Preliminary Results of In Vitro Study of Cell Growth in a 45S5 Bioactive Glass as Bone Substitute Using Scanning Electron and Confocal Microscopies

2007 ◽  
Vol 361-363 ◽  
pp. 1111-1114 ◽  
Author(s):  
Rami Maksoud ◽  
Leila Lefebvre ◽  
Laurence Heinrich ◽  
Laurent Gremillard ◽  
Jérôme Chevalier ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Cell Growth ◽  
Confocal Microscopy ◽  
Bioactive Glass ◽  
Bone Substitute ◽  
Type I ◽  
Matrix Deposition ◽  
Extracellular Matrix Components ◽  
Extracellular Matrix Deposition ◽  
Scanning Electron

The aim of this study was to evaluate the cytocompatibility, cell ingrowth and extracellular matrix deposition of a newly developed porous bioactive glass as a bone substitute. Two types of bioactive glass, different in their pore size (75 and 20 ppi, resp. ~350 and ~1200 $m), were used in this study. The materials were seeded with human osteoblastic (MG63) and fibroblastic (M-228 F01 and M-191 F01) cell lines. The cells were visualized by two techniques, scanning electron microscopy and confocal microscopy. For confocal microscopy cell nuclei were labeled with propidium iodide (IP) and the extracellular matrix components (type I collagen and osteocalcin) by specific antibodies. Cells and matrix were visualized by fluorescence. The bioactive glass used in this study was shown to be non cytotoxic. Cell growth and colonization at the surface and in the depth of the material were observed. Extracellular matrix deposition was also demonstrated which proved the proper biofunctionality of the biomaterial. Scanning electron microscope allowed us to visualize cells at a high magnification at the surface of the bioglass and evidenced that the biomaterials were covered by a sheet of cells with their matrix; on the other hand, confocal microscopy permitted us to observe cell ingrowth and matrix deposition within the depth of the substitute. We showed that extracellular matrix was synthesized mainly in the upper levels where the cell population was the most confluent. In summary, this porous bioglass appears promising for bone substitution.

scholarly journals Extracellular Matrix Deposition and Remodeling after Corneal Alkali Burn in Mice

2021 ◽  
Vol 22 (11) ◽  
pp. 5708
Author(s):  
Kazadi N. Mutoji ◽  
Mingxia Sun ◽  
Garrett Elliott ◽  
Isabel Y. Moreno ◽  
Clare Hughes ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Dermatan Sulfate ◽  
Temporal Distribution ◽  
Keratan Sulfate ◽  
Collagen Fibrils ◽  
Type I ◽  
Chemical Injury ◽  
Matrix Deposition ◽  
Alkali Burn ◽  
Extracellular Matrix Deposition

Corneal transparency relies on the precise arrangement and orientation of collagen fibrils, made of mostly Type I and V collagen fibrils and proteoglycans (PGs). PGs are essential for correct collagen fibrillogenesis and maintaining corneal homeostasis. We investigated the spatial and temporal distribution of glycosaminoglycans (GAGs) and PGs after a chemical injury. The chemical composition of chondroitin sulfate (CS)/dermatan sulfate (DS) and heparan sulfate (HS) were characterized in mouse corneas 5 and 14 days after alkali burn (AB), and compared to uninjured corneas. The expression profile and corneal distribution of CS/DSPGs and keratan sulfate (KS) PGs were also analyzed. We found a significant overall increase in CS after AB, with an increase in sulfated forms of CS and a decrease in lesser sulfated forms of CS. Expression of the CSPGs biglycan and versican was increased after AB, while decorin expression was decreased. We also found an increase in KS expression 14 days after AB, with an increase in lumican and mimecan expression, and a decrease in keratocan expression. No significant changes in HS composition were noted after AB. Taken together, our study reveals significant changes in the composition of the extracellular matrix following a corneal chemical injury.

scholarly journals Giantin is required for intracellular N-terminal processing of type I procollagen

2020 ◽  
Author(s):  
Nicola L. Stevenson ◽  
J. M. Bergen Dylan ◽  
Chrissy L. Hammond ◽  
David J. Stephens
Keyword(s):  
Extracellular Matrix ◽  
Type I Collagen ◽  
Fish Analysis ◽  
Type I ◽  
Matrix Assembly ◽  
Matrix Deposition ◽  
Type I Procollagen ◽  
Main Protein ◽  
Extracellular Matrix Deposition ◽  
Craniofacial Defects

AbstractKnockout of the golgin giantin leads to skeletal and craniofacial defects driven by poorly studied changes in glycosylation and extracellular matrix deposition. Here, we sought to determine how giantin impacts the production of healthy bone tissue by focussing on the main protein component of the osteoid, type I collagen. Giantin mutant zebrafish accumulate multiple spontaneous fractures in their caudal fin, suggesting their bones may be more brittle. Inducing new experimental fractures revealed defects in the mineralisation of newly deposited collagen as well as diminished procollagen reporter expression in mutant fish. Analysis of giantin knockout cells expressing a GFP-tagged procollagen showed that procollagen trafficking is independent of giantin. However, our data show that intracellular N-propeptide processing of pro-α1(I) is defective in the absence of giantin. These data demonstrate a conserved role for giantin in collagen biosynthesis and extracellular matrix assembly. Our work also provides evidence of a giantin-dependent pathway for intracellular procollagen processing.

scholarly journals The extracellular matrix of the lung and its role in edema formation

2007 ◽  
Vol 79 (2) ◽  
pp. 285-297 ◽  
Author(s):  
Paolo Pelosi ◽  
Patricia R.M. Rocco ◽  
Daniela Negrini ◽  
Alberto Passi
Keyword(s):  
Extracellular Matrix ◽  
Three Dimensional ◽  
Protective Role ◽  
Lung Edema ◽  
Type I ◽  
Matrix Remodeling ◽  
Edema Formation ◽  
Surface Receptors ◽  
Matrix Deposition ◽  
Extracellular Matrix Components

The extracellular matrix is composed of a three-dimensional fiber mesh filled with different macromolecules such as: collagen (mainly type I and III), elastin, glycosaminoglycans, and proteoglycans. In the lung, the extracellular matrix has several functions which provide: 1) mechanical tensile and compressive strength and elasticity, 2) low mechanical tissue compliance contributing to the maintenance of normal interstitial fluid dynamics, 3) low resistive pathway for an effective gas exchange, d) control of cell behavior by the binding of growth factors, chemokines, cytokines and the interaction with cell-surface receptors, and e) tissue repair and remodeling. Fragmentation and disorganization of extracellular matrix components comprises the protective role of the extracellular matrix, leading to interstitial and eventually severe lung edema. Thus, once conditions of increased microvascular filtration are established, matrix remodeling proceeds fairly rapidly due to the activation of proteases. Conversely, a massive matrix deposition of collagen fiber decreases interstitial compliance and therefore makes the tissue safety factor stronger. As a result, changes in lung extracellular matrix significantly affect edema formation and distribution in the lung.

Fat-Soluble Vitamins Affect Composition of Extracellular Matrix Deposited by Human Aortic Smooth Muscle and Endothelial Cells In Vitro

2020 ◽  
Vol 19 (1) ◽  
pp. 36-45
Author(s):  
V. Ivanov ◽  
S. Ivanova ◽  
A. Niedzwiecki ◽  
M. Rath
Keyword(s):  
Extracellular Matrix ◽  
Endothelial Cells ◽  
Smooth Muscle ◽  
Type Iv Collagen ◽  
Type I ◽  
Aortic Smooth Muscle ◽  
Matrix Deposition ◽  
Type Iv ◽  
Extracellular Matrix Deposition ◽  
Fat Soluble Vitamins

Atherosclerotic cardiovascular disease is accompanied by changes in arterial connective tissue. We evaluated the effects of fat-soluble vitamins A, D, and E individually and in combinations on the composition of extracellular matrix produced and deposited by arterial wall cells, human aortic smooth muscle cells, and endothelial cells. Individually, vitamins D and E stimulated collagen type I extracellular matrix deposition in human aortic smooth muscle cell cultures. However, vitamins A, D, and E reduced collagen type IV deposition by human aortic smooth muscle cell, counteracting the stimulatory effects of vitamin C. The extracellular matrix deposition of heparan sulfate by human aortic smooth muscle cells increased by vitamin C and its combination (C+D+E). β-carotene + D + C induced the extracellular matrix deposition of collagen I by endothelial cells. Vitamin E with other vitamins resulted in either induction (E+C+A) or inhibition (E+D). The extracellular matrix deposition of type IV collagen and elastin by human aortic endothelial cells was not affected by test vitamins, except the extracellular matrix type IV collagen decrease by combinations (A+E), (A+D+E), and (C+D+E). The extracellular matrix deposition of all tested glycosaminoglycans was reduced by vitamin A and its combination (A+C+D+E). Therefore, the fat-soluble vitamins applied individually or in combination—both with each other or with ascorbic acid—can affect extracellular matrix deposition of type I and IV collagens, and key glycosaminoglycans by cultured human aortic arterial wall cells.

scholarly journals Giantin is required for intracellular N-terminal processing of type I procollagen

2021 ◽  
Vol 220 (6) ◽  
Author(s):  
Nicola L. Stevenson ◽  
Dylan J.M. Bergen ◽  
Yinhui Lu ◽  
M. Esther Prada-Sanchez ◽  
Karl E. Kadler ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Type I Collagen ◽  
Fish Analysis ◽  
Type I ◽  
Matrix Assembly ◽  
Matrix Deposition ◽  
Type I Procollagen ◽  
Main Protein ◽  
Extracellular Matrix Deposition ◽  
Craniofacial Defects

Knockout of the golgin giantin leads to skeletal and craniofacial defects driven by poorly studied changes in glycosylation and extracellular matrix deposition. Here, we sought to determine how giantin impacts the production of healthy bone tissue by focusing on the main protein component of the osteoid, type I collagen. Giantin mutant zebrafish accumulate multiple spontaneous fractures in their caudal fin, suggesting their bones may be more brittle. Inducing new experimental fractures revealed defects in the mineralization of newly deposited collagen as well as diminished procollagen reporter expression in mutant fish. Analysis of a human giantin knockout cell line expressing a GFP-tagged procollagen showed that procollagen trafficking is independent of giantin. However, our data show that intracellular N-propeptide processing of pro-α1(I) is defective in the absence of giantin. These data demonstrate a conserved role for giantin in collagen biosynthesis and extracellular matrix assembly. Our work also provides evidence of a giantin-dependent pathway for intracellular procollagen processing.

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