Preparation of ready-to-use, storable and reconstituted type I collagen from rat tail tendon for tissue engineering applications

2006 ◽  
Vol 1 (6) ◽  
pp. 2753-2758 ◽  
Author(s):  
Navneeta Rajan ◽  
Jason Habermehl ◽  
Marie-France Coté ◽  
Charles J Doillon ◽  
Diego Mantovani
Keyword(s):  
Tissue Engineering ◽  
Type I Collagen ◽  
Type I ◽  
Engineering Applications ◽  
Tail Tendon ◽  
Rat Tail

scholarly journals Functionalised type-I collagen as a hydrogel building block for bio-orthogonal tissue engineering applications

2016 ◽  
Vol 4 (2) ◽  
pp. 318-326 ◽  
Author(s):  
R. Ravichandran ◽  
M. M. Islam ◽  
E. I. Alarcon ◽  
A. Samanta ◽  
S. Wang ◽  
...  
Keyword(s):  
Tissue Engineering ◽  
Michael Addition ◽  
Building Block ◽  
Type I Collagen ◽  
Click Reaction ◽  
Type I ◽  
Engineering Applications

Modulating the hydrogel properties from injectable to implantable scaffolds using the bio-orthogonal thiol-Michael addition click reaction.

scholarly journals Potential of Electrospun Poly(3-hydroxybutyrate)/Collagen Blends for Tissue Engineering Applications

2018 ◽  
Vol 2018 ◽  
pp. 1-13 ◽  
Author(s):  
Luca Salvatore ◽  
Vito Emanuele Carofiglio ◽  
Paolo Stufano ◽  
Valentina Bonfrate ◽  
Emanuela Calò ◽  
...  
Keyword(s):  
Tissue Engineering ◽  
Type I Collagen ◽  
Hydrolytic Degradation ◽  
Weight Ratio ◽  
Type I ◽  
Engineering Applications ◽  
Weight Losses ◽  
Murine Fibroblasts ◽  
Nonwoven Mats ◽  
Degradation Properties

In this work, tunable nonwoven mats based on poly(3-hydroxybutyrate) (PHB) and type I collagen (Coll) were successfully produced by electrospinning. The PHB/Coll weight ratio (fixed at 100/0, 70/30, and 50/50, resp.) was found to control the morphological, thermal, mechanical, and degradation properties of the mats. Increasing collagen amounts led to larger diameters of the fibers (in the approximate range 600–900 nm), while delaying their thermal decomposition (from 245°C to 262°C). Collagen also accelerated the hydrolytic degradation of the mats upon incubation in aqueous medium at 37°C for 23 days (with final weight losses of 1%, 15%, and 23% for 100/0, 70/30, and 50/50 samples, resp.), as a result of increased mat wettability and reduced PHB crystallinity. Interestingly, 70/30 meshes were the ones displaying the lowest stiffness (~116 MPa; p<0.05 versus 100/0 and 50/50 meshes), while 50/50 samples had an elastic modulus comparable to that of 100/0 ones (~250 MPa), likely due to enhanced physical crosslinking of the collagen chains, at least at high protein amounts. All substrates were also found to allow for good viability and proliferation of murine fibroblasts, up to 6 days of culture. Collectively, the results evidenced the potential of as-spun PHB/Coll meshes for tissue engineering applications.

scholarly journals Correction: Functionalised type-I collagen as a hydrogel building block for bio-orthogonal tissue engineering applications

2017 ◽  
Vol 5 (26) ◽  
pp. 5284-5284
Author(s):  
R. Ravichandran ◽  
M. M. Islam ◽  
E. I. Alarcon ◽  
A. Samanta ◽  
S. Wang ◽  
...  
Keyword(s):  
Tissue Engineering ◽  
Building Block ◽  
Type I Collagen ◽  
Type I ◽  
Engineering Applications

Correction for ‘Functionalised type-I collagen as a hydrogel building block for bio-orthogonal tissue engineering applications’ by R. Ravichandran et al., J. Mater. Chem. B, 2016, 4, 318–326.

Investigation on interaction of tannic acid with type I collagen and its effect on thermal, enzymatic, and conformational stability for tissue engineering applications

Biopolymers ◽  
2014 ◽  
Vol 101 (5) ◽  
pp. 471-483 ◽  
Author(s):  
Punitha Velmurugan ◽  
Ettayapuram Ramaprasad Azhagiya Singam ◽  
Raghava Rao Jonnalagadda ◽  
Venkatesan Subramanian
Keyword(s):  
Tissue Engineering ◽  
Tannic Acid ◽  
Type I Collagen ◽  
Conformational Stability ◽  
Type I ◽  
Engineering Applications

Sachharide Staining in Thin Sections

1981 ◽  
Vol 39 ◽  
pp. 554-555
Author(s):  
K. Marenus ◽  
E. Kuhn ◽  
M. Beer
Keyword(s):  
Type I Collagen ◽  
Cross Linking ◽  
Type I ◽  
Thin Sections ◽  
Protein Fibers ◽  
Thin Sectioning ◽  
Specific Band ◽  
Tail Tendon ◽  
Rat Tail ◽  
Specific Reagent

A specific reagent for the glycol groups of sugars yields similar staining patterns in isolated or embedded and thin sectioned rat tail tendon. These results suggest that the stain specificity and the structure of the protein fibers are retained after cross linking, embedding and thin sectioning.Osmate in the presence of tetramethylethylenediamine (TEMED) binds to glycols and has been found to stain sugar residues. SLS aggregates, in which adjacent molecules lie in exact register, can be formed by addition of ATP to collagen monomers. Osmate-TEMED staining of these has produced a specific band in Type I collagen at a known glycol position 10% along the molecule from the N-terminal end. We have observed a second band 10% from the C-terminal end (Fig. 1) which is also faintly visible in. In addition, other weak bands have been observed.

Tissue Engineering of Bone by Osteoinductive Biomaterials

MRS Bulletin ◽  
1996 ◽  
Vol 21 (11) ◽  
pp. 36-39 ◽  
Author(s):  
Ugo Ripamonti ◽  
Nicolaas Duneas
Keyword(s):  
Tissue Engineering ◽  
Bone Formation ◽  
Type I Collagen ◽  
Demineralized Bone Matrix ◽  
Bone Matrix ◽  
Mesenchymal Cells ◽  
Tissue Response ◽  
Type I ◽  
New Bone Formation ◽  
Demineralized Bone

Recent advances in materials science and biotechnology have given birth to the new and exciting field of tissue engineering, in which the two normally disparate fields are merging into a profitable matrimony. In particular the use of biomaterials capable of initiating new bone formation via a process called osteoinduction is leading to quantum leaps for the tissue engineering of bone.The classic work of Marshall R. Urist and A. Hari Reddi opened the field of osteoinductive biomaterials. Urist discovered that, upon implantation of devitalized, demineralized bone matrix in the muscle of experimental animals, new bone formation occurs within two weeks, a phenomenon he described as bone formation by induction. The tissue response elicited by implantation of demineralized bone matrix in muscle or under the skin includes activation and migration of undifferentiated mesenchymal cells by chemotaxis, anchoragedependent cell attachment to the matrix, mitosis and proliferation of mesenchymal cells, differentiation of cartilage, mineralization of the cartilage, vascular invasion of the cartilage, differentiation of osteoblasts and deposition of bone matrix, and finally mineralization of bone and differentiation of marrow in the newly developed ossicle.The osteoinductive ability of the extracellular matrix of bone is abolished by the dissociative extraction of the demineralized matrix, but is recovered when the extracted component, itself inactive, is reconstituted with the inactive residue—mainly insoluble collagenous bone matrix. This important experiment showed that the osteoinductive signal resides in the solubilized component but needs to be reconstituted with an appropriate carrier to restore the osteoinductive activity. In this case, the carrier is the insoluble collagenous bone matrix—mainly crosslinked type I collagen.

Tissue engineering of dental pulp on type I collagen

2004 ◽  
Vol 29 (4) ◽  
pp. 370
Author(s):  
Gwang-Hee Lee ◽  
Sung-Yoon Huh ◽  
Sang-Hyuk Park
Keyword(s):  
Tissue Engineering ◽  
Dental Pulp ◽  
Type I Collagen ◽  
Type I
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