Alpha-methyl-proline restores normal levels of bone collagen type i synthesis in ovariectomized rats

Life Sciences ◽  
1995 ◽  
Vol 57 (24) ◽  
pp. 2245-2252 ◽  
Author(s):  
G. Lubec ◽  
O. Labudova ◽  
D. Seebach ◽  
A. Beck ◽  
H. Hoeger ◽  
...  
Author(s):  
Anastasia Stavropoulou ◽  
Gina E. Christopoulou ◽  
George Anastassopoulos ◽  
Sofia D. Panteliou ◽  
George P. Lyritis ◽  
...  

AbstractThe role of leptin during the progression of osteoporosis was investigated in ovariectomized rats by correlation of serum leptin levels with N-telopeptide of collagen type I (NTx) and osteocalcin levels before ovariectomy and 20, 40 and 60days after the operation. Furthermore, peripheral quantitative computed tomography was used to confirm the development of severe osteoporosis in rats on day 60. The levels of NTx and osteocalcin were significantly increased on day 20 [61.9±5.4nM BCE (bone collagen equivalents) and 215.6±53.3ng/mL, respectively] in comparison to those before ovariectomy (41.3±1.7nM BCE and 60.4±10.9ng/mL). Accordingly, leptin was significantly elevated on day 20 (3033±661 vs. 606±346 pg/mL before ovariectomy). Bone markers and leptin levels remained constant up to day 40, while a slight, but not statistically significant, decrease was noted for osteocalcin and leptin on day 60. Although leptin and bone markers did not correlate before ovariectomy (r=0.09 for NTx and r=−0.05 for osteocalcin), strong correlation was observed at all time points after ovariectomy. The data obtained suggest that the alterations in serum leptin levels during the progression of osteoporosis in ovariectomized rats follow the alterations in bone markers.


2007 ◽  
Vol 19 (4) ◽  
pp. 547-552 ◽  
Author(s):  
Diaa E. E. Rizk ◽  
Hazem A. Hassan ◽  
Ahmed H. Al-Marzouqi ◽  
Gaber A. Ramadan ◽  
Soha S. Al-Kedrah ◽  
...  

2000 ◽  
Vol 66 (2) ◽  
pp. 151-156 ◽  
Author(s):  
L. Moro ◽  
M. Romanello ◽  
A. Favia ◽  
M. P. Lamanna ◽  
E. Lozupone

1991 ◽  
Vol 274 (2) ◽  
pp. 615-617 ◽  
Author(s):  
P Kern ◽  
M Menasche ◽  
L Robert

The biosynthesis of type I, type V and type VI collagens was studied by incubation of calf corneas in vitro with [3H]proline as a marker. Pepsin-solubilized collagen types were isolated by salt fractionation and quantified by SDS/PAGE. Expressed as proportions of the total hydroxyproline solubilized, corneal stroma comprised 75% type I, 8% type V and 17% type VI collagen. The rates of [3H]proline incorporation, linear up to 24 h for each collagen type, were highest for type VI collagen and lowest for type I collagen. From pulse-chase experiments, the calculated apparent half-lives for types I, V and VI collagens were 36 h, 10 h and 6 h respectively.


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