Estimation of the binding force of the collagen molecule-decorin core protein complex in collagen fibril

2005 ◽  
Vol 38 (3) ◽  
pp. 433-443 ◽  
Author(s):  
Simone Vesentini ◽  
Alberto Redaelli ◽  
Franco M. Montevecchi
Keyword(s):  
Protein Complex ◽  
Collagen Fibril ◽  
Core Protein ◽  
Collagen Molecule ◽  
Binding Force

scholarly journals Marine Polysaccharide-Collagen Coatings on Ti6Al4V Alloy Formed by Self-Assembly

Micromachines ◽  
2019 ◽  
Vol 10 (1) ◽  
pp. 68 ◽  
Author(s):  
Karl Norris ◽  
Oksana Mishukova ◽  
Agata Zykwinska ◽  
Sylvia Colliec-Jouault ◽  
Corinne Sinquin ◽  
...  
Keyword(s):  
Self Assembly ◽  
Collagen Fibril ◽  
Hydrothermal Vents ◽  
Sem Analysis ◽  
Collagen Fibrils ◽  
Collagen Molecule ◽  
Biological Characterization ◽  
Collagen Hydrogel ◽  
Biomaterial Surfaces ◽  
Titanium Alloy Ti6al4v

Polysaccharides of marine origin are gaining interest as biomaterial components. Bacteria derived from deep-sea hydrothermal vents can produce sulfated exopolysaccharides (EPS), which can influence cell behavior. The use of such polysaccharides as components of organic, collagen fibril-based coatings on biomaterial surfaces remains unexplored. In this study, collagen fibril coatings enriched with HE800 and GY785 EPS derivatives were deposited on titanium alloy (Ti6Al4V) scaffolds produced by rapid prototyping and subjected to physicochemical and cell biological characterization. Coatings were formed by a self-assembly process whereby polysaccharides were added to acidic collagen molecule solution, followed by neutralization to induced self-assembly of collagen fibrils. Fibril formation resulted in collagen hydrogel formation. Hydrogels formed directly on Ti6Al4V surfaces, and fibrils adsorbed onto the surface. Scanning electron microscopy (SEM) analysis of collagen fibril coatings revealed association of polysaccharides with fibrils. Cell biological characterization revealed good cell adhesion and growth on bare Ti6Al4V surfaces, as well as coatings of collagen fibrils only and collagen fibrils enhanced with HE800 and GY785 EPS derivatives. Hence, the use of both EPS derivatives as coating components is feasible. Further work should focus on cell differentiation.

scholarly journals Structure–mechanics relationships of collagen fibrils in the osteogenesis imperfecta mouse model

2015 ◽  
Vol 12 (111) ◽  
pp. 20150701 ◽  
Author(s):  
O. G. Andriotis ◽  
S. W. Chang ◽  
M. Vanleene ◽  
P. H. Howarth ◽  
D. E. Davies ◽  
...  
Keyword(s):  
Mouse Model ◽  
Osteogenesis Imperfecta ◽  
Collagen Fibril ◽  
Bound Water ◽  
Collagen Fibrils ◽  
Collagen Molecule ◽  
Indentation Modulus ◽  
Microscopy Imaging ◽  
Col1a2 Gene ◽  
The Individual

The collagen molecule, which is the building block of collagen fibrils, is a triple helix of two α1(I) chains and one α2(I) chain. However, in the severe mouse model of osteogenesis imperfecta (OIM), deletion of the COL1A2 gene results in the substitution of the α2(I) chain by one α1(I) chain. As this substitution severely impairs the structure and mechanics of collagen-rich tissues at the tissue and organ level, the main aim of this study was to investigate how the structure and mechanics are altered in OIM collagen fibrils. Comparing results from atomic force microscopy imaging and cantilever-based nanoindentation on collagen fibrils from OIM and wild-type (WT) animals, we found a 33% lower indentation modulus in OIM when air-dried (bound water present) and an almost fivefold higher indentation modulus in OIM collagen fibrils when fully hydrated (bound and unbound water present) in phosphate-buffered saline solution (PBS) compared with WT collagen fibrils. These mechanical changes were accompanied by an impaired swelling upon hydration within PBS. Our experimental and atomistic simulation results show how the structure and mechanics are altered at the individual collagen fibril level as a result of collagen gene mutation in OIM. We envisage that the combination of experimental and modelling approaches could allow mechanical phenotyping at the collagen fibril level of virtually any alteration of collagen structure or chemistry.

scholarly journals The spliceosomal proteins PPIH and PRPF4 exhibit bi-partite binding

2017 ◽  
Vol 474 (21) ◽  
pp. 3689-3704 ◽  
Author(s):  
Caroline Rajiv ◽  
S. RaElle Jackson ◽  
Simon Cocklin ◽  
Elan Z. Eisenmesser ◽  
Tara L. Davis
Keyword(s):  
Protein Interactions ◽  
Protein Complex ◽  
Mutational Analysis ◽  
Core Protein ◽  
Point Mutations ◽  
Unexpected Result ◽  
Small Nuclear Rna ◽  
Peptidyl Prolyl Isomerase ◽  
Intrinsically Disordered ◽  
N Terminus

Pre-mRNA splicing is a dynamic, multistep process that is catalyzed by the RNA (ribonucleic acid)–protein complex called the spliceosome. The spliceosome contains a core set of RNAs and proteins that are conserved in all organisms that perform splicing. In higher organisms, peptidyl-prolyl isomerase H (PPIH) directly interacts with the core protein pre-mRNA processing factor 4 (PRPF4) and both integrate into the pre-catalytic spliceosome as part of the tri-snRNP (small nuclear RNA–protein complex) subcomplex. As a first step to understand the protein interactions that dictate PPIH and PRPF4 function, we expressed and purified soluble forms of each protein and formed a complex between them. We found two sites of interaction between PPIH and the N-terminus of PRPF4, an unexpected result. The N-terminus of PRPF4 is an intrinsically disordered region and does not adopt secondary structure in the presence of PPIH. In the absence of an atomic resolution structure, we used mutational analysis to identify point mutations that uncouple these two binding sites and find that mutations in both sites are necessary to break up the complex. A discussion of how this bipartite interaction between PPIH and PRPF4 may modulate spliceosomal function is included.

scholarly journals Decorin Core Protein (Decoron) Shape Complements Collagen Fibril Surface Structure and Mediates Its Binding

PLoS ONE ◽  
2009 ◽  
Vol 4 (9) ◽  
pp. e7028 ◽  
Author(s):  
Joseph P. R. O. Orgel ◽  
Aya Eid ◽  
Olga Antipova ◽  
Jordi Bella ◽  
John E. Scott
Keyword(s):  
Surface Structure ◽  
Collagen Fibril ◽  
Core Protein

Elongated dermatan sulphate in post-inflammatory healing skin distributes among collagen fibrils separated by enlarged interfibrillar gaps

2001 ◽  
Vol 358 (1) ◽  
pp. 157-163 ◽  
Author(s):  
Kumiko KUWABA ◽  
Miya KOBAYASHI ◽  
Yoshihiro NOMURA ◽  
Shinkichi IRIE ◽  
Yoh-ichi KOYAMA
Keyword(s):  
Electron Microscopy ◽  
Collagen Fibril ◽  
Core Protein ◽  
Mouse Skin ◽  
Molecular Size ◽  
Collagen Fibrils ◽  
Dermatan Sulphate ◽  
Disaccharide Composition ◽  
Control Skin

It has been reported that the disaccharide composition of dermatan sulphate shows transient changes after epicutaneous application of the hapten 2,4-dinitrofluorobenzene to mouse skin, and that these changes are most conspicuous in healing skin on day 15 after chemical insult [Kuwaba, Nomura, Irie and Koyama (1999) J. Dermatol. Sci. 19, 23–30]. In the present study it was found that the molecular size of dermatan sulphate was increased on day 15 after hapten application. The molecular size of decorin increased in healing skin, whereas the size of dermatan-sulphate-depleted core protein did not increase. The length and localization of decorin dermatan sulphate were investigated by electron microscopy. Dermatan sulphate filaments oriented orthogonally to collagen fibrils were longer in healing skin than in control skin. In control skin, dermatan sulphate filaments were found among tightly packed collagen fibrils. In contrast, the interfibrillar gaps between each collagen fibril were enlarged in healing skin; elongated dermatan sulphate filaments extended from the surface of collagen fibrils across the enlarged gap. These results suggest that the increase in molecular size of decorin dermatan sulphate is important in organizing collagen fibrils separated by enlarged interfibrillar gaps in healing skin.

scholarly journals A Consensus of Core Protein Complex Compositions for Saccharomyces cerevisiae

2010 ◽  
Vol 38 (6) ◽  
pp. 916-928 ◽  
Author(s):  
Joris J. Benschop ◽  
Nathalie Brabers ◽  
Dik van Leenen ◽  
Linda V. Bakker ◽  
Hanneke W.M. van Deutekom ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Complex ◽  
Core Protein

Ultrastructural analysis of collagen formation in the developing primate amnion

1990 ◽  
Vol 48 (3) ◽  
pp. 106-107
Author(s):  
Barry F. King ◽  
Grete N. Fry
Keyword(s):  
Golgi Apparatus ◽  
Collagen Fibril ◽  
Fibril Formation ◽  
Amniotic Cavity ◽  
Cytological Evidence ◽  
Mammalian Embryo ◽  
Intracellular Location ◽  
Collagen Formation ◽  
Amniotic Epithelium ◽  
Extraembryonic Mesoderm

The amnion surrounding the mammalian embryo consists of the amniotic epithelium facing the amniotic cavity, a layer of extraembryonic mesoderm bordering the exocoelom and an intervening layer of extracellular matrix (Fig. 1). During gestation the amnion expands remarkably to acommodate the rapidly growing embryo. In this study we have examined the process of collagen fibril formation in the developing amnion of the rhesus monkey between 20 and 60 days of gestation.Most cytological evidence of collagen fibril formation was observed in association with the extraembryonic mesodermal cells rather than the amniotic epithelium. The mesodermal cells h ad abundant cisternae of rough endoplasmic reticulum and a prominent Golgi apparatus. Elongated secretory vacuoles were associated with the Golgi apparatus and often contained parallel aggregates of fine filaments (Fig. 2). In some secretory vacuoles, periodic densities also were observed. Some striated collagen fibrils were observed in an apparent intracellular location in long, membrane-limited compartments (Fig. 3). Still other striated fibrils were observed in dense bodies, presumably lysosomes (Fig. 4).

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