scholarly journals PCL Scaffold Combined with Rat Tail Collagen Type I to Reduce Keratocyte Differentiation and Prevent Corneal Stroma Fibrosis after Injury.

2021 ◽  
Author(s):  
Wenhan Xu ◽  
Bin Kong ◽  
Huatao Xie ◽  
Weijian Liu ◽  
Sheng Liu ◽  
...  
Keyword(s):  
Composite Material ◽  
Collagen Type ◽  
Corneal Stroma ◽  
Collagen Type I ◽  
Type I ◽  
Corneal Tissue ◽  
Self Healing ◽  
Corneal Injury ◽  
3D Composite ◽  
Rat Tail

Abstract The cornea is one of the major refractive eye components with significant functions, and its transparency is essential for clear vision. With regard to corneal injury, the corneal epithelium has a strong self-healing ability, while the corneal stroma is not capable of total self-repair. Therefore, preventing fibrosis and reducing keratocyte differentiation after injury have always been a challenge. The severe shortage of donor corneas for transplantation and transplant rejection prompted the development of corneal tissue engineering. In this study, we fabricated a poly(ε-caprolactone) (PCL) microfibrous scaffold and infused the scaffold with rat tail collagen type I to obtain a 3D composite material. The PCL/collagen scaffold was designed to fabricate an optimal construct that simulates the stromal structure with properties that are most similar to the native cornea. The PCL scaffold has good mechanical properties, and infusion with rat tail collagen type I improved its biocompatibility. The results demonstrate that 3D composite material could reduce keratocyte differentiation, help achieve regular collagen distribution, and promote corneal repair.

scholarly journals Relative rates of biosynthesis of collagen type I, type V and type VI in calf cornea

1991 ◽  
Vol 274 (2) ◽  
pp. 615-617 ◽  
Author(s):  
P Kern ◽  
M Menasche ◽  
L Robert
Keyword(s):  
Type I Collagen ◽  
Collagen Type ◽  
Corneal Stroma ◽  
Collagen Type I ◽  
Type I ◽  
Type Vi Collagen ◽  
Sds Page ◽  
Proline Incorporation ◽  
Type V

The biosynthesis of type I, type V and type VI collagens was studied by incubation of calf corneas in vitro with [3H]proline as a marker. Pepsin-solubilized collagen types were isolated by salt fractionation and quantified by SDS/PAGE. Expressed as proportions of the total hydroxyproline solubilized, corneal stroma comprised 75% type I, 8% type V and 17% type VI collagen. The rates of [3H]proline incorporation, linear up to 24 h for each collagen type, were highest for type VI collagen and lowest for type I collagen. From pulse-chase experiments, the calculated apparent half-lives for types I, V and VI collagens were 36 h, 10 h and 6 h respectively.

scholarly journals Histopathological Features in a Case of Peters' Anomaly with Acquired Corneal Staphyloma

2011 ◽  
Vol 2011 ◽  
pp. 1-5 ◽  
Author(s):  
Kumi Shirai ◽  
Yuka Okada ◽  
Yasushi Nakamura ◽  
Shizuya Saika
Keyword(s):  
Collagen Type ◽  
Corneal Stroma ◽  
Posterior Part ◽  
Collagen Type I ◽  
Type I ◽  
Peters Anomaly ◽  
Hematoxylin And Eosin ◽  
Corneal Staphyloma ◽  
The Right ◽  
Peripheral Cornea

We report a case of corneal staphyloma histologically diagnosed as caused by Peters' anomaly. A 62-year-old male had a protruding opaque vascularized cornea that began to bulge from six months ago in the right eye. Since his right eye was blind and he wanted us to remove the eyeball for cosmetic improvement, we enucleated the affected eye. The enucleated tissue was fixed in formalin and embedded in paraffin for histological examination. Hematoxylin and eosin staining showed that the cornea lacked the posterior part of the corneal stroma and Descemet's membrane in the central region and the entire corneal endothelium. The corneal epithelium was keratinized. Collagen type I was strongly positive in peripheral cornea and weakly in protruding stroma. The cells labeled by antibodies againstαSMA were scattered in the entire corneal stroma. As judged by the histological findings, the eye with the central corneal staphyloma was diagnosed as Peters' anomaly.

A Novel Rat Tail Collagen Type-I Gel for the Cultivation of Human Articular Chondrocytes in Low Cell Density

2007 ◽  
Vol 30 (12) ◽  
pp. 1057-1067 ◽  
Author(s):  
R. Muller-Rath ◽  
K. Gavénis ◽  
S. Andereya ◽  
T. Mumme ◽  
B. Schmidt-Rohlfing ◽  
...  
Keyword(s):  
Cell Density ◽  
Collagen Type ◽  
Articular Chondrocytes ◽  
Collagen Type I ◽  
Human Articular Chondrocytes ◽  
Type I ◽  
Low Cell Density ◽  
Rat Tail

Sequence Alignment between vWF and Peptides Inhibiting the vWF-collagen Interaction Does not Result in the Identification of a Collagen-binding Site in vWF

2000 ◽  
Vol 84 (10) ◽  
pp. 621-625 ◽  
Author(s):  
R. M. van der Plas ◽  
G. Vandecasteele ◽  
S. Vauterin ◽  
E. G. Huizinga ◽  
J. J. Sixma ◽  
...  
Keyword(s):  
Binding Site ◽  
Collagen Type ◽  
Collagen Type I ◽  
Type I ◽  
Binding Studies ◽  
Collagen Types ◽  
Collagen Binding ◽  
Human Collagen ◽  
Rat Tail ◽  
Calf Skin

SummaryWe previously found that two peptides (N- and Q-peptide) selected by phage display for binding to an anti-vWF antibody, were able to inhibit vWF-binding to collagen (1). The sequence of those peptides could be aligned with the sequence in vWF at position 1129-1136 just outside the A3-domain. As the peptides represent an epitope or mimotope of vWF for binding to collagen we next wanted to study whether the alignment resulted in the identification of a new collagen binding site in vWF. We mutated the 1129-1136 VWTLPDQC sequence in vWF to VATAPAAC. Expressing this mutant vWF (7.8-vWF) in a fur-BHK cell line resulted in well processed 7.8-vWF containing a normal distribution of molecular weight multimers. However, binding studies of this mutant vWF to rat tail, human and calf skin collagens type I, to human collagen types III and VI, revealed no decrease in vWF-binding to any of these collagens. Thus, although the N-and Q-peptides did inhibit the vWF-collagen interaction, the resulting alignment with the vWF sequence did not identify a collagen binding site, pointing out that alignments (although with a high percentage of identity) do not always result in identification of binding epitopes. However, suprisingly removal of the A3-domain or changing the vWF sequence at position 1129-1136 resulted in an increase of vWF-binding to human collagen type VI and to rat tail collagen type I, implying that these changes result in a different conformation of vWF with an increased binding to these collagens as a consequence.

Identification of Peptides, Selected by Phage Display Technology, That Inhibit von Willebrand Factor Binding to Collagen

Blood ◽  
1998 ◽  
Vol 92 (11) ◽  
pp. 4207-4211
Author(s):  
H. Depraetere ◽  
A. Viaene ◽  
S. Deroo ◽  
S. Vauterin ◽  
H. Deckmyn
Keyword(s):  
Von Willebrand Factor ◽  
Cyclic Peptides ◽  
Collagen Type ◽  
Collagen Type I ◽  
Type I ◽  
Dependent Manner ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Dose Dependent ◽  
Rat Tail

A repeated selection of phages from a cyclic hexapeptide phage display library resulted in an enrichment of phages that bound to the monoclonal antibody (MoAb) 82D6A3 (an anti–von Willebrand Factor [vWF] antibody that inhibits binding of vWF to collagen). Two clones were selected that bound both to MoAb 82D6A3 and to rat tail collagen type I in a specific and dose-dependent manner. The two phage clones were further used in a two-direction competition experiment with vWF. vWF was able to displace phages from collagen in a dose-dependent manner with an IC50 of 35 μg/mL and phages were able to inhibit vWF binding to collagen. With the use of specific primers, the sequence of the cysteine-flanked hexapeptide inserts could be deduced. The two phage clones carried an almost identical sequence, CVWLWEQC and CVWLWENC, with a substitution of an N for a Q at position 6 of the hexapeptide. Sequence comparison with the known vWF sequence showed the presence of a comparable sequence at position 1129-1136 (VWTLPDQC), located between the collagen-binding A3-domain and the D4-domain. The two cyclic peptides, the putative corresponding vWF peptide, and a peptide with a scrambled cyclic sequence were synthesized. The two cyclic peptides inhibited vWF binding to rat tail collagen type I in a dose-dependent manner, whereas the linear vWF peptide and the scrambled cyclic peptide were inactive. For half maximal inhibition, 100 ± 12.7 μmol/L and 34.8 ± 8.59 μmol/L (mean ± SEM, n = 3) of the N- and the Q-peptide, respectively, were needed. The two cyclic peptides were also able to inhibit vWF binding to calfskin and human collagen type I, but effective concentrations were some 5 to 10 times higher.

Identification of Peptides, Selected by Phage Display Technology, That Inhibit von Willebrand Factor Binding to Collagen

Blood ◽  
1998 ◽  
Vol 92 (11) ◽  
pp. 4207-4211 ◽  
Author(s):  
H. Depraetere ◽  
A. Viaene ◽  
S. Deroo ◽  
S. Vauterin ◽  
H. Deckmyn
Keyword(s):  
Von Willebrand Factor ◽  
Cyclic Peptides ◽  
Collagen Type ◽  
Collagen Type I ◽  
Type I ◽  
Dependent Manner ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Dose Dependent ◽  
Rat Tail

Abstract A repeated selection of phages from a cyclic hexapeptide phage display library resulted in an enrichment of phages that bound to the monoclonal antibody (MoAb) 82D6A3 (an anti–von Willebrand Factor [vWF] antibody that inhibits binding of vWF to collagen). Two clones were selected that bound both to MoAb 82D6A3 and to rat tail collagen type I in a specific and dose-dependent manner. The two phage clones were further used in a two-direction competition experiment with vWF. vWF was able to displace phages from collagen in a dose-dependent manner with an IC50 of 35 μg/mL and phages were able to inhibit vWF binding to collagen. With the use of specific primers, the sequence of the cysteine-flanked hexapeptide inserts could be deduced. The two phage clones carried an almost identical sequence, CVWLWEQC and CVWLWENC, with a substitution of an N for a Q at position 6 of the hexapeptide. Sequence comparison with the known vWF sequence showed the presence of a comparable sequence at position 1129-1136 (VWTLPDQC), located between the collagen-binding A3-domain and the D4-domain. The two cyclic peptides, the putative corresponding vWF peptide, and a peptide with a scrambled cyclic sequence were synthesized. The two cyclic peptides inhibited vWF binding to rat tail collagen type I in a dose-dependent manner, whereas the linear vWF peptide and the scrambled cyclic peptide were inactive. For half maximal inhibition, 100 ± 12.7 μmol/L and 34.8 ± 8.59 μmol/L (mean ± SEM, n = 3) of the N- and the Q-peptide, respectively, were needed. The two cyclic peptides were also able to inhibit vWF binding to calfskin and human collagen type I, but effective concentrations were some 5 to 10 times higher.

scholarly journals Collagen type I and type V are present in the same fibril in the avian corneal stroma.

1988 ◽  
Vol 106 (3) ◽  
pp. 999-1008 ◽  
Author(s):  
D E Birk ◽  
J M Fitch ◽  
J P Babiarz ◽  
T F Linsenmayer
Keyword(s):  
Monoclonal Antibodies ◽  
Collagen Type ◽  
Corneal Stroma ◽  
Collagen Type I ◽  
Collagen Molecule ◽  
Type I ◽  
Collagen Types ◽  
Type V Collagen ◽  
Fibril Structure ◽  
Type V

The distribution, supramolecular form, and arrangement of collagen types I and V in the chicken embryo corneal stroma were studied using electron microscopy, collagen type-specific monoclonal antibodies, and a preembedding immunogold method. Double-label immunoelectron microscopy with colloidal gold-tagged monoclonal antibodies was used to simultaneously localize collagen type I and type V within the chick corneal stroma. The results definitively demonstrate, for the first time, that both collagens are codistributed within the same fibril. Type I collagen was localized to striated fibrils throughout the corneal stroma homogeneously. Type V collagen could be localized only after pretreatment of the tissue to partially disrupt collagen fibril structure. After such pretreatments the type V collagen was found in regions where fibrils were partially dissociated and not in regions where fibril structure was intact. When pretreated tissues were double labeled with antibodies against types I and V collagen coupled to different size gold particles, the two collagens colocalized in areas where fibril structure was partially disrupted. Antibodies against type IV collagen were used as a control and were nonreactive with fibrils. These results indicate that collagen types I and V are assembled together within single fibrils in the corneal stroma such that the interaction of these collagen types within heterotypic fibrils masks the epitopes on the type V collagen molecule. One consequence of the formation of such heterotypic fibrils may be the regulation of corneal fibril diameter, a condition essential for corneal transparency.

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