Novel method for fabrication of skeletal muscle construct from the C2C12 myoblast cell line using serum-free medium AIM-V

2009 ◽  
Vol 103 (5) ◽  
pp. 1034-1041 ◽  
Author(s):  
Hideaki Fujita ◽  
Kazunori Shimizu ◽  
Eiji Nagamori
1997 ◽  
Vol 29 (4) ◽  
pp. 209-216 ◽  
Author(s):  
Jae-Jeong Lee ◽  
Jai-Hyun Kwon ◽  
Yong Keun Park ◽  
Ohoak Kwon ◽  
Tai-Wook Yoon

Toxicology ◽  
2006 ◽  
Vol 219 (1-3) ◽  
pp. 73-84 ◽  
Author(s):  
Jiunn-Wang Liao ◽  
Jaw-Jou Kang ◽  
Chian-Ren Jeng ◽  
Shao-Kuang Chang ◽  
Ming-Jang Kuo ◽  
...  

PLoS ONE ◽  
2018 ◽  
Vol 13 (5) ◽  
pp. e0197934 ◽  
Author(s):  
Xi Chen ◽  
Long-Yun Li ◽  
Jin-Lan Jiang ◽  
Kai Li ◽  
Zhen-Bo Su ◽  
...  

Nutrients ◽  
2020 ◽  
Vol 12 (12) ◽  
pp. 3727
Author(s):  
Petey W. Mumford ◽  
Shelby C. Osburn ◽  
Carlton D. Fox ◽  
Joshua S. Godwin ◽  
Michael D. Roberts

There is evidence in rodents to suggest that theacrine-based supplements modulate tissue sirtuin activity as well as other biological processes associated with aging. Herein, we examined if a theacrine-based supplement (termed NAD3) altered sirtuin activity in vitro while also affecting markers of mitochondrial biogenesis. The murine C2C12 myoblast cell line was used for experimentation. Following 7 days of differentiation, myotubes were treated with 0.45 mg/mL of NAD3 (containing ~2 mM theacrine) for 3 and 24 h (n = 6 treatment wells per time point). Relative to control (CTL)-treated cells, NAD3 treatments increased (p < 0.05) Sirt1 mRNA levels at 3 h, as well as global sirtuin activity at 3 and 24 h. Follow-up experiments comparing 24 h NAD3 or CTL treatments indicated that NAD3 increased nicotinamide phosphoribosyltransferase (NAMPT) and SIRT1 protein levels (p < 0.05). Cellular nicotinamide adenine dinucleotide (NAD+) levels were also elevated nearly two-fold after 24 h of NAD3 versus CTL treatments (p < 0.001). Markers of mitochondrial biogenesis were minimally affected. Although these data are limited to select biomarkers in vitro, these preliminary findings suggest that a theacrine-based supplement can modulate select biomarkers related to NAD+ biogenesis and sirtuin activity. However, these changes did not drive increases in mitochondrial biogenesis. While promising, these data are limited to a rodent cell line and human muscle biopsy studies are needed to validate and elucidate the significance of these findings.


2014 ◽  
Vol 86 (2) ◽  
pp. 194-199 ◽  
Author(s):  
Wataru Mizunoya ◽  
Ayumi Tashima ◽  
Yusuke Sato ◽  
Ryuichi Tatsumi ◽  
Yoshihide Ikeuchi

2012 ◽  
Vol 65 (3) ◽  
pp. 363-378 ◽  
Author(s):  
Huifeng Zhang ◽  
Haibin Wang ◽  
Mei Liu ◽  
Tao Zhang ◽  
Ji Zhang ◽  
...  

1985 ◽  
Vol 5 (6) ◽  
pp. 1385-1390 ◽  
Author(s):  
P Pohjanpelto ◽  
E Hölttä ◽  
O A Jänne

We previously described an arginase-deficient, polyamine-dependent Chinese hamster ovary cell line which grows in serum-free medium. From this strain we isolated a new mutant strain that has no detectable catalytic ornithine decarboxylase activity. The mutant cells contain, however, immunoreactive ornithine decarboxylase-like protein roughly in the same quantity as the parent strain. The mutant and the parent cell line strains also contain similar amounts of ornithine decarboxylase-mRNA hybridizable to a specific cDNA. If polyamines are omitted from the medium, proliferation of the mutant cells is considerably retarded and ceases in 6 to 10 days. Addition of ornithine or alpha-difluoromethylornithine, a specific inhibitor of ornithine decarboxylase, has no effect on these cells. Putrescine and spermidine decreased in the mutant cells to undetectable levels during polyamine starvation, whereas spermine was reduced to 1/5th of that found in the control cultures. Polyamines appear to be indispensable for the mutant strain, but this was obvious only after the amount of polyamines, found as impurities in bovine serum albumin used in the medium, was reduced by dialysis to 10(-12) M. Because sera contain polyamines, the ability of the mutant strain to grow in serum-free medium is a great advantage in elucidation of the mechanisms of polyamine function.


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