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 ◽  
...  

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.

2010 ◽  
Vol 109 (3) ◽  
pp. 840-848 ◽  
Author(s):  
Chau-Zen Wang ◽  
Gwo-Jaw Wang ◽  
Mei-Ling Ho ◽  
Yan-Hsiung Wang ◽  
Ming-Long Yeh ◽  
...  

Whole body vibration training is widely used in rehabilitation and sports activities to improve muscle strength, balance, and flexibility. However, the molecular mechanisms of vertical vibration (VV) training and their effect on the myogenesis of myoblasts remain undefined. This study was undertaken to address the hypothesis that VV can enhance the expression of ECM proteins and myogenic regulatory factors (MRFs) in myoblasts and, in turn, increase myotube formation. Using real-time PCR, Western blot analysis, and immunofluorescence studies, we examined the effect of VV treatment with frequencies of 5, 8, or 10 Hz on the expression of ECM proteins and MRFs as well as myotube formation in C2C12 myoblasts. We showed that VV stimulation is safe and effective at stimulating myogenesis in C2C12 myoblasts. The levels of expression of the ECM proteins type I collagen and decorin were the highest after VV treatment at frequencies of 8 and 10 Hz. Expression of the MRFs MyoD and myogenin increased after VV stimulation in a time- and dose-dependent manner. The total number of myotubes formed, as well as the length and the average area of myotubes, were substantially increased following VV treatment at frequencies of 8 to 10 Hz. In conclusion, VV treatment at frequencies of 8 to 10 Hz can stimulate the expression of ECM proteins and MRFs in myoblasts and, in turn, increase myotube formation.


2015 ◽  
Vol 3 (39) ◽  
pp. 7658-7666 ◽  
Author(s):  
Md. Tariful Islam Mredha ◽  
Xi Zhang ◽  
Takayuki Nonoyama ◽  
Tasuku Nakajima ◽  
Takayuki Kurokawa ◽  
...  

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.


2018 ◽  
Vol 17 (2) ◽  
pp. 206-213
Author(s):  
Wang Yan-Bo ◽  
Li Xiao-Hui ◽  
Zhou Jin-Ru ◽  
Zhang Yan ◽  
Ma Ai-Jin ◽  
...  

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.


Soft Matter ◽  
2014 ◽  
Vol 10 (44) ◽  
pp. 8855-8863 ◽  
Author(s):  
Christopher Allen Rucksack Jones ◽  
Long Liang ◽  
Daniel Lin ◽  
Yang Jiao ◽  
Bo Sun

Type I collagen abounds in mammalian extracellular matrix (ECM) and is crucial to many biophysical processes.


Author(s):  
Arthur J. Wasserman ◽  
Kathy C. Kloos ◽  
David E. Birk

Type I collagen is the predominant collagen in the cornea with type V collagen being a quantitatively minor component. However, the content of type V collagen (10-20%) in the cornea is high when compared to other tissues containing predominantly type I collagen. The corneal stroma has a homogeneous distribution of these two collagens, however, immunochemical localization of type V collagen requires the disruption of type I collagen structure. This indicates that these collagens may be arranged as heterpolymeric fibrils. This arrangement may be responsible for the control of fibril diameter necessary for corneal transparency. The purpose of this work is to study the in vitro assembly of collagen type V and to determine whether the interactions of these collagens influence fibril morphology.


2007 ◽  
Vol 177 (4S) ◽  
pp. 314-314 ◽  
Author(s):  
Joon-Yang Kim ◽  
Hoon Seog Jean ◽  
Beom Joon Kim ◽  
Kye Yong Song

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