scholarly journals Osteopontin regulates type I collagen fibril formation in bone tissue

2020 ◽  
Author(s):  
Baptiste Depalle ◽  
Catriona M. McGilvery ◽  
Sabah Nobakhti ◽  
Nouf Aldegaither ◽  
Sandra J. Shefelbine ◽  
...  
Keyword(s):  
Bone Tissue ◽  
Collagen Fibril ◽  
Type I Collagen ◽  
Fibril Formation ◽  
Type I

scholarly journals The Mammalian Chitinase-like Lectin, YKL-40, Binds Specifically to Type I Collagen and Modulates the Rate of Type I Collagen Fibril Formation

2006 ◽  
Vol 281 (30) ◽  
pp. 21082-21095 ◽  
Author(s):  
Heather F. Bigg ◽  
Robin Wait ◽  
Andrew D. Rowan ◽  
Tim E. Cawston
Keyword(s):  
Collagen Fibril ◽  
Type I Collagen ◽  
Fibril Formation ◽  
Type I

Effect of UV irradiation on type I collagen fibril formation in neutral collagen solutions

2001 ◽  
Vol 17 (3) ◽  
pp. 114-120 ◽  
Author(s):  
Julian M. Menter ◽  
Abrienne M. Patta ◽  
Robert M. Sayre ◽  
John Dowdy ◽  
Isaac Willis
Keyword(s):  
Uv Irradiation ◽  
Collagen Fibril ◽  
Type I Collagen ◽  
Fibril Formation ◽  
Type I

Characterization of Type I Collagen Fibril Formation Using Thioflavin T Fluorescent Dye

2009 ◽  
Vol 145 (5) ◽  
pp. 677-684 ◽  
Author(s):  
K. Morimoto ◽  
K. Kawabata ◽  
S. Kunii ◽  
K. Hamano ◽  
T. Saito ◽  
...  
Keyword(s):  
Collagen Fibril ◽  
Type I Collagen ◽  
Fibril Formation ◽  
Fluorescent Dye ◽  
Thioflavin T ◽  
Type I

scholarly journals Structure–function studies on Hsp47: pH-dependent inhibition of collagen fibril formation in vitro

2000 ◽  
Vol 349 (3) ◽  
pp. 877-883 ◽  
Author(s):  
Christy A. THOMSON ◽  
Vettai S. ANANTHANARAYANAN
Keyword(s):  
Endoplasmic Reticulum ◽  
Collagen Fibril ◽  
Type I Collagen ◽  
Fibril Formation ◽  
Molar Ratio ◽  
Functional Assay ◽  
Type I ◽  
Ph Dependent ◽  
Ph Range

Hsp47, a 47kDa heat shock protein whose expression level parallels that of collagen, has been regarded as a collagen-specific molecular chaperone. Studies from other laboratories have established the association of Hsp47 with the nascent as well as the triple-helical procollagen molecule in the endoplasmic reticulum and its dissociation from procollagen in the Golgi. One of several roles suggested for Hsp47 in collagen biosynthesis is the prevention of aggregation of procollagen in the endoplasmic reticulum. However, no experimental evidence has been available to verify this suggestion. In the present study we have followed the aggregation of mature triple-helical collagen molecules into fibrils by using turbidimetric measurements in the absence and presence of Hsp47. In the pH range 6–7, fibril formation of type I collagen, as monitored by turbidimetry, proceeds with a lag of approx. 10min and levels off by approx. 60min. The addition of Hsp47 at pH 7 effectively inhibits fibril formation at and above a 1:1 molar ratio of Hsp47 to triple-helical collagen. This inhibition is markedly pH-dependent, being significantly diminished at pH 6. CD and fluorescence spectral data of Hsp47 in the pH range 4.2–7.4 reveal a significant alteration in its structure at pH values below 6.2, with a decrease in α-helix and an increase in β-structure. This conformational change is likely to be the basis of the decreased binding of Hsp47 to collagen in vitro at pH 6.3 as well as its inability to inhibit collagen fibril formation at this pH. Our results also provide a functional assay for Hsp47 that can be used in studies on collagen and Hsp47 interactions.

scholarly journals Structural Property of Decorin from Small Intestine and its Effect of Type I Collagen Fibril Formation

1998 ◽  
Vol 69 (8) ◽  
pp. 779-791
Author(s):  
Yoshihiro NOMURA ◽  
Takahiro MIZUTANI ◽  
Yasuhiro ISHII ◽  
Kunio SHIRAI
Keyword(s):  
Small Intestine ◽  
Structural Property ◽  
Collagen Fibril ◽  
Type I Collagen ◽  
Fibril Formation ◽  
Type I

Phosphorylated chitosan to promote biomimetic mineralization of type I collagen as a strategy for dentin repair and bone tissue engineering

2019 ◽  
Vol 43 (4) ◽  
pp. 2002-2010 ◽  
Author(s):  
Bo Zheng ◽  
Caiyun Mao ◽  
Tianyi Gu ◽  
Haihua Pan ◽  
Changyu Shao ◽  
...  
Keyword(s):  
Tissue Engineering ◽  
Bone Tissue Engineering ◽  
Bone Tissue ◽  
Efficient Method ◽  
Type I Collagen ◽  
Type I ◽  
Biomimetic Mineralization ◽  
Mineralized Matrix

This novel biomimetic mineralization technique provides an efficient method to produce an advanced mineralized matrix.

scholarly journals Actinidain-hydrolyzed Type I Collagen Reveals a Crucial Amino Acid Sequence in Fibril Formation

2010 ◽  
Vol 285 (23) ◽  
pp. 17465-17470 ◽  
Author(s):  
Saori Kunii ◽  
Koichi Morimoto ◽  
Kouhei Nagai ◽  
Takuya Saito ◽  
Kenji Sato ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Type I Collagen ◽  
Fibril Formation ◽  
Type I

scholarly journals Development and Biocompatibility of Collagen-Based Composites Enriched with Nanoparticles of Strontium Containing Mesoporous Glass

Materials ◽  
2019 ◽  
Vol 12 (22) ◽  
pp. 3719 ◽  
Author(s):  
Giorgia Montalbano ◽  
Giorgia Borciani ◽  
Carlotta Pontremoli ◽  
Gabriela Ciapetti ◽  
Monica Mattioli-Belmonte ◽  
...  
Keyword(s):  
Tissue Engineering ◽  
Bone Tissue Engineering ◽  
Bone Tissue ◽  
Type I Collagen ◽  
Bone Tissue Regeneration ◽  
In Vitro Tests ◽  
Type I ◽  
Natural Polymers ◽  
Bioactive Glasses ◽  
Composition And Structure

In the last years bone tissue engineering has been increasingly indicated as a valid solution to meet the challenging requirements for a healthy bone regeneration in case of bone loss or fracture. In such a context, bioactive glasses have already proved their great potential in promoting the regeneration of new bone tissue due to their high bioactivity. In addition, their composition and structure enable us to incorporate and subsequently release therapeutic ions such as strontium, enhancing the osteogenic properties of the material. The incorporation of these inorganic systems in polymeric matrices enables the formulation of composite systems suitable for the design of bone scaffolds or delivery platforms. Among the natural polymers, type I collagen represents the main organic phase of bone and thus is a good candidate to develop biomimetic bioactive systems for bone tissue regeneration. However, alongside the specific composition and structure, the key factor in the design of new biosystems is creating a suitable interaction with cells and the host tissue. In this scenario, the presented study aimed at combining nano-sized mesoporous bioactive glasses produced by means of a sol–gel route with type I collagen in order to develop a bioactive hybrid formulation suitable for bone tissue engineering applications. The designed system has been fully characterized in terms of physico-chemical and morphological analyses and the ability to release Sr2+ ions has been studied observing a more sustained profile in presence of the collagenous matrix. With the aim to improve the mechanical and thermal stability of the resulting hybrid system, a chemical crosslinking approach using 4-star poly (ethylene glycol) ether tetrasuccinimidyl glutarate (4-StarPEG) has been explored. The biocompatibility of both non-crosslinked and 4-StarPEG crosslinked systems was evaluated by in vitro tests with human osteoblast-like MG-63 cells. Collected results confirmed the high biocompatibility of composites, showing a good viability and adhesion of cells when cultured onto the biomaterial samples.

Stability of the Magnesium Carbonate Apatite/Anionic Collagen Scaffolds: Effect of the Cross-Link Concentration

2011 ◽  
Vol 493-494 ◽  
pp. 844-848 ◽  
Author(s):  
Marcia S. Sader ◽  
Gutemberg Alves ◽  
Racquel Z. LeGeros ◽  
Gloria Dulce de Almeida Soares
Keyword(s):  
Bone Tissue ◽  
Culture Medium ◽  
Type I Collagen ◽  
Type I ◽  
Carbonate Apatite ◽  
Reaction Products ◽  
Collagen Scaffolds ◽  
Freeze Dried ◽  
The Cross

Natural bone constitutes of an inorganic phase (a biological nanoapatite) and an organic phase (mostly type I collagen). The challenge is to develop a material that can regenerate lost bone tissue with degradation and resorption kinetics compatible with the new bone formation. The aim of this study was to prepare self-organized magnesium and carbonate substituted apatite/collagen scaffolds, cross-linked with glutaraldehyde (GA). Bovine tendon was submitted to alkaline treatment resulting in a negatively charged collagen surface. The scaffolds were prepared by precipitation: simultaneous dropwise addition of solution containing calcium (Ca) and magnesium (Mg) ions and collagen into a buffered solution containing carbonate and phosphate ions in reaction vessel maintained at 37 °C, pH=8. The reaction products were cross-linked with 0.125 and 0.25% (v/v) glutaraldehyde (GA) solution and freeze-dried. The samples were characterized by Fourier-transformed infrared spectroscopy (FTIR). In vitro cytotoxicity (based on three parameters assays) and scaffolds degradation in culture medium and osteoblastic cells culture were performed in the cross-linked materials. No cytotoxic effects were observed. The cross-linked samples with the lower GA concentration showed a lower stability when placed in contact with culture medium. Human osteoblasts attached on the scaffolds surface cross-linked with 0.25% GA, forming a continuous layer after 14 days of incubation. These results showed potential application of the designed scaffolds for bone tissue engineering.

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