title: Study on pretreatment of FPS-1 in rats with hepatic ischemia-reperfusion injury.
abstract: This study was designed to determine whether FPS-1, the water-soluble polysaccharide isolated from fuzi, protected against hepatic damage in hepatic ischemia-reperfusion injury in rats, and its mechanism. SD rats were subjected to 60 min of hepatic ischemia, followed by 120 min reperfusion. FPS-1 (160 mg/kg/day) was administered orally for 5 days before ischemia-reperfusion injury in treatment group. Serum aspartate aminotransferase (AST), alanine aminotransferase (ALT) and albumin (ALB) were assayed to evaluate liver functions. Liver samples were taken for histological examination and determination of malondialdehyde (MDA), superoxide dismutase (SOD), that catalase (CAT) in liver. Na(+)-K(+)-ATPase and Ca(2+)-ATPase in mitochondria were measured with colorimetry method. Morphological changes were also investigated by using both light microscopy and electron microscopy (EM). In addition, apoptosis and oncosis were detected by Annexin V-FITC/PI immunofluorescent flow cytometry analysis. Serum AST and ALT levels were elevated in groups exposed to ischemia-reperfusion (p < 0.05). Ischemia-reperfusion caused a marked increase in MDA level, and significant decreases in hepatic SOD and CAT (p < 0.05). Na(+)-K(+)-ATPase and Ca(2+)-ATPase were reduced in ischemia-reperfusion groups compared to the sham group (p < 0.05). Oncosis and apoptosis were also observed in ischemia-reperfusion groups. Pretreatment with FPS-1 reversed all these biochemical parameters as well as histological alterations, evidently by increased SOD, CAT, reduced MDA and histological scores compared to the model group (p < 0.05). FPS-1 could attenuate the necrotic states by the detection of immunofluorescent flow cytometry analysis. Pretreatment with FPS-1 reduced hepatic ischemia-reperfusion injury through its potent antioxidative effects and attenuation of necrotic states.
authors.affiliation: Department of Anesthesiology, The First Affiliated Hospital of Zhongshan University, Guangzhou 510800, China.
authors.forename: Shiqing
authors.initials: S
authors.lastname: Lin
authors.forename: Kexuan
authors.initials: K
authors.lastname: Liu
authors.forename: Weikang
authors.initials: W
authors.lastname: Wu
authors.forename: Chao
authors.initials: C
authors.lastname: Chen
authors.forename: Zhi
authors.initials: Z
authors.lastname: Wang
authors.forename: Xuanhong
authors.initials: X
authors.lastname: Zhang
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism; D000410:Alanine Transaminase / Q000378:metabolism; D000418:Albumins / Q000378:metabolism; D000818:Animals; D001219:Aspartate Aminotransferases / Q000378:metabolism; D002374:Catalase / Q000378:metabolism; D008099:Liver / Q000098:blood supply* / Q000648:ultrastructure; D008297:Male; D008315:Malondialdehyde / Q000378:metabolism; D008854:Microscopy, Electron; D018384:Oxidative Stress; D011134:Polysaccharides / Q000627:therapeutic use*; D051381:Rats; D017207:Rats, Sprague-Dawley; D015427:Reperfusion Injury / Q000188:drug therapy* / Q000201:enzymology / Q000378:metabolism; D013482:Superoxide Dismutase / Q000378:metabolism
chemical_list: D000418:Albumins; C510406:FPS-1 polysaccharide; D011134:Polysaccharides; D008315:Malondialdehyde; D002374:Catalase; D013482:Superoxide Dismutase; D001219:Aspartate Aminotransferases; D000410:Alanine Transaminase; D000251:Adenosine Triphosphatases