Posttranslational Modifications of Bone Collagen Type I are Related to the Function of Rat Femoral Regions

2000 ◽  
Vol 66 (2) ◽  
pp. 151-156 ◽  
Author(s):  
L. Moro ◽  
M. Romanello ◽  
A. Favia ◽  
M. P. Lamanna ◽  
E. Lozupone
Keyword(s):  
Posttranslational Modifications ◽  
Collagen Type ◽  
Collagen Type I ◽  
Bone Collagen ◽  
Type I

scholarly journals Collagen transport and related pathways in Osteogenesis Imperfecta

2021 ◽  
Author(s):  
Lauria Claeys ◽  
Silvia Storoni ◽  
Marelise Eekhoff ◽  
Mariet Elting ◽  
Lisanne Wisse ◽  
...  
Keyword(s):  
Osteogenesis Imperfecta ◽  
Posttranslational Modifications ◽  
Collagen Type ◽  
Retrograde Transport ◽  
Collagen Type I ◽  
Bone Fragility ◽  
Disease Classification ◽  
Type I ◽  
Complex Process ◽  
Molecular Landscape

AbstractOsteogenesis Imperfecta (OI) comprises a heterogeneous group of patients who share bone fragility and deformities as the main characteristics, albeit with different degrees of severity. Phenotypic variation also exists in other connective tissue aspects of the disease, complicating disease classification and disease course prediction. Although collagen type I defects are long established as the primary cause of the bone pathology, we are still far from comprehending the complete mechanism. In the last years, the advent of next generation sequencing has triggered the discovery of many new genetic causes for OI, helping to draw its molecular landscape. It has become clear that, in addition to collagen type I genes, OI can be caused by multiple proteins connected to different parts of collagen biosynthesis. The production of collagen entails a complex process, starting from the production of the collagen Iα1 and collagen Iα2 chains in the endoplasmic reticulum, during and after which procollagen is subjected to a plethora of posttranslational modifications by chaperones. After reaching the Golgi organelle, procollagen is destined to the extracellular matrix where it forms collagen fibrils. Recently discovered mutations in components of the retrograde transport of chaperones highlight its emerging role as critical contributor of OI development. This review offers an overview of collagen regulation in the context of recent gene discoveries, emphasizing the significance of transport disruptions in the OI mechanism. We aim to motivate exploration of skeletal fragility in OI from the perspective of these pathways to identify regulatory points which can hint to therapeutic targets.

Alteration in serum leptin correlates with alterations in serum N-telopeptide of collagen type I and serum osteocalcin during the progression of osteoporosis in ovariectomized rats

2005 ◽  
Vol 43 (12) ◽  
Author(s):  
Anastasia Stavropoulou ◽  
Gina E. Christopoulou ◽  
George Anastassopoulos ◽  
Sofia D. Panteliou ◽  
George P. Lyritis ◽  
...  
Keyword(s):  
Bone Markers ◽  
Collagen Type ◽  
Quantitative Computed Tomography ◽  
Peripheral Quantitative Computed Tomography ◽  
Collagen Type I ◽  
Bone Collagen ◽  
Ovariectomized Rats ◽  
Type I ◽  
Serum Leptin

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.

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 ◽  
...  
Keyword(s):  
Collagen Type ◽  
Collagen Type I ◽  
Bone Collagen ◽  
Ovariectomized Rats ◽  
Type I
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