Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 2 de 2
Filter
Add more filters










Database
Language
Publication year range
1.
Lett Appl Microbiol ; 73(3): 383-391, 2021 Sep.
Article in English | MEDLINE | ID: mdl-34173250

ABSTRACT

This study was conducted to investigate the inhibitory effects of the cell-free culture supernatant of Lactobacillus curvatus Wikim 38 (LC38-CS) on RANKL-induced osteoclast differentiation and bone loss in a mice model of ovariectomy-induced post-menopausal osteoporosis. LC38-CS inhibited the RANKL-induced differentiation of bone marrow-derived macrophages (BMDMs) into osteoclasts in a dose-dependent manner. F-actin ring formation and bone resorption were also reduced by LC38-CS treatment of RANKL-treated BMDMs. In addition, LC38-CS decreased the RANKL-induced activation of the TRAF6/NF-κB/MAPKs axis at the early stage and the expression of osteoclastogenesis-related genes in BMDMs treated with RANKL. PRMT1 and ADMA levels, new biomarkers for osteoclastogenesis, were decreased by LC38-CS treatment. The administration of LC38-CS increased bone volume and bone mineral density in ovariectomized mice in µ-CT analysis. These findings suggest that LC38-CS inhibited RANKL-induced osteoclast differentiation by the downregulation of molecular mechanisms and exerted anti-osteoporotic effects.


Subject(s)
Bone Resorption , Osteoclasts , Animals , Cell Differentiation , Female , Lactobacillus , Mice , NF-kappa B
2.
J Dairy Sci ; 95(1): 15-9, 2012 Jan.
Article in English | MEDLINE | ID: mdl-22192180

ABSTRACT

Molecular weights (MW) of major proteins in milk of 3 Korean dairy goat breeds were determined by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, after treatment of milk samples with the reduction buffer used in capillary electrophoresis. The MW of caprine milk proteins were compared with those of Holstein milk counterparts using commercial bovine milk protein standards. The MW of α-lactalbumin, ß-lactoglobulin, and α- and ß-casein standards were 14,197±3.4, 18,326±26.3, 23,591±13.0, and 23,967±12.8 m/z, respectively, whereas those of Holstein milk treated with the reduction buffer were 14,199±8.3, 18,397±25.9, 23,614±64.8, and 23,984±75.6 m/z, respectively. The respective MW of α-lactalbumin in Saanen, Toggenberg, and Alpine milk were 14,194±27.2, 14,266±105.9, and 14,241±13.2 m/z, which were not different from those of the bovine milk. The respective MW of ß- lactoglobulin in corresponding caprine milk were 18,840±31.5, 18,856±26.3, and 18,857±21.3 m/z, which were higher than those in the bovine milk. The MW of ß-casein in corresponding caprine milk were 23,860±27.2, 23,886±12.3, and 23,901±8.4 m/z, which were lower than those in the bovine milk. The results indicated that matrix-assisted laser desorption/ionization time-of-flight mass spectrometry could be used for rapid determination of MW of Korean caprine milk proteins without protein separation steps.


Subject(s)
Milk Proteins/chemistry , Animals , Caseins/chemistry , Cattle , Goats , Lactalbumin/chemistry , Lactoglobulins/chemistry , Molecular Weight , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
SELECTION OF CITATIONS
SEARCH DETAIL
...