Ca2+-activated mitochondrial biogenesis and functions improve stem cell fate in Rg3-treated human mesenchymal stem cells
STEM CELL RESEARCH & THERAPY
Authors: Hong, Taeui; Kim, Moon Young; Ly, Dat Da; Park, Su Jung; Eom, Young Woo; Park, Kyu-Sang; Baik, Soon Koo
Abstract
Although mitochondrial functions are essential for cell survival, their critical roles in stem cell fate, including proliferation, differentiation, and senescence, remain elusive. Ginsenoside Rg3 exhibits various biological activities and reportedly increases mitochondrial biogenesis and respiration. Herein, we observed that Rg3 increased proliferation and suppressed senescence of human bone marrow-derived mesenchymal stem cells. Osteogenic, but not adipogenic, differentiation was facilitated by Rg3 treatment. Rg3 suppressed reactive oxygen species production and upregulated mitochondrial biogenesis and antioxidant enzymes, including superoxide dismutase. Consistently, Rg3 strongly augmented basal and ATP synthesis-linked respiration with high spare respiratory capacity. Rg3 treatment elevated cytosolic Ca2+ concentration contributing to mitochondrial activation. Reduction of intracellular or extracellular Ca2+ levels strongly inhibited Rg3-induced activation of mitochondrial respiration and biogenesis. Taken together, Rg3 enhances capabilities of mitochondrial and antioxidant functions mainly through a Ca2+-dependent pathway, which improves the proliferation and differentiation potentials and prevents the senescence of human mesenchymal stem cells.
Effect and mechanism of calcium ions on the gelation properties of cellulose nanocrystals-whey protein isolate composite gels
FOOD HYDROCOLLOIDS
Authors: Xiao, Yaqing; Kang, Shufang; Liu, Yingnan; Guo, Xinyu; Li, Mei; Xu, Huaide
Abstract
This study aimed to evaluate the effect of calcium ions (Ca2+) on the thermal gelling properties of cellulose nanocrystals-whey protein isolate composite gels, as well as to propose a corresponding ion-induced gelation mechanism. It was found that the gel strength, viscoelasticity, and thermal stability of the mixed gels gradually improved with an increase in the Ca2+ concentration from 0 M to 0.15 M. The addition of an appropriate Ca2+ could induce the conformational transformation from alpha-helix to beta-sheet, increase the content of tryptophan residues and reactive sulfhydryl groups, and enhance the hydrophobic interactions and the amide II band, which promoted the full unfolding and orderly aggregation of protein molecules to form a stable three-dimensional gel network. However, 0.20 M Ca2+ resulted in the formation of a coarse gel structure with some irregular aggregates, thereby leading to the decreased water holding capacity and gel strength. This research offers a theoretical foundation for the design and development of novel composite food gels with various functional properties.