 25x103 to 200x103/ml) and neutralized collagen type I (from 2 to 4 mg/ml), with or without vitamin C. The routine histological and morphometrical examination was performed. Results. Enzymatic dissociation of the foreskin proved to be a faster method for production of desired number of fibroblasts (7.5x105 for 4 days). The contraction of collagen-gels started from day one through day seven and was dependent on cell and collagen concentration with higher density gels being contracted to a greater extent, except for the lowest/highest values. The best result was achieved with 100x103 cells and 2 mg/ml collagen. Vitamin C at 50 ?g/ml had no effect on speed of tissue formation. Conclusion. A precise approach that mimic the in vivo conditions is needed for the in vitro production of the dermal equivalent suitable for the possible treatment of tissue defects. Nearly ten days are necessary from the donor tissue dissociation to the final product.

scholarly journals Modelling fibrillogenesis of collagen-mimetic molecules

2020 ◽  
Author(s):  
A. E. Hafner ◽  
N. G. Gyori ◽  
C. A. Bench ◽  
L. K. Davis ◽  
A. Šarić
Keyword(s):  
Extracellular Matrix ◽  
Electrostatic Interactions ◽  
Collagen Type ◽  
Collagen Type I ◽  
Coarse Grained ◽  
Cell Phenotype ◽  
Type I ◽  
Collagen Scaffolds ◽  
Crucial Component ◽  
Self Assembled

One of the most robust examples of self-assembly in living organisms is the formation of collagen architectures. Collagen type I molecules are a crucial component of the extracellular-matrix where they self-assemble into fibrils of well defined striped patterns. This striped fibrilar pattern is preserved across the animal kingdom and is important for the determination of cell phenotype, cell adhesion, and tissue regulation and signalling. The understanding of the physical processes that determine such a robust morphology of self-assembled collagen fibrils is currently almost completely missing. Here we develop a minimal coarse-grained computational model to identify the physical principles of the assembly of collagen-mimetic molecules. We find that screened electrostatic interactions can drive the formation of collagen-like filaments of well-defined striped morphologies. The fibril pattern is determined solely by the distribution of charges on the molecule and is robust to the changes in protein concentration, monomer rigidity, and environmental conditions. We show that the fibril pattern cannot be easily predicted from the interactions between two monomers, but is an emergent result of multi-body interactions. Our results can help address collagen remodelling in diseases and ageing, and guide the design of collagen scaffolds for biotechnological applications.Statement of SignificanceCollagen type I protein is the most abundant protein in mammals. It is a crucial component of the extracellular-matrix where it robustly self-assembles into fibrils of specific striped architectures that are crucial for the correct collagen function. The molecular features that determine such robust fibril architectures are currently not well understood. Here we develop a minimal coarse-grained model to connect the design of collagen-like molecules to the architecture of the resulting self-assembled fibrils. We find that the pattern of charged residues on the surface of molecules can drive the formation of collagen-like fibrils and fully control their architectures. Our findings can help understand changes in collagen architectures observed in diseases and guide the design of synthetic collagen scaffolds.

A Collagen Grafting on Hydroxyapatite to Enhancement of Bone Cell Attachment

2008 ◽  
Vol 396-398 ◽  
pp. 41-45
Author(s):  
D.W. Lee ◽  
E.J. Lee ◽  
Sung Su Chun ◽  
Myun Whan Ahn ◽  
I.W. Song ◽  
...  
Keyword(s):  
Collagen Type ◽  
Cell Attachment ◽  
Collagen Type I ◽  
Bone Cell ◽  
Major Constituent ◽  
Type I ◽  
Connective Tissues ◽  
Coating Materials ◽  
Attached Cell ◽  
Scanning Electron

A collagen material was chemically grafted on hydroxyapatite (HA) to enhance bone cell attachment because the collagen is a major constituent of connective tissues and has been regarded as one of the most excellent coating materials for bone bonding. First, HA disks were prepared with 12mm diameter and 1mm thickness. And then collagen (type I) was immobilbized on the HA surface using a 3-APTES coupling agent on HA disk surfaces. MC3T3-E1 osteoblasts were seeded on the collagen-grafted and non-grated HA disks and cultured for 4 hrs to evaluate the cell adhesion on the HA discs. The Attached cell morphology on discs was observed with a fluorescent optical microscopy (FOM) and a scanning electron microscopy (SEM). The osteoblasts on the collagen-grafted sample were more spread than those on the non-grafted sample. It is believed that collagen-grafted HA surface provides suitable sites for cell attaching due to the high biocompatibility of collagen.

scholarly journals Poly(NaSS) Functionalization Modulates the Conformation of Fibronectin and Collagen Type I To Enhance Osteoblastic Cell Attachment onto Ti6Al4V

Langmuir ◽  
2014 ◽  
Vol 30 (31) ◽  
pp. 9477-9483 ◽  
Author(s):  
Helena P. Felgueiras ◽  
Sven D. Sommerfeld ◽  
N. Sanjeeva Murthy ◽  
Joachim Kohn ◽  
Véronique Migonney
Keyword(s):  
Collagen Type ◽  
Cell Attachment ◽  
Collagen Type I ◽  
Osteoblastic Cell ◽  
Type I

scholarly journals MECHANICAL AND STRUCTURAL PROPERTIES OF COLLAGEN NANOFRIBROUS LAYERS UNDER SIMULATED BODY CONDITIONS

2019 ◽  
Vol 25 ◽  
pp. 73-78
Author(s):  
Jitka Říhová ◽  
Tomáš Suchý ◽  
Lucie Vištejnová ◽  
Lukáš Horný ◽  
Monika Šupová
Keyword(s):  
Structural Properties ◽  
Metabolic Activity ◽  
Cell Activity ◽  
Collagen Type I ◽  
Ethanol Solution ◽  
Dermal Fibroblasts ◽  
Molar Ratio ◽  
Assay Method ◽  
Type I ◽  
Mechanical And Structural Properties

The theme of this paper is the analysis of mechanical and structural properties of nanofibrous COL under simulated body conditions and in the presence of osteoblasts and dermal fibroblasts. COL were prepared by electrostatic spinning of 8wt% collagen type I dispersion with 8wt% (to COL) of PEG in phosphate buffer/ethanol solution (1/1vol). The stability of COL was enhanced by means of cross-linking with EDC and NHS at a molar ratio of 4:1. COL were exposed in culture medium for 21 days and human SAOS-2 human dermal fibroblasts and osteoblasts were cultured therein for 21 days as well. The cell culture on COL was assessed by fluorescence microscopy and metabolic activity. Then the metabolic activity of both cell types grown on COL and PS were measured after 1, 7, 14 and 21 days using the Alamar Blue assay method. Mechanical properties were determined using an tensile test. The influence of the cell activity on secondary structure of COL was verified by IR spectroscopy. Furthermore, the influence of cells on COL was evaluated by SEM.

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