scholarly journals Recombinant expression and structural and binding properties of alpha1(VI) and alpha2(VI) chains of human collagen type VI

1994 ◽  
Vol 221 (1) ◽  
pp. 177-187 ◽  
Author(s):  
Emmanuelle TILLET ◽  
Hanna WIEDEMANN ◽  
Ralph GOLBIK ◽  
Te-Cheng PAN ◽  
Rui-Zhu ZHANG ◽  
...  
Keyword(s):  
Collagen Type ◽  
Recombinant Expression ◽  
Binding Properties ◽  
Collagen Type Vi ◽  
Human Collagen

scholarly journals Sources of Collagen for Biomaterials in Skin Wound Healing

2019 ◽  
Vol 6 (3) ◽  
pp. 56 ◽  
Author(s):  
Evan Davison-Kotler ◽  
William S. Marshall ◽  
Elena García-Gareta
Keyword(s):  
Collagen Type ◽  
Recombinant Expression ◽  
Collagen Type I ◽  
Skin Wound ◽  
Type I ◽  
Expression Systems ◽  
Skin Wound Healing ◽  
Skin Collagen ◽  
Human Collagen ◽  
Collagen Type Vii

Collagen is the most frequently used protein in the fields of biomaterials and regenerative medicine. Within the skin, collagen type I and III are the most abundant, while collagen type VII is associated with pathologies of the dermal–epidermal junction. The focus of this review is mainly collagens I and III, with a brief overview of collagen VII. Currently, the majority of collagen is extracted from animal sources; however, animal-derived collagen has a number of shortcomings, including immunogenicity, batch-to-batch variation, and pathogenic contamination. Recombinant collagen is a potential solution to the aforementioned issues, although production of correctly post-translationally modified recombinant human collagen has not yet been performed at industrial scale. This review provides an overview of current collagen sources, associated shortcomings, and potential resolutions. Recombinant expression systems are discussed, as well as the issues associated with each method of expression.

scholarly journals Amino acid sequence of the triple-helical domain of human collagen type VI.

1988 ◽  
Vol 263 (35) ◽  
pp. 18601-18606 ◽  
Author(s):  
M L Chu ◽  
D Conway ◽  
T C Pan ◽  
C Baldwin ◽  
K Mann ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Collagen Type ◽  
Helical Domain ◽  
Collagen Type Vi ◽  
Human Collagen ◽  
Triple Helical Domain

scholarly journals Plant Recombinant Human Collagen Type I Hydrogels for Corneal Regeneration

2021 ◽  
Author(s):  
Michel Haagdorens ◽  
Elle Edin ◽  
Per Fagerholm ◽  
Marc Groleau ◽  
Zvi Shtein ◽  
...  
Keyword(s):  
Collagen Type ◽  
Collagen Type I ◽  
Collagen Fibrils ◽  
Type I ◽  
Safe Alternative ◽  
Human Donor ◽  
Human Collagen ◽  
Donor Corneas

Abstract Purpose To determine feasibility of plant-derived recombinant human collagen type I (RHCI) for use in corneal regenerative implants Methods RHCI was crosslinked with 1-ethyl-3-(3-dimethyl aminopropyl) carbodiimide (EDC) and N-hydroxysuccinimide (NHS) to form hydrogels. Application of shear force to liquid crystalline RHCI aligned the collagen fibrils. Both aligned and random hydrogels were evaluated for mechanical and optical properties, as well as in vitro biocompatibility. Further evaluation was performed in vivo by subcutaneous implantation in rats and corneal implantation in Göttingen minipigs. Results Spontaneous crosslinking of randomly aligned RHCI (rRHCI) formed robust, transparent hydrogels that were sufficient for implantation. Aligning the RHCI (aRHCI) resulted in thicker collagen fibrils forming an opaque hydrogel with insufficient transverse mechanical strength for surgical manipulation. rRHCI showed minimal inflammation when implanted subcutaneously in rats. The corneal implants in minipigs showed that rRHCI hydrogels promoted regeneration of corneal epithelium, stroma, and nerves; some myofibroblasts were seen in the regenerated neo-corneas. Conclusion Plant-derived RHCI was used to fabricate a hydrogel that is transparent, mechanically stable, and biocompatible when grafted as corneal implants in minipigs. Plant-derived collagen is determined to be a safe alternative to allografts, animal collagens, or yeast-derived recombinant human collagen for tissue engineering applications. The main advantage is that unlike donor corneas or yeast-produced collagen, the RHCI supply is potentially unlimited due to the high yields of this production method. Lay Summary A severe shortage of human-donor corneas for transplantation has led scientists to develop synthetic alternatives. Here, recombinant human collagen type I made of tobacco plants through genetic engineering was tested for use in making corneal implants. We made strong, transparent hydrogels that were tested by implanting subcutaneously in rats and in the corneas of minipigs. We showed that the plant collagen was biocompatible and was able to stably regenerate the corneas of minipigs comparable to yeast-produced recombinant collagen that we previously tested in clinical trials. The advantage of the plant collagen is that the supply is potentially limitless.

scholarly journals POS-777 ELEVATED PLASMA PRO-COLLAGEN TYPE VI PREDICTS ACUTE KIDNEY INJURY AFTER RENAL TRANSPLANTATION

2021 ◽  
Vol 6 (4) ◽  
pp. S338-S339
Author(s):  
M. Tepel ◽  
S. J. L. Bakker ◽  
O. Thaunat ◽  
S. Nagarajah ◽  
F. Genovese ◽  
...  
Keyword(s):  
Acute Kidney Injury ◽  
Renal Transplantation ◽  
Collagen Type ◽  
Kidney Injury ◽  
Elevated Plasma ◽  
Collagen Type Vi

scholarly journals Collagen type VI in the human bone marrow microenvironment: a strong cytoadhesive component

Blood ◽  
1995 ◽  
Vol 86 (5) ◽  
pp. 1740-1748 ◽  
Author(s):  
G Klein ◽  
CA Muller ◽  
E Tillet ◽  
ML Chu ◽  
R Timpl
Keyword(s):  
Bone Marrow ◽  
Cell Lines ◽  
Triple Helix ◽  
Collagen Type ◽  
Hematopoietic Cell ◽  
Human Bone ◽  
Human Bone Marrow ◽  
Collagen Vi ◽  
Collagen Type Vi ◽  
Hematopoietic Cell Lines

Collagen type VI, which forms characteristic microfibrillar structures, is assembled from three individual alpha(VI) chains that form a short triple helix and two adjacent globular domains. Expression of all three alpha (VI) collagen chains in the human bone marrow (BM) microenvironment could be detected by chain-specific antibodies in tissue sections and in the adherent stromal layer of long-term BM cultures. In functional studies, collagen type VI was shown to be a strong adhesive substrate for various hematopoietic cell lines and light-density BM mononuclear cells. The adhesive site within the molecule seems to be restricted to the triple helical domain of all three alpha (VI) chains, because individual alpha (VI) chains were not active in the attachment assays. Adhesion of the hematopoietic cell lines to collagen VI was dose-dependent and could be inhibited by heparin. Although the triple helix contains several RGD sequences, adhesion of the hematopoietic cell types to collagen VI could be blocked neither by RGD-containing peptides nor by a neutralizing antibody to the beta 1 integrin subunit. In combination with an antiadhesive substrate, the binding properties of collagen VI could be downregulated. These data suggest that this collagen type may play an important role in the adhesion of hematopoietic cells within the BM microenvironment.

Specificity and T cell receptor β chain usage of a human collagen type II-reactive T cell clone derived from a healthy individual

1992 ◽  
Vol 22 (1) ◽  
pp. 51-56 ◽  
Author(s):  
Tan Yan ◽  
Harald Burkhardt ◽  
Thomas Ritter ◽  
Barbara Bröker ◽  
Karl Heinz Mann ◽  
...  
Keyword(s):  
T Cell ◽  
T Cell Receptor ◽  
Collagen Type ◽  
Cell Clone ◽  
Cell Receptor ◽  
Type Ii ◽  
Collagen Type Ii ◽  
T Cell Clone ◽  
Human Collagen ◽  
Β Chain

scholarly journals Abnormal human chondrocyte morphology is related to increased levels of cell-associated IL-1β and disruption to pericellular collagen type VI

2010 ◽  
Vol 28 (11) ◽  
pp. 1507-1514 ◽  
Author(s):  
Dianne H. Murray ◽  
Peter G. Bush ◽  
Ivan J. Brenkel ◽  
Andrew C. Hall
Keyword(s):  
Collagen Type ◽  
Human Chondrocyte ◽  
Collagen Type Vi

scholarly journals Recombinant expression of hydroxylated human collagen in Escherichia coli

2013 ◽  
Vol 98 (10) ◽  
pp. 4445-4455 ◽  
Author(s):  
Christoph Rutschmann ◽  
Stephan Baumann ◽  
Jürg Cabalzar ◽  
Kelvin B. Luther ◽  
Thierry Hennet
Keyword(s):  
Escherichia Coli ◽  
Recombinant Expression ◽  
Human Collagen

scholarly journals Correction: Microenvironment-responsive multifunctional hydrogels with spatiotemporal sequential release of tailored recombinant human collagen type III for the rapid repair of infected chronic diabetic wounds

2022 ◽  
Author(s):  
Cheng Hu ◽  
Wenqi Liu ◽  
Linyu Long ◽  
Zhicun Wang ◽  
Yihui Yuan ◽  
...  
Keyword(s):  
Collagen Type ◽  
Collagen Type Iii ◽  
Rapid Repair ◽  
Type Iii ◽  
Sequential Release ◽  
Human Collagen ◽  
Diabetic Wounds

Correction for ‘Microenvironment-responsive multifunctional hydrogels with spatiotemporal sequential release of tailored recombinant human collagen type III for the rapid repair of infected chronic diabetic wounds’ by Cheng Hu et al., J. Mater. Chem. B, 2021, 9, 9684–9699, DOI: 10.1039/D1TB02170B.

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