scholarly journals Octanoate in Human Albumin Preparations Is Detrimental to Mesenchymal Stromal Cell Culture

2015 ◽  
Vol 2015 ◽  
pp. 1-8 ◽  
Author(s):  
Way-Wua Wong ◽  
Andrew D. MacKenzie ◽  
Vicky J. Nelson ◽  
James M. Faed ◽  
Paul R. Turner

Cell therapies hold great promise as the next major advance in medical treatment. To enable safe, effectiveex vivoculture whilst maintaining cell phenotype, growth media constituents must be carefully controlled. We have used a chemically defined mesenchymal stromal cell culture medium to investigate the influence of different preparations of human serum albumin. We examined two aspects of cell culture, growth rate as measured by population doubling time and colony forming ability which is a representative measure of the stemness of the cell population. Albumin preparations showed comparative differences in both of these criteria. Analysis of the albumin bound fatty acids also showed differences depending on the manufacturing procedure used. We demonstrated that octanoate, an additive used to stabilize albumin during pasteurization, slows growth and lowers colony forming ability duringex vivoculture. Further to this we also found the level of Na+/K+ATPase, a membrane bound cation pump inhibited by octanoate, is increased in cells exposed to this compound. We conclude that the inclusion of human serum albumin inex vivogrowth media requires careful consideration of not only the source of albumin, but also the associated molecular cargo, for optimal cell growth and behavior.

2020 ◽  
Vol 8 (14) ◽  
pp. 3819-3829
Author(s):  
Ngoc Nhi T. Le ◽  
Tianran Leona Liu ◽  
James Johnston ◽  
John D. Krutty ◽  
Kayla Marie Templeton ◽  
...  

Synthetic hydrogel arrays combined with a design of experiments approach identified hydrogel compositions for media-agnostic human mesenchymal stromal cell culture.


2014 ◽  
Vol 27 (9) ◽  
pp. 1566-1574 ◽  
Author(s):  
Davide Garzon ◽  
Adriana Ariza ◽  
Luca Regazzoni ◽  
Riccardo Clerici ◽  
Alessandra Altomare ◽  
...  

Endocrinology ◽  
2005 ◽  
Vol 146 (7) ◽  
pp. 3052-3058 ◽  
Author(s):  
Lucie Jetté ◽  
Roger Léger ◽  
Karen Thibaudeau ◽  
Corinne Benquet ◽  
Martin Robitaille ◽  
...  

Abstract In vivo bioconjugation to the free thiol on Cys34 of serum albumin by a strategically placed reactive group on a bioactive peptide is a useful tool to extend plasma half-life. Three maleimido derivates of human GH-releasing factor (hGRF)1–29 were synthesized and bioconjugated to human serum albumin ex vivo. All three human serum albumin conjugates showed enhanced in vitro stability against dipeptidylpeptidase-IV and were bioactive in a GH secretion assay in cultured rat anterior pituitary cells. When the maleimido derivatives were individually administered sc to normal male Sprague Dawley rats, an acute secretion of GH was measured in plasma. The best compound, CJC-1295, showed a 4-fold increase in GH area under the curve over a 2-h period compared with hGRF1–29. CJC-1295, a tetrasubstituted form of hGRF1–29 with an added Nε-3-maleimidopropionamide derivative of lysine at the C terminus, was selected for further pharmacokinetic evaluation, where it was found to be present in plasma beyond 72 h. A Western blot analysis of the plasma of a rat injected with CJC-1295 showed the presence of a CJC-1295 immunoreactive species on the band corresponding to serum albumin, appearing after 15 min and remaining in circulation beyond 24 h. These results led to the identification of CJC-1295 as a stable and active hGRF1–29 analog with an extended plasma half-life.


2019 ◽  
Vol 2019 ◽  
pp. 1-9 ◽  
Author(s):  
Miaomiao Chen ◽  
Xiaoshuang Zuo ◽  
Qinqin Xu ◽  
Rong Wang ◽  
Suhua Fan ◽  
...  

Nanodiamonds (NDs) have been recognized as emerging carbon-based delivery vehicles due to their biocompatibility. NDs were reported to be nontoxic and suited for biomedical applications in the complete cell culture medium. However, in this study, the cytotoxicity of NDs in serum-free medium was studied and indicated that serum proteins in cell culture medium played significant effect on the toxicity of NDs. Therefore, the interaction mechanism between NDs and a serum protein (human serum albumin, HSA) was first investigated by fluorescence quenching technique and circular dichroism (CD) spectrometry. The results suggest that HSA strongly bonds on the NDs surface to form “protein corona,” which not only prevents the aggregation of NDs and improves its stability but also inhibits the cytotoxicity of NDs. In serum-free medium, NDs exhibited obvious toxicity toward the human lung epithelial cell line (BEAS-2B) and showed concentration-dependent cytotoxicity. In the presence of bovine serum albumin (BSA), which shares structural homology and similar properties with HSA, toxicity of NDs was apparently inhibited. Therefore, the interaction between serum protein and NDs should be considered in the understanding of the biological effects of NDs exposure in biomedical applications.


Cytotherapy ◽  
2015 ◽  
Vol 17 (2) ◽  
pp. 163-173 ◽  
Author(s):  
Allen Kuan-Liang Chen ◽  
Yi Kong Chew ◽  
Hong Yu Tan ◽  
Shaul Reuveny ◽  
Steve Kah Weng Oh

2005 ◽  
Vol 14 (5) ◽  
pp. 569-581 ◽  
Author(s):  
Li-Fen Huang ◽  
Yu-Kuo Liu ◽  
Chung-An Lu ◽  
Shie-Liang Hsieh ◽  
Su-May Yu

Cytotherapy ◽  
2014 ◽  
Vol 16 (5) ◽  
pp. 683-691 ◽  
Author(s):  
Suphakde Julavijitphong ◽  
Suparat Wichitwiengrat ◽  
Nednapis Tirawanchai ◽  
Pornpimol Ruangvutilert ◽  
Chanchai Vantanasiri ◽  
...  

2001 ◽  
Vol 114 (3) ◽  
pp. 681-689 ◽  
Author(s):  
Hiroto Araki ◽  
Naoyuki Katayama ◽  
Hidetsugu Mitani ◽  
Hirohito Suzuki ◽  
Hiroyoshi Nishikawa ◽  
...  

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