Beneficial Effects of Total Phenylethanoid Glycoside Fraction Isolated from Cistanche deserticola on Bone Microstructure in Ovariectomized Rats. (27th June 2019)

• Record Type: Journal Article
• Authors: Yang, Lingling; Ding, Shuqin; Zhang, Bo; Liu, Jingjing; Dong, Yanhong; Tang, Qiwen; Yang, Pingping; Ma, Xueqin
• Other Names: Carnevale Gianluca Academic Editor.
• Is Part Of: Oxidative medicine and cellular longevity. Volume 2019(2019)
• Publication Date: 2019-06-27
• Subjects: Oxidative stress -- Periodicals; Cells -- Aging -- Periodicals; Cells -- Aging; Oxidative stress; Oxidative Stress -- Periodicals; Cell Aging -- Periodicals; Periodicals; 611.0181
• DOI: 10.1155/2019/2370862
• Languages: English
• ISSNs: 1942-0900

Abstract

Abstract : The present study was designed to estimate the antiosteoporotic activity of total phenylethanoid glycoside fraction isolated from C. deserticola (CDP) on rats induced by ovariectomy (OVX) as well as the related mechanisms. After 3 months of oral administration, the decreased bone mineral density, serum Ca, and P in OVX rats were recovered and the deteriorated trabecular bone microarchitecture was partly improved by CDP (60, 120, and 240 mg/kg) intervention, the activities of bone resorption markers were downregulated, and the bioactive of the bone formation index was upregulated; meanwhile, the content of MDA was declined, and GSH was increased by CDP treatment. Compositionally, 8 phenylethanoid glycoside compounds were identified in CDP, with the total contents quantified as 50.3% by using the HPLC method. Mechanistically, CDP declined the levels of TRAF6, RANKL, and RANK, thus suppressing RANKL/RANK/TRAF6-induced activation of downstream NF- κ B and PI3K/AKT signaling pathways and ultimately preventing activities of the key osteoclastogenic proteins of NFAT2 and c-Fos. All of the above data implied that CDP exhibited beneficial effects on bone microstructure in ovariectomized rats, and these effects may be related to the NF- κ B and PI3K/AKT signaling pathways which were triggered by the binding of RANKL, RANK, and TRAF6.