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.

scholarly journals THE HISTOLOGICAL, EXTRACTION AND CHARACTERIZATION COLLAGENS YELLOW-PIKE CONGER Muarenesox talabon

2018 ◽  
Vol 9 (2) ◽  
pp. 665-683 ◽  
Author(s):  
Dewi Setiyowati Gadi ◽  
Wini Trilaksani ◽  
Tati Nurhayati
Keyword(s):  
Heavy Metals ◽  
Thermal Stability ◽  
Amino Acids ◽  
Type I Collagen ◽  
Raw Material ◽  
Acid Extraction ◽  
Type I ◽  
Swim Bladder ◽  
Molecular Weights ◽  
Acid Soluble Collagen

By product Muarenesox talabon swim bladders can be used as a raw material for desperately needed in the food, biomedical, pharmaceutical, and cosmeceuticals industries. The aims of the research were to observed the histological and determine chemical characteristics of swim bladder including proximate and amino acids; extraction of acid soluble collagen and determine the characteristics of collagen including proximate, pH, heavy metals, microbial, amino acids, functional groups, molecular weights, and thermal stability. The morphology of cunang swim bladder consists of outer, middle, and inner layers containing collagen fibers; 33.67±0.71%wb and protein whichwere dominated by three amino acids that were glycine, proline, and alanine. Pretreatment by 0.1 M NaOH for 8 hours (K1T4) and acid extraction by 0.25 M acetic acid for 72 hours (M1T3) was the best treatment yielding 14.51± 0.43% of collagen; having 12.12±0.04% wb of moisture; 88.54 ± 0.08% wb of protein; 1.31±0.23% wb of fat; 0.17±0.03% wb of ash. Not detected any heavy metals (Pb, Hg, As, Cd). Acidity pH was 4.31 and negative of E. coli and Salmonella. The main amino acids detected were glycine 241.06 mg/g; proline 88.73mg/g; and alanine 86,98 mg/g; FTIR spectra were revealed the presence of triple helix structures; electrophoresis patterns consisted of 136 kDa of mol weight of α1 and 117 kDa of mol weight of α2 were characterisedto be type I collagen; which had Tmax of 195.59ºC and ΔH 7.8113 J/g. Keywords: acid extraction, swim bladder, collagens, thermal stability

The anti-skin-aging effect of oral administration of gelatin from the swim bladder of Amur sturgeon (Acipenser schrenckii)

2019 ◽  
Vol 10 (7) ◽  
pp. 3890-3897 ◽  
Author(s):  
Lin Wang ◽  
Xiaoxiao Wang ◽  
Fan Bai ◽  
Yong Fang ◽  
Jinlin Wang ◽  
...  
Keyword(s):  
Oral Administration ◽  
Type I Collagen ◽  
Aging Effect ◽  
Skin Aging ◽  
Hot Water ◽  
Type I ◽  
Swim Bladder ◽  
Amur Sturgeon

Gelatin was extracted from the swim bladder of Amur sturgeon with hot water at 50 °C with acceptable yield (76.54%) and it showed and type I collagen features.

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.

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 Thermal stability of human-fibroblast-collagenase-cleavage products of type-I and type-III collagens

1987 ◽  
Vol 247 (3) ◽  
pp. 725-729 ◽  
Author(s):  
C C Danielsen
Keyword(s):  
Thermal Stability ◽  
Human Fibroblast ◽  
Type I Collagen ◽  
Type Iii Collagen ◽  
Type I ◽  
Type Iii ◽  
Melting Temperatures ◽  
Large Type ◽  
Fibroblast Collagenase ◽  
Thermal Stability Of

Rat skin type-I and type-III collagens were degraded by human fibroblast collagenase at a temperature below the ‘melting’ temperature for the two resulting fragments, namely the N-terminal three-fourths, TCA, and the C-terminal one-fourth, TCB. The specific cleavage of the collagen was confirmed by electrophoresis and determination of molecular length by electron microscopy. The two fragments were separated by gel filtration and the thermal stabilities of the isolated fragments were determined. For type-I collagen, the ‘melting’ temperatures of the two fragments were found to differ by only 0.5 degrees C and were 4.5-5.0 degrees C below that of the uncleaved molecule. The ‘melting’ temperatures of the uncleaved molecule and the N-terminal fragment were independent of the extent of N-terminal intramolecular cross-linking. For type-III collagen, the ‘melting’ temperatures of the fragments were found to differ by 1.3 degrees C. The small fragments of the two types of collagen ‘melted’ at the same temperature, whereas the large type-III fragment ‘melted’ at a slightly higher temperature than did the large type-I fragment. Reduction of the disulphide bonds located in the C-terminal type-III fragment did not affect the thermal stability of this fragment. The thermal stability of uncleaved type-III collagen was found to be variable, but the reason for this is not known at present.

Changes in mechanical properties, thermal stability, reducible cross-links and glycosyl-lysines in rat skin induced by corticosteroid treatment

1982 ◽  
Vol 101 (2) ◽  
pp. 312-320 ◽  
Author(s):  
Hans Oxlund ◽  
Trevor Sims ◽  
Nicholas D. Light
Keyword(s):  
Thermal Stability ◽  
Type I Collagen ◽  
Corticosteroid Treatment ◽  
Biochemical Properties ◽  
Type Iii Collagen ◽  
Type I ◽  
Clinical Observations ◽  
Skin Collagen ◽  
Lysine Residues ◽  
Cross Links

Abstract. The effects of systemic cortisol treatment on the biophysical and biochemical properties of skin were investigated. Rats were injected sc with cortisol for 14, 60 and 120 days and samples of lumbar skin were studied. Corticosteroids exert a biphasic effect on the strength of skin: 1) a relatively fast increase in the strength and stability, caused by an increased collagen cross-linking and 2) an inhibited collagen synthesis which ultimately results in a thinning of the skin and a decrease of collagen content consistent with clinical observations. The thermal stability is increased indicating an increased proportion of thermostable cross-links in skin collagen. No changes are observed in the percentage type III collagen with respect to type I collagen. Increased amounts of glucose attached to the ε-amino group of lysine residues in the collagen are found after long-term treatments, an alteration which may play a role in hampering the tissue functions.

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