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.

Comparative Analysis of the Proteomic Profile of Cattle Hides that Produce Loose and Tight Leather using In-Gel Tryptic Digestion followed by LC-MS/MS

2020 ◽  
Vol 115 (11) ◽  
pp. 399-408
Author(s):  
Catherine Maidment ◽  
Meekyung Ahn ◽  
Rafea Naffa ◽  
Trevor Loo ◽  
Gillian Norris
Keyword(s):  
Type I Collagen ◽  
Raw Material ◽  
Type I ◽  
Collagen Structure ◽  
Proteomic Profile ◽  
Collagen Network ◽  
Collagen Concentration ◽  
Different Types ◽  
Molecular Components ◽  
First Time

Looseness is a defect found in leather that reduces its quality by causing a wrinkly appearance in the finished product, resulting in a reduction in its value. Earlier studies on loose leather using microscopy and Raman spectroscopy reported a change in the collagen structure of loose leather. In this study, proteomics was used to investigate the possible molecular causes of looseness in the raw material, the first time such a study has been carried out. Proteins extracted from two regions of raw hide using two different methods were analysed; those taken from the distal axilla, an area prone to looseness, and those taken from the backbone which is less prone to looseness. Analyses using 1DE-LC-MS/MS showed that although the overall collagen concentration was similar in both areas of the hide, the distribution of the different types of collagen differed.  Specifically, concentrations of type I collagen, and the collagen-associated proteoglycan decorin were lower in samples taken from the distal axilla, symptomatic of a collagen network with excess space seen for these samples using confocal microscopy. This study suggests a possible link between the molecular components of raw cattle hide and looseness and more importantly between the molecular components of skin and skin defects. There is therefore potential to develop biomarkers for looseness which will enable early preventative action.

Preparation and Some Properties of Type I Collagen from Fish Scales

1996 ◽  
Vol 60 (12) ◽  
pp. 2092-2094 ◽  
Author(s):  
Yoshihiro Nomura ◽  
Hiromitu Sakai ◽  
Yasuhiro Ishii ◽  
and Kunio Shirai
Keyword(s):  
Type I Collagen ◽  
Type I ◽  
Fish Scales

scholarly journals Hydroxyl radical induced structural changes of collagen

2007 ◽  
Vol 21 (2) ◽  
pp. 91-103 ◽  
Author(s):  
Helan Xiao ◽  
Guoping Cai ◽  
Mingyao Liu
Keyword(s):  
Free Radical ◽  
Hydroxyl Radicals ◽  
Structural Changes ◽  
Type I Collagen ◽  
Free Radical Scavenger ◽  
Radical Scavenger ◽  
Type I ◽  
Dependent Manner ◽  
First Time

Extracellular matrix (ECM) plays an important role in cell differentiation, growth, migration and apoptosis. Collagen is the most abundant protein familyin vivo, but its function has still not been clearly defined yet. Reactive oxygen species (ROS) have a central role in oxidative cell stress. Electron spin resonance (ESR) spectroscopy indicates that type I collagen could uniquely scavenge hydroxyl radicals in dose- and time-dependent manner; whereas BSA and gelatin (a denatured collagen) have no such an effect. However, the mechanism by which type I collagen scavenges hydroxyl radicals is different from that of GSH, a well-known free radical scavenger. Using a new method, two-dimensional FTIR correlation analysis, for the first time, we show that the order of functional group changes of type I collagen in this process is amide I earlier than amide II than amide III than –CH– thanν(C=O). The results indicates that the structure of the main chain of collagen changed first, followed by more residue groupν(C=O) exposed to hydroxyl radicals. The reaction with the carbonyl group in collagen causes the hydroxyl free radicals to be scavenged. Therefore, ECM can effectively scavenge ROS under normal physiological conditions. When the proteins of ECM were denatured in the same way as gelatin, they lost their function as a free radical scavenger. All of these results provide new insight into therapy or prevention of oxidative stress, apoptosis and ageing.

THE INFLUENCE OF THE ORIENTATION OF THE COLLAGEN DIPOLES ON SECOND HARMONIC GENERATION (SHG) WITH HIGH NA UNDER CRYSTALLIZED TYPE I COLLAGEN FIBER MODEL

2012 ◽  
Vol 26 (29) ◽  
pp. 1250148
Author(s):  
FEI FEI WANG ◽  
JIAN MEI LIU ◽  
XIAO YUAN DENG
Keyword(s):  
Second Harmonic Generation ◽  
Harmonic Generation ◽  
Collagen Fiber ◽  
Type I Collagen ◽  
Second Harmonic ◽  
Numerical Aperture ◽  
Orientation Angle ◽  
Type I ◽  
Dipole Orientation ◽  
First Time

In this paper, for the first time, we consider theoretically all the potential orientations of dipoles for second harmonic generation (SHG) under crystallized type I collagen fiber. With high numerical aperture ( NA = 14), the effect of dipole orientation angle Φ on the SHG intensity, on the maximum SHG emergence angles (θ max , φ max ) and the action of these dipole sources on the ratio of forward to backward (F/B) SHG have been studied under different cases of fibrils diameter d1 and the QPM order (m, l) in the crystallized collagen fiber, and it is found that the influential patterns of the same Φ on SHG at different fibrils diameter d1 and the QPM order (m, l) are different. The dipoles arrangement is related to the characteristic changes in biological tissue so that our work may provide a helpful theoretical tool for pathological status detecting.

scholarly journals Cytoplasmic polyadenylation by TENT5A is required for proper bone formation

2020 ◽  
Author(s):  
Olga Gewartowska ◽  
Goretti Aranaz Novaliches ◽  
Paweł S Krawczyk ◽  
Seweryn Mroczek ◽  
Monika Kusio-Kobiałka ◽  
...  
Keyword(s):  
Bone Formation ◽  
Type I Collagen ◽  
Bone Mineralization ◽  
Bone Fragility ◽  
Type I ◽  
Human Genetic Disease ◽  
Cytoplasmic Polyadenylation ◽  
Disease Symptoms ◽  
Biologically Relevant ◽  
First Time

AbstractOsteoblasts orchestrate bone formation by secreting dense, highly cross-linked type I collagen and other proteins involved in osteogenesis. Mutations in Col1α1, Col1α2, or collagen biogenesis factors lead to the human genetic disease, osteogenesis imperfecta (OI). Herein, we show that the TENT5A gene, whose mutation is responsible for poorly characterized type XVIII OI, encodes an active cytoplasmic poly(A) polymerase regulating osteogenesis. TENT5A is induced during osteoblast differentiation and TENT5A KO osteoblasts are defective in mineralization. The TENT5A KO mouse recapitulates OI disease symptoms such as bone fragility and hypomineralization. Direct RNA sequencing revealed that TENT5A polyadenylates and increases expression of Col1α1 and Col1α2 RNAs, as well as those of other genes mutated in OI, resulting in lower production and improper folding of collagen chains. Thus, we have identified the specific pathomechanism of XVIII OI and report for the first time a biologically relevant post-transcriptional regulator of collagen production. We further postulate that TENT5A, possibly together with its paralogue TENT5C, is responsible for the wave of cytoplasmic polyadenylation of mRNAs encoding secreted proteins occurring during bone mineralization.

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.

Physical properties of type I collagen extracted from fish scales of Pagrus major and Oreochromis niloticas

2003 ◽  
Vol 32 (3-5) ◽  
pp. 199-204 ◽  
Author(s):  
Toshiyuki Ikoma ◽  
Hisatoshi Kobayashi ◽  
Junzo Tanaka ◽  
Dominic Walsh ◽  
Stephen Mann
Keyword(s):  
Physical Properties ◽  
Type I Collagen ◽  
Type I ◽  
Fish Scales ◽  
Pagrus Major

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 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

Organization and characterization of fibrillar collagens in fish scales in situ and in vitro

1992 ◽  
Vol 103 (1) ◽  
pp. 273-285 ◽  
Author(s):  
L. ZYLBERBERG ◽  
J. BONAVENTURE ◽  
L. COHEN-SOLAL ◽  
D. J. HARTMANN ◽  
J. BEREITERHAHN
Keyword(s):  
Cyanogen Bromide ◽  
Type I Collagen ◽  
Collagen Fibrils ◽  
Type I ◽  
Fish Scales ◽  
Fibrillar Collagens ◽  
Collagen Genes

The characterization of the fibrillar collagens and the cellular control of their spatial deposition were studied in fish scales using immunofluorescence, electron microscopy, electrophoretic and HPLC analyses, immunoprecipitation and hybridization with cDNA probes. This study was carried out on undisturbed and regenerating scales in situ and in organ and cell cultures from regenerating scales. The hyposquamal scleroblasts forming a pseudoepithelium show an apico-basal polarization and synthesize thick collagen fibrils (100 nm) organized in a plywood pattern as long as the integrity of the cell-cell and cell-collagenous matrix contacts are preserved. In culture, scleroblasts become fibroblastlike and produce an unordered meshwork of thin collagen fibrils (30 nm). Comparison of the synthesized collagens in culture with those extracted from the scales indicates that culture conditions modify fibrillogenesis but do not change the expression of fibrillar collagen genes. Type I collagen, the predominent component, is associated with the minor type V collagen. Type III collagen was not present. In type I collagen, a third chain, α3 chain, was identified. The ratio between the 3 chains suggests the coexistence of two heterotrimers (α(I))2 α2(I) and αl(I) α2(I) α3(I). Analysis by HPLC and electrophoresis of the cyanogen bromide-derived peptides obtained from the purified a3 chain support the hypothesis that α(I) and α3(I) chains are encoded by two different genes. The presence of the two types of heterotrimers in vivo as well as in vitro could correspond to an innate property of the goldfish scleroblasts. Despite the fact that teleost cyanogen bromide-derived peptides differ from those of higher vertebrates, homologies with the mammalian collagen genes (human, for example) are sufficient to allow the detection of mRNA transcripts for αl(I), α2(I) and α2(V) from confluent scleroblast cultures with human probes.

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