Identification of Linear IgE Epitopes for a Major Allergen–Type I Collagen in Fish (Rainbow Trout)

2018 ◽  
Vol 17 (2) ◽  
pp. 206-213
Author(s):  
Wang Yan-Bo ◽  
Li Xiao-Hui ◽  
Zhou Jin-Ru ◽  
Zhang Yan ◽  
Ma Ai-Jin ◽  
...  
Keyword(s):  
Rainbow Trout ◽  
Type I Collagen ◽  
Solid Phase ◽  
Strong Support ◽  
Major Allergen ◽  
Cross Reactivity ◽  
Type I ◽  
Linear Epitope ◽  
Fish Collagen ◽  
P Type

Type I collagen was described as a major allergen in fish. The purpose of this study was to screen and identify the linear IgE epitopes of type I collagen α1 and α2 subunits in rainbow trout. Five bioinformatics tools were used to predict the potential epitopes and the resultant epitopes were confirmed by LAD2 cells degranulation assay with sera from fish allergic patients. As the result, 10 peptides of α1 and α2 subunits were predicted, respectively, and these peptides were assembled by solid-phase synthesis. 14 epitopes were identified by LAD2 cells degranulation assay, among which, peptide 2, 5–7 were identified as linear epitope of α1 and peptide 11–20 were identified as linear epitope of α2. Moreover, for α1 and α2 subunits, the similarity of sequences was greater than 79%, suggesting the cross-reactivity of fish collagen. The findings of this study provided a strong support for further research of reduction of the collagen allergenicity.

scholarly journals Swim bladder collagen forms hydrogel with macroscopic superstructure by diffusion induced fast gelation

2015 ◽  
Vol 3 (39) ◽  
pp. 7658-7666 ◽  
Author(s):  
Md. Tariful Islam Mredha ◽  
Xi Zhang ◽  
Takayuki Nonoyama ◽  
Tasuku Nakajima ◽  
Takayuki Kurokawa ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Type I Collagen ◽  
Type I ◽  
Swim Bladder ◽  
P Type

Type I collagen extracted from the swim bladder of Bester sturgeon forms an oriented hydrogel with mechanical and thermal stability by diffusion induced fast gelation.

Type I collagen promotes the migration and myogenic differentiation of C2C12 myoblasts via the release of interleukin-6 mediated by FAK/NF-κB p65 activation

2020 ◽  
Vol 11 (1) ◽  
pp. 328-338
Author(s):  
Xiaoling Liu ◽  
Yanfang Gao ◽  
Xinyu Long ◽  
Toshihiko Hayashi ◽  
Kazunori Mizuno ◽  
...  
Keyword(s):  
Interleukin 6 ◽  
Type I Collagen ◽  
Myogenic Differentiation ◽  
Type I ◽  
C2c12 Myoblasts ◽  
P Type

Type I collagen has the potential to promote the migration and differentiation of C2C12 myoblast via IL-6 release that was mediated by FAK/NF-κB pathway.

scholarly journals Partial Characterization of cDNA Clones Encoding the Three Distinct Proα Chains of Type I Collagen from Rainbow Trout

1998 ◽  
Vol 64 (5) ◽  
pp. 780-786 ◽  
Author(s):  
Masataka Saito ◽  
Naomichi Kunisaki ◽  
Ikuo Hirono ◽  
Takashi Aoki ◽  
Masami Ishida ◽  
...  
Keyword(s):  
Rainbow Trout ◽  
Type I Collagen ◽  
Partial Characterization ◽  
Cdna Clones ◽  
Type I

Fish Scales as a Biocomposite of Collagen and Calcium Salts

2013 ◽  
Vol 587 ◽  
pp. 185-190 ◽  
Author(s):  
Alina Sionkowska ◽  
Justyna Kozlowska
Keyword(s):  
Type I Collagen ◽  
Quantitative Estimation ◽  
Esox Lucius ◽  
Type I ◽  
Fish Scales ◽  
Calcium Salts ◽  
Fish Collagen ◽  
Inorganic Content ◽  
Viscous Solution ◽  
First Time

Collagen for biomedical applications is mainly isolated from animal tissues (bovine or porcine skin and bovine or equine Achilles tendons). Type I collagen has been also extracted from skin, bone, fins and scales of fresh water and marine fishes. Fish scales are composed of collagen covered with calcium salts. In the present study we report the preparation of collagen from fish scales for potential cosmetic, pharmaceutical and implant applications. In our laboratory collagen was isolated from scales ofEsox lucius. It was the first time that this species were used as sources of collagen. Extraction of collagen from fish scales was done in two steps. In the first step, fish scales were demineralized using EDTA. Energy dispersive X-ray analysis of demineralized scale was carried out for quantitative estimation of inorganic content. Then, demineralized fish scales were dissolved in acetic acid. Collagen isolated fromEsox Luciusmay serve as an attractive and safe source of collagen for biomedical and pharmaceutical applications. Fish collagen can be processed in sheet, sponges foams, injectable viscous solution, and dispersions.

scholarly journals Characterization of a rainbow trout matrix metalloproteinase capable of degrading type I collagen

2000 ◽  
Vol 267 (23) ◽  
pp. 6943-6950 ◽  
Author(s):  
Masataka Saito ◽  
Kenji Sato ◽  
Naomichi Kunisaki ◽  
Shigeru Kimura
Keyword(s):  
Rainbow Trout ◽  
Matrix Metalloproteinase ◽  
Type I Collagen ◽  
Type I

scholarly journals Biological Safety of Fish (Tilapia) Collagen

2014 ◽  
Vol 2014 ◽  
pp. 1-9 ◽  
Author(s):  
Kohei Yamamoto ◽  
Kazunari Igawa ◽  
Kouji Sugimoto ◽  
Yuu Yoshizawa ◽  
Kajiro Yanagiguchi ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Collagen Gel ◽  
Growth Potential ◽  
Type I ◽  
Environmental Signals ◽  
Negative Results ◽  
Biological Studies ◽  
Fish Collagen

Marine collagen derived from fish scales, skin, and bone has been widely investigated for application as a scaffold and carrier due to its bioactive properties, including excellent biocompatibility, low antigenicity, and high biodegradability and cell growth potential. Fish type I collagen is an effective material as a biodegradable scaffold or spacer replicating the natural extracellular matrix, which serves to spatially organize cells, providing them with environmental signals and directing site-specific cellular regulation. This study was conducted to confirm the safety of fish (tilapia) atelocollagen for use in clinical application. We performedin vitroandin vivobiological studies of medical materials to investigate the safety of fish collagen. The extract of fish collagen gel was examined to clarify its sterility. All present sterility tests concerning bacteria and viruses (including endotoxin) yielded negative results, and all evaluations of cell toxicity, sensitization, chromosomal aberrations, intracutaneous reactions, acute systemic toxicity, pyrogenic reactions, and hemolysis were negative according to the criteria of the ISO and the http://dx.doi.org/10.13039/501100003478 Ministry of Health, Labour and Welfare. The present study demonstrated that atelocollagen prepared from tilapia is a promising biomaterial for use as a scaffold in regenerative medicine.

scholarly journals Cross-reactivity of cell-mediated immunity between interstitial (type I) and basement membrane (type IV) collagens.

1982 ◽  
Vol 156 (4) ◽  
pp. 1042-1056 ◽  
Author(s):  
A M Mackel ◽  
F DeLustro ◽  
E C LeRoy
Keyword(s):  
Type Iv Collagen ◽  
Type I Collagen ◽  
Cross Reactivity ◽  
Delayed Type Hypersensitivity ◽  
Antigenic Determinants ◽  
Collagen Molecule ◽  
Cell Mediated Immunity ◽  
Type I ◽  
Spleen Cells ◽  
Type Iv

In the present study, we demonstrate delayed-type hypersensitivity (DTH) to homologous type I collagen that cross-reacts with type IV collagen. Mice immunized with native or denatured type I collagens and challenged with these same antigens or native type IV collagen develop a peak DTH response on day 7. Challenge with denatured type IV collagen or collagenase-treated type IV collagen failed to elicit DTH in type I collagen-sensitized mice. Type I collagen-sensitized spleen cells adoptively transferred DTH to types IV and I collagen to normal recipients; T cell-depleted spleen cells failed to transfer immunity. Periodate-treated type IV collagen did not elicit DTH in mice sensitized to type I collagen; however, mice sensitized with type IV collagen displayed significant DTH when challenged with periodate-treated type IV collagen. Furthermore, treatment of type IV collagen with a mixed glycosidase or alpha-glucosidase before challenge eliminated the DTH response in type I collagen-sensitized mice; beta-galactosidase treatment of type IV collagen had no effect on this response. Mice sensitized with type IV collagen, however, displayed significant DTH when challenged with these glycosidase-treated antigens. Antibodies produced to types I and IV collagen by repeated immunizations were specific for the sensitizing antigen and did not react with other connective tissue antigens. These studies indicate that a CMI response to type I collagen recognizes similar antigenic determinants on the type IV collagen molecule. These cross-reacting determinants are dependent on conformation and contain carbohydrates, particularly glucose residues.

scholarly journals Effect of Fish Collagen Hydrolysates on Type I Collagen mRNA Levels of Human Dermal Fibroblast Culture

Marine Drugs ◽  
2018 ◽  
Vol 16 (5) ◽  
pp. 144 ◽  
Author(s):  
Ana Sanchez ◽  
Maria Blanco ◽  
Begoña Correa ◽  
Ricardo I. Perez-Martin ◽  
Carmen Sotelo
Keyword(s):  
Type I Collagen ◽  
Dermal Fibroblast ◽  
Human Dermal Fibroblast ◽  
Fibroblast Culture ◽  
Type I ◽  
Mrna Levels ◽  
Collagen Mrna ◽  
Fish Collagen ◽  
Collagen Hydrolysates
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