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Wyszukujesz frazę "marine collagen" wg kryterium: Temat


Wyświetlanie 1-2 z 2
Tytuł:
Hydrolyzed Collagen from Salmon Skin Increases the Migration and Filopodia Formation of Skin Keratinocytes by Activation of FAK/Src Pathway
Autorzy:
Woonnoi, Wanwipha
Chotphruethipong, Lalita
Tanasawet, Supita
Benjakul, Soottawat
Sutthiwong, Nuthathai
Sukketsiri, Wanida
Powiązania:
https://bibliotekanauki.pl/articles/1417272.pdf
Data publikacji:
2021-09-03
Wydawca:
Instytut Rozrodu Zwierząt i Badań Żywności Polskiej Akademii Nauk w Olsztynie
Tematy:
cell culture
keratinocyte stem cells
marine collagen
re-epithelialization
skin barrier
wound healin
Opis:
Previous studies reported hydrolyzed collagen increase cell proliferation and migration involved in the wound repair process. Nevertheless, the knowledge related with wound repair mechanism of hydrolyzed collagen from salmon skin (HCSS) has not been fully elucidated. Therefore, this study aimed to elucidate the effects of HCSS on the migration of keratinocyte HaCaT cells. Additionally, its molecular mechanism through cell division control protein 42 (Cdc42), Ras-related C3 botulinum toxin substrate 1 (Rac1), and Ras homolog family member A (RhoA) via focal adhesion kinase (FAK)-steroid receptor coactivator (Src) regulation and keratinocyte stem cells (KSCs) markers were also evaluated. After 24 h of incubation, keratinocyte proliferation was detected by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) and double stranded DNA (dsDNA) assays, and by determining the total cellular protein content. Keratinocyte migration and filopodia formation were measured by wound healing assay and phalloidin‐rhodamine staining, respectively. The migratory related proteins were evaluated by western blot analysis. HCSS had a high content of hydrophobic amino acids and imino acids. HaCaT cell proliferation and migration were significantly increased in response to HCSS at the concentration of 100-1000 μg/mL. The formation of filopodia was subsequently increased in response to HCSS at concentrations of 100-1000 μg/mL. Moreover, HCSS upregulated Cdc42, Rac1, and RhoA protein expression and activated the phosphorylation of FAK and Src pathway. HCSS at the concentration of 100-1000 μg/mL could trigger stemness by increased KSC markers, including keratin 19 and β-catenin expression. This study has demonstrated that HCSS induces proliferation and migration of keratinocytes, subsequently promotes the second phase of wound healing process by FAK-Src activation and also increases the KSC properties.
Źródło:
Polish Journal of Food and Nutrition Sciences; 2021, 71, 3; 323-332
1230-0322
2083-6007
Pojawia się w:
Polish Journal of Food and Nutrition Sciences
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Characteristic of fish collagen films cross-linked with glutaraldehyde
Autorzy:
Kulka-Kamińska, Karolina
Brudzyńska, Patrycja
Sionkowska, Alina
Lewandowska, Katarzyna
Piwowarski, Łukasz
Powiązania:
https://bibliotekanauki.pl/articles/27324037.pdf
Data publikacji:
2023
Wydawca:
Akademia Górniczo-Hutnicza im. Stanisława Staszica w Krakowie. Polskie Towarzystwo Biominerałów
Tematy:
collagen
glutaraldehyde
cross-linking
polymer films
marine sources
kolagen
biomateriały
polimery
Opis:
Collagen is a valuable biopolymer in many fields, especially in biomedical sciences. Thanks to its biodegradability and high biocompatibility, it is a desirable material for applications that require contact with the human body. There are many sources of collagen, of which marine-origin collagen has become an important one in recent times. Pure collagen has poor stability and is sensitive to the effects of heat and other external factors. The cross-linking process can improve the properties of collagen materials. Many different methods of cross-linking can be distinguished, including chemical ones. In this study, we were concerned to obtain collagen films modified with glutaraldehyde (GTA). The influence of this additive on the chemical, mechanical, swelling, and hydrophilic properties of the biopolymeric matrix was evaluated. Two different concentrations of collagen were used, as well as three different concentrations of GTA. Results of the analysis showed that the properties of the obtained films were affected by the addition of even a small amount of cross-linker. Spectroscopic measurements indicated minor changes that reflect interactions between GTA and the collagen matrix. Mechanical tests showed changes for modified samples in values of tensile strength, breaking force, and elongation at break. The hydrophilicity decreased slightly for films with GTA. The durability of the modified samples in the swelling test increased. Differences between 1% and 2% collagen films with additives were also observed. The GTA-obtained fish collagen films can be promising materials for biomedical applications.
Źródło:
Engineering of Biomaterials; 2023, 26, 168; 25--32
1429-7248
Pojawia się w:
Engineering of Biomaterials
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-2 z 2

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