scholarly journals MOLECULAR CHARACTERISTICS OF ACID AND PEPSIN SOLUBLE COLLAGENS FROM THE SCALES OF GOLDEN CARP (PROBARBUS JULLIENI)

2017 ◽  
pp. 450 ◽  
Author(s):  
Ali Muhammed Moula Ali ◽  
Soottawat Benjakul ◽  
Hideki Kishimura
Keyword(s):  
Amino Acid ◽  
Type I Collagen ◽  
Helical Structure ◽  
Dry Weight ◽  
Total Amino Acid ◽  
Molecular Characteristics ◽  
Type I ◽  
Scanning Calorimetry ◽  
Soluble Collagen ◽  
Golden Carp

Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) were isolated from the scales of golden carp (Probarbus jullieni). Both ASC and PSC, identified as type I collagen, contained α- and β-chains as the dominant constituents. ASC and PSC had the yields of 0.42 and 1.16 g 100 g‒1 (dry weight basis), respectively. Amino acid composition revealed that glycine constituted 1/3 of total amino acid residues and no cysteine was found. ASC and PSC had imino acid contents of 197 and 202 residues/1000 residues, respectively. Fourier transform infrared spectroscopy (FTIR) and circular dichroism (CD) spectra indicated high integrity of the triple helical structure of both collagens. Based on differential scanning calorimetry (DSC), ASC and PSC had Tmax of 37.67 and 37.83 °C, respectively. Both collagens exhibited high solubility in acidic pH range (1‒3) and the decrease in solubility was found in the presence of NaCl at concentrations above 30 g L‒1. The overall results demonstrated that scales of golden carp could serve as another source of collagen.

scholarly journals Comprehensive Assessment of Nile Tilapia Skin (Oreochromis niloticus) Collagen Hydrogels for Wound Dressings

Marine Drugs ◽  
2020 ◽  
Vol 18 (4) ◽  
pp. 178 ◽  
Author(s):  
Baosheng Ge ◽  
Haonan Wang ◽  
Jie Li ◽  
Hengheng Liu ◽  
Yonghao Yin ◽  
...  
Keyword(s):  
Wound Dressing ◽  
Type I Collagen ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Wound Dressings ◽  
Type I ◽  
Rheological Characterization ◽  
Scanning Calorimetry ◽  
Soluble Collagen ◽  
Collagen Hydrogels

Collagen plays an important role in the formation of extracellular matrix (ECM) and development/migration of cells and tissues. Here we report the preparation of collagen and collagen hydrogel from the skin of tilapia and an evaluation of their potential as a wound dressing for the treatment of refractory wounds. The acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) were extracted and characterized using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), differential scanning calorimetry (DSC), circular dichroism (CD) and Fourier transform infrared spectroscopy (FTIR) analysis. Both ASC and PSC belong to type I collagen and have a complete triple helix structure, but PSC shows lower molecular weight and thermal stability, and has the inherent low antigenicity. Therefore, PSC was selected to prepare biomedical hydrogels using its self-aggregating properties. Rheological characterization showed that the mechanical strength of the hydrogels increased as the PSC content increased. Scanning electron microscope (SEM) analysis indicated that hydrogels could form a regular network structure at a suitable PSC content. Cytotoxicity experiments confirmed that hydrogels with different PSC content showed no significant toxicity to fibroblasts. Skin repair experiments and pathological analysis showed that the collagen hydrogels wound dressing could significantly accelerate the healing of deep second-degree burn wounds and the generation of new skin appendages, which can be used for treatment of various refractory wounds.

scholarly journals Comparison of Physicochemical Characteristics and Fibril Formation Ability of Collagens Extracted from the Skin of Farmed River Puffer (Takifugu obscurus) and Tiger Puffer (Takifugu rubripes)

Marine Drugs ◽  
2019 ◽  
Vol 17 (8) ◽  
pp. 462 ◽  
Author(s):  
Wang ◽  
Yu ◽  
Sun ◽  
Liu ◽  
Zhou
Keyword(s):  
Type I Collagen ◽  
Molecular Form ◽  
Formation Rate ◽  
Helical Structure ◽  
Fibril Formation ◽  
Takifugu Rubripes ◽  
Type I ◽  
Soluble Collagen ◽  
Skin Collagen ◽  
Tiger Puffer

Acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) from the skin of river puffer (ASC-RP and PSC-RP) and tiger puffer (ASC-TP and PSC-TP) were extracted and physicochemically examined. Denaturation temperature (Td) for all the collagens was found to be 25.5–29.5 °C, which was lower than that of calf skin collagen (35.9 °C). Electrophoretic patterns indicated all four samples were type I collagen with molecular form of (α1)2α2. FTIR spectra confirmed the extracted collagens had a triple-helical structure, and that the degree of hydrogen bonding in ASC was higher than PSC. All the extracted collagens could aggregate into fibrils with D-periodicity. The fibril formation rate of ASC-RP and PSC-RP was slightly higher than ASC-TP and PSC-TP. Turbidity analysis revealed an increase in fibril formation rate when adding a low concentration of NaCl (less than 300 mM). The fibril formation ability was suppressed with further increasing of NaCl concentration, as illustrated by a reduction in the turbidity and formation degree. SEM analysis confirmed the well-formed interwoven structure of collagen fibrils after 24 h of incubation. Summarizing the experimental results suggested that the extracted collagens from the skin of river puffer and tiger puffer could be considered a viable substitute to mammalian-derived collagens for further use in biomaterial applications.

scholarly journals Isolation and properties of collagen extracted from mixed by-products obtained from different fish species

Biotecnia ◽  
2021 ◽  
Vol 23 (3) ◽  
pp. 109-116
Author(s):  
Celia Olivia García-Sifuentes ◽  
Julio Cesar Zamorano-Apodaca ◽  
Marcel Martinez-Porchas ◽  
Susana Maria Scheuren-Acevedo ◽  
Miguel Angel Mazorra-Manzano
Keyword(s):  
Fish Species ◽  
Type I Collagen ◽  
Helical Structure ◽  
Extraction Process ◽  
Type I ◽  
Denaturation Temperature ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Sds Page ◽  
By Products

Fish by-products consisting of skin, bones, or scales are collagen sources. Acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) mixed by-products derived from different fish species were extracted and evaluated. The properties evaluated for both collagens were chemical composition, amino acid- and SDS-PAGE- protein profiles, Fourier transform infrared spectroscopy (FTIR), denaturation temperature (Tmax), enthalpy (ΔH), and solubility. The ASC and PSC registered a protein content of 48.56 and 38.80 %, respectively. From the total amino acids detected, hydroxyproline accounted for 7 % and 6 % for ASC and PSC, respectively. The electrophoretic profile showed the presence of the type I collagen bands (α1, α2, β, and γ), whereas FTIR spectrum showed the presence of diverse collagen functional groups (Amide A, B, I, II, and III) for both extracted types, and demonstrated that the extraction process did not affect the collagen´s triple-helical structure. The Tmax of ASC and PSC were 38.27 and 38.07° C, respectively, whereas ΔH were 0.64 and 0.33 J g-1. The lowest solubility was registered at pH 5 for ASC and pH 9 for PSC. The caractheristics of the collagen extracted, indicated that a mixture of by-products from different species could be an alternative for their reutilization by the local markets.

scholarly journals Physicochemical and Antioxidant Properties of Acid- and Pepsin-Soluble Collagens from the Scales of Miiuy Croaker (Miichthys Miiuy)

Marine Drugs ◽  
2018 ◽  
Vol 16 (10) ◽  
pp. 394 ◽  
Author(s):  
Long-Yan Li ◽  
Yu-Qin Zhao ◽  
Yu He ◽  
Chang-Feng Chi ◽  
Bin Wang
Keyword(s):  
Amino Acid ◽  
Hydroxyl Radical ◽  
Superoxide Anion ◽  
Anion Radical ◽  
Antioxidant Properties ◽  
Superoxide Anion Radical ◽  
Type I ◽  
Dpph Radical ◽  
Soluble Collagen ◽  
Miichthys Miiuy

In this report, acid-soluble collagen (ASC-MC) and pepsin-soluble collagen (PSC-MC) were extracted from the scales of miiuy croaker (Miichthys miiuy) with yields of 0.64 ± 0.07% and 3.87 ± 0.15% of dry weight basis, respectively. ASC-MC and PSC-MC had glycine as the major amino acid with the contents of 341.8 ± 4.2 and 344.5 ± 3.2 residues/1000 residues, respectively. ASC-MC and PSC-MC had lower denaturation temperatures (32.2 °C and 29.0 °C for ASC-MC and PSC-MC, respectively) compared to mammalian collagen due to their low imino acid content (197.6 and 195.2 residues/1000 residues for ASC-MC and PSC-MC, respectively). ASC-MC and PSC-MC were mainly composed of type I collagen on the literatures and results of amino acid composition, SDS-PAGE pattern, ultraviolet (UV) and Fourier-transform infrared spectroscopy (FTIR) spectra. The maximum solubility of ASC-MC and PSC-MC was appeared at pH 1–3 and a sharp decrease in solubility was observed when the NaCl concentration was above 2%. Zeta potential studies indicated that ASC-MC and PSC-MC exhibited a net zero charge at pH 6.66 and 6.81, respectively. Furthermore, the scavenging capabilities on 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical, hydroxyl radical, superoxide anion radical and 2,2′-azino-bis-3-ethylbenzothiazoline-6-sulfonic acid (ABTS) radical of ASC-MC and PSC-MC were positively correlated with their tested concentration ranged from 0 to 5 mg/mL and PSC-MC showed significantly higher activity than that of ASC-MC at most tested concentrations (p < 0.05). In addition, the scavenging capability of PSC-MC on hydroxyl radical and superoxide anion radical was higher than those of DPPH radical and ABTS radical, which suggested that ASC-SC and PSC-SC might be served as hydroxyl radical and superoxide anion radical scavenger in cosmeceutical products for protecting skins from photoaging and ultraviolet damage.

scholarly journals Comparison of the Structural Characteristics of Native Collagen Fibrils Derived from Bovine Tendons Using Two Different Methods: Modified Acid-Solubilized and Pepsin-Aided Extraction

Materials ◽  
2020 ◽  
Vol 13 (2) ◽  
pp. 358 ◽  
Author(s):  
Haiyan Ju ◽  
Xiuying Liu ◽  
Gang Zhang ◽  
Dezheng Liu ◽  
Yongsheng Yang
Keyword(s):  
Type I Collagen ◽  
Structural Characteristics ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Dry Weight ◽  
Collagen Fibrils ◽  
Type I ◽  
X Ray Diffraction ◽  
Aggregation Structure ◽  
Native Collagen

Native collagen fibrils (CF) were successfully extracted from bovine tendons using two different methods: modified acid-solubilized extraction for A-CF and pepsin-aided method for P-CF. The yields of A-CF and P-CF were up to 64.91% (±1.07% SD) and 56.78% (±1.22% SD) (dry weight basis), respectively. The analyses of both amino acid composition and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) confirmed that A-CF and P-CF were type I collagen fibrils. Both A-CF and P-CF retained the intact crystallinity and integrity of type I collagen’s natural structure by FTIR spectra, circular dichroism spectroscopy (CD) and X-ray diffraction detection. The aggregation structures of A-CF and P-CF were displayed by UV–Vis. However, A-CF showed more intact aggregation structure than P-CF. Microstructure and D-periodicities of A-CF and P-CF were observed (SEM and TEM). The diameters of A-CF and P-CF are about 386 and 282 nm, respectively. Although both A-CF and P-CF were theoretically concordant with the Schmitt hypothesis, A-CF was of evener thickness and higher integrity in terms of aggregation structure than P-CF. Modified acid-solubilized method provides a potential non-enzyme alternative to extract native collagen fibrils with uniform thickness and integral aggregation structure.

scholarly journals Effect of hydroxylysine-O-glycosylation on the structure of type I collagen molecule: A computational study

Glycobiology ◽  
2020 ◽  
Vol 30 (10) ◽  
pp. 830-843
Author(s):  
Ming Tang ◽  
Xiaocong Wang ◽  
Neha S Gandhi ◽  
Bethany Lachele Foley ◽  
Kevin Burrage ◽  
...  
Keyword(s):  
Force Field ◽  
Type I Collagen ◽  
Computational Study ◽  
Experimental Studies ◽  
Helical Structure ◽  
Atomic Level ◽  
Collagen Molecule ◽  
Type I ◽  
Dynamic Simulations ◽  
Force Field Parameters

Abstract Collagen undergoes many types of post-translational modifications (PTMs), including intracellular modifications and extracellular modifications. Among these PTMs, glycosylation of hydroxylysine (Hyl) is the most complicated. Experimental studies demonstrated that this PTM ceases once the collagen triple helix is formed and that Hyl-O-glycosylation modulates collagen fibrillogenesis. However, the underlying atomic-level mechanisms of these phenomena remain unclear. In this study, we first adapted the force field parameters for O-linkages between Hyl and carbohydrates and then investigated the influence of Hyl-O-glycosylation on the structure of type I collagen molecule, by performing comprehensive molecular dynamic simulations in explicit solvent of collagen molecule segment with and without the glycosylation of Hyl. Data analysis demonstrated that (i) collagen triple helices remain in a triple-helical structure upon glycosylation of Hyl; (ii) glycosylation of Hyl modulates the peptide backbone conformation and their solvation environment in the vicinity and (iii) the attached sugars are arranged such that their hydrophilic faces are well exposed to the solvent, while their hydrophobic faces point towards the hydrophobic portions of collagen. The adapted force field parameters for O-linkages between Hyl and carbohydrates will aid future computational studies on proteins with Hyl-O-glycosylation. In addition, this work, for the first time, presents the detailed effect of Hyl-O-glycosylation on the structure of human type I collagen at the atomic level, which may provide insights into the design and manufacture of collagenous biomaterials and the development of biomedical therapies for collagen-related diseases.

scholarly journals Preparation and Characterization of Gelatin and Antioxidant Peptides from Gelatin Hydrolysate of Skipjack Tuna (Katsuwonus pelamis) Bone Stimulated by in vitro Gastrointestinal Digestion

Marine Drugs ◽  
2019 ◽  
Vol 17 (2) ◽  
pp. 78 ◽  
Author(s):  
Xiu-Rong Yang ◽  
Yu-Qin Zhao ◽  
Yi-Ting Qiu ◽  
Chang-Feng Chi ◽  
Bin Wang
Keyword(s):  
Amino Acid ◽  
Type I Collagen ◽  
Type I ◽  
Skipjack Tuna ◽  
Antioxidant Peptides ◽  
Gastrointestinal Digestion ◽  
Katsuwonus Pelamis ◽  
In Vitro Gastrointestinal Digestion ◽  
Gelatin Hydrolysate

In China, a large amount of fish bones are produced during the processing of tuna cans production. For full use of those by-products, gelatin (STB-G) with a yield of 6.37 ± 0.64% was extracted from skipjack tuna (Katsuwonus pelamis) bone using water at 60 °C for 8 h. Amino acid analysis showed that STB-G contained Gly (340.3 residues/1000 residues) as the major amino acid and its imino acid content was 177.3 residues/1000 residues. Amino acid composition, SDS-PAGE, and Fourier transform infrared (FTIR) spectrum investigations confirmed that the physicochemical properties of STB-G were similar to those of type I collagen from skipjack tuna bone (STB-C), but partial high molecular weight components of STB-G were degraded during the extraction process, which induced that the gelatin was easier to be hydrolyzed by protease than mammalian gelatins and was suitable for preparation of hydrolysate. Therefore, STB-G was hydrolyzed under in vitro gastrointestinal digestion (pepsin-trypsin system) and five antioxidant peptides were purified from the resulted hydrolysate (STB-GH) and identified as GPDGR, GADIVA, GAPGPQMV, AGPK, and GAEGFIF, respectively. Among the gelatin hydrolysate, fractions, and isolated peptides, GADIVA and GAEGFIF exhibited the strongest scavenging activities on 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical (EC50 0.57 and 0.30 mg/mL), hydroxyl radical (EC50 0.25 and 0.32 mg/mL), superoxide anion radical (EC50 0.52 and 0.48 mg/mL), and 2,2′-azino-bis-3-ethylbenzothiazoline-6-sulfonic acid (ABTS) radical (EC50 0.41 and 0.21 mg/mL). Moreover, GADIVA and GAEGFIF showed a high inhibiting ability on lipid peroxidation in a linoleic acid model system. The strong activities of five isolated peptides profited by their small molecular sizes and the antioxidant amino acid residues in their sequences. These results suggested that five isolated peptides (STP1–STP5), especially GADIVA and GAEGFIF, might serve as potential antioxidants applied in health food industries.

scholarly journals Regulation of type I collagen mRNA in lung fibroblasts by cystine availability

1998 ◽  
Vol 331 (2) ◽  
pp. 417-422 ◽  
Author(s):  
David C. RISHIKOF ◽  
Ping-Ping KUANG ◽  
Christine POLIKS ◽  
Ronald H. GOLDSTEIN
Keyword(s):  
Amino Acids ◽  
Steady State ◽  
Amino Acid ◽  
Type I Collagen ◽  
State Level ◽  
Lung Fibroblasts ◽  
Type I ◽  
Mrna Levels ◽  
Collagen Mrna ◽  
Amino Acid Availability

The steady-state level of α1(I) collagen mRNA is regulated by amino acid availability in human lung fibroblasts. Depletion of amino acids decreases α1(I) collagen mRNA levels and repletion of amino acids induces rapid re-expression of α1(I) mRNA. In these studies, we examined the requirements for individual amino acids on the regulation of α1(I) collagen mRNA. We found that re-expression of α1(I) collagen mRNA was critically dependent on cystine but not on other amino acids. However, the addition of cystine alone did not result in re-expression of α1(I) collagen mRNA. Following amino acid depletion, the addition of cystine with selective amino acids increased α1(I) collagen mRNA levels. The combination of glutamine and cystine increased α1(I) collagen mRNA levels 6.3-fold. Methionine or a branch-chain amino acid (leucine, isoleucine or valine) also acted in combination with cystine to increase α1(I) collagen mRNA expression, whereas other amino acids were not effective. The prolonged absence of cystine lowered steady-state levels of α1(I) collagen mRNA through a mechanism involving decreases in both the rate of gene transcription as assessed by nuclear run-on experiments and mRNA stability as assessed by half-life determination in the presence of actinomycin D. The effect of cystine was not mediated via alterations in the level of glutathione, the major redox buffer in cells, as determined by the addition of buthionine sulphoximine, an inhibitor of γ-glutamylcysteine synthetase. These data suggest that cystine directly affects the regulation of α1(I) collagen mRNA.

Archaeological Bone from Macro- to Nanoscale: Heat-Induced Modifications at Low Temperatures

2009 ◽  
Vol 8 ◽  
pp. 157-172 ◽  
Author(s):  
Céline Chadefaux ◽  
Ina Reiche
Keyword(s):  
Electron Microscopy ◽  
Low Temperatures ◽  
Type I Collagen ◽  
Bone Structure ◽  
Heating Temperature ◽  
Global Analysis ◽  
Type I ◽  
Scanning Calorimetry ◽  
Bone Material ◽  
X Ray

The present work focuses on the characterization of structural modifications in bone material induced by heating at low temperatures (90 - 250°C). This is of outmost importance when archaeological bone material is concerned. Changes occurring in the structure of the type I collagen and of the mineral-organic arrangement are especially investigated. This precise characterization required the combination of complementary analytical techniques: Differential Scanning Calorimetry (DSC) for global analysis of the collagen state of conservation, Scanning Electron Microscopy coupled with an Energy Dispersive X-Ray system (SEM-EDX), micro-Proton-Induced X-ray and Gamma-ray Emission (micro-PIXE/PIGE) for chemical analysis of the mineral fraction, Infrared microspectroscopy in attenuated total reflectance mode (micro-ATR-FT-IR) combined with curve-fitting for microscopic investigations and Transmission Electron Microscopy (TEM) on ultrathin sections to characterize the modifications in the mineral/organic interface at nanoscale. New criteria characterizing the effect of a thermal treatment at low temperatures on the bone structure from the macroscopic to the nanoscale were determined. There are namely a broadening of the Haversian canals, the inversion of the turns to -sheet ratio in the collagen structure determined by decomposition of the amide I IR band as well as a shift of amide II IR band position with the heating temperature to lower wavenumbers. At nanoscale, melting of the organic phase and clustering of hydroxyapatite (HAP) bone crystals can be observed. For comparison, unheated archaeological bones have been analyzed in order to test if the heat-induced modification can be distinguished from diagenetic alterations, generally dissolution-recrystallisation processes, in soils.

A Newly Identified Platelet and Megakaryocyte Lysyl Oxidase-Adhesion to Collagen Axis in Human Primary Myelofibrosis

Blood ◽  
2016 ◽  
Vol 128 (22) ◽  
pp. 3133-3133
Author(s):  
Alessandra Balduini ◽  
Vittorio Abbonante ◽  
Shinobu Matsuura ◽  
Vittorio Rosti ◽  
Katya Ravid
Keyword(s):  
Type I Collagen ◽  
Conflicts Of Interest ◽  
Lysyl Oxidase ◽  
Primary Myelofibrosis ◽  
Collagen Type I ◽  
Type I ◽  
Soluble Collagen ◽  
Peripheral Blood Cd34 ◽  
Acid Soluble Collagen

Abstract Controlling platelet function is central to management of various pathologies, including Primary Myelofibrosis (PMF), which is associated with increased incidence of thrombosis and cardiovascular disease. In recent studies we showed that the matrix cross-linking enzyme, Lysyl Oxidase (LOX) is elevated in platelets and megakartocytes of myelofibrotic mice, and transgenic upregulation of LOX increases platelet and megakaryocyte adhesion to monomeric type I collagen (preferred by alpha2β1 collagen receptors), and augments propensity for in vivo thrombosis. Here, we examined the relevance of these findings to human disease, by first determining platelet LOX level, as well as platelet and megakaryocyte adhesion to collagen using samples derived from PMF patients and matching controls. In analyzing 10 PMF platelet samples (5 males and 5 females; 6 JAK2V617F; 4 CALR mutations; age range 30-55; PMF grade 1-3), we found a nearly 20 fold upregulation of LOX expression compared to matching healthy controls (p<0.001). Intriguingly, there was a significant increase in adhesion (plt/mm2) and spreading (pixel2) of PMF platelets relative to control on monomeric, pepsinated acid soluble collagen (PSCI) (p<0.05), while no differences were observed between the samples on native triple helical acid soluble collagen type I collagen (ASCI). To examine the role of LOX in this phenotype, we treated control and PMF-derived human megakaryocytes, differentiated from peripheral blood CD34+ cells, grown in presence or not of LOX inhibitor, β-aminopropionitrile (BAPN) from day 2 of culture. Our preliminary data, based on a cohort of 2 controls and 5 PMF samples, demonstrated that although on ASCI megakaryocyte adhesion is not altered by BAPN treatment both in CTRL and PMF derived megakaryocytes, on PSCI the adhesion of PMF derived megakaryocytes was reduced by about a 50% by BAPN treatment, while the adhesion of CTRL derived MKs was not significantly affected. Taken together, we identified LOX level to be upregulated in human PMF platelets and megakaryocytes, and LOX activity to be important for PMF cells adhesion to collagen. These newly identified properties are highly relevant to megakaryocyte adhesion to the niche, and to platelet activation in PMF. Disclosures No relevant conflicts of interest to declare.

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