Effects of Artesunate on the Expressions of Insulin-Like Growth Factor-1, Osteopontin and C-Telopeptides of Type II Collagen in a Rat Model of Osteoarthritis

Pharmacology ◽  
2017 ◽  
Vol 101 (1-2) ◽  
pp. 1-8 ◽  
Author(s):  
Zhe Bai ◽  
Xiao-Hui Guo ◽  
Chi Tang ◽  
Si-Tong Yue ◽  
Long Shi ◽  
...  

Objective: The study aims to explore the effects of artesunate on insulin-like growth factor-1 (IGF-1), Osteopontin (OPN), and C-telopeptides of type II collagen (CTX-II) in serum, synovial fluid (SF), and cartilage tissues of rats with osteoarthritis (OA). Methods: OA models were established. Normal model, artesunate, and Viatril-S groups (20 rats respectively) were set. Enzyme-linked immunosorbent assay, IHC staining, and quantitative real-time polymerase chain reaction were conducted to calculate IGF-1, OPN, and CTX-II levels in serum, SF, and cartilage tissues of rats. The pathological changes in cartilage tissues were evaluated with Mankin score and Hematoxylin-Eosin staining. Results: Compared with the normal group, the model group showed increased IGF-1 level; decreased OPN, CTX-II levels in the serum and SF; and contrary results were seen in the cartilage tissues. A gradual ascending IGF-1 level and descending OPN and CTX-II levels existed in the serum and SF in the artesunate and Viatril-S groups after 2 weeks. The model group showed the most obvious pathological changes and highest Mankin score compared with the other groups. Higher IGF-1 level and lower OPN, CTX-II levels were exhibited in the cartilage tissue in the artesunate and Viatril-S groups but not in the model group. Conclusion: Artesunate and Viatril-S inhibit OA development by elevating IGF-1 level and reducing OPN and CTX-II levels.

2015 ◽  
Vol 36 (6) ◽  
pp. 2480-2493 ◽  
Author(s):  
Guoqing Du ◽  
Yi Song ◽  
Lei Wei ◽  
Linghui Li ◽  
Xuezong Wang ◽  
...  

Background/Aims: Cartilage destruction is thought to be the major mediator of osteoarthritis. Recent studies suggest that inhibition of subchrondral bone loss by anti-osteoporosis (OP) drug can protect cartilige erosion. Osthole, as a promising agent for treating osteoporosis, may show potential in treating osteoarthritis. The purpose of this study was to investigate whether Osthole affects the proliferation and catabolism of rat chondrocytes, and the degeneration of cartilage explants. Methods: Rat chondrocytes were treated with Osthole (0 μM, 6.25 μM, 12.5 μM, and 25 μM) with or without IL1-β (10ng/ml) for 24 hours. The expression levels of type II collagen and MMP13 were detected by western Blot. Marker genes for chondrocytes (A-can and Sox9), matrix metalloproteinases (MMPs), aggrecanases (ADAMTS5) and genes implicated in extracellular matrix catabolism were evaluated by qPCR. Cell proliferation was assessed by measuring proliferating cell nuclear antigen (PCNA) expression and fluorescence activated cell sorter. Wnt7b/β-catenin signaling was also investigated. Cartilage explants from two-week old SD rats were cultured with IL-1β, Osthole and Osthole plus IL-1β for four days and glycosaminoglycan (GAG) synthesis was assessed with toluidine blue staining and Safranine O/Fast Green FCF staining, collagen type II expression was detected by immunofuorescence. Results: Osthole reduced expression of chondrocyte markers and increased expression of MMP13, ADAMTS5 and MMP9 in a dose-dependent manner. Catabolic gene expression levels were further improved by Osthole plus IL-1β. Osthole inhibited chondrocyte proliferation. GAG synthesis and type II collagen were decreased in both the IL-1β groups and the Osthole groups, and significantly reduced by Osthole plus IL-1β. Conclusions: Our data suggested that Osthole increases the catabolism of rat chondrocytes and cartilage explants, this effect might be mediated through inhibiting Wnt7b/β-catenin pathway.


2010 ◽  
Vol 37 (7) ◽  
pp. 1519-1526 ◽  
Author(s):  
CRISTIANE S. MARA ◽  
ADRIANA S.S. DUARTE ◽  
ANGELICA SARTORI ◽  
ANGELA C. LUZO ◽  
SARA T.O. SAAD ◽  
...  

Objective.Mature articular cartilage is vulnerable to injuries and disease processes that cause irreversible tissue damage because of its limited capacity for self-repair. Umbilical cord blood is a source of mesenchymal stem cells, which can give rise to cells of different lineages, including cartilage, bone, and fat. Cellular condensation is a required step in the initiation of mesenchymal chondrogenesis. We attempted to differentiate cells from umbilical cord blood into chondrocytes with insulin-like growth factor 1 (IGF-1) and transforming growth factor-ß3 (TGF-ß3).Methods.Cells were grown in high density micromass and monolayer culture systems and then evaluated for expression of type II collagen, aggrecan, and Sox9. Umbilical cord blood from 130 patients was harvested.Results.Expression of type II collagen, aggrecan, and Sox9 was detected after 14 days in TGF-ß3- and IGF-1-stimulated cells in both types of culture (monolayer and micromass). On Day 21 in the micromass culture, expression levels were greater than they were at 14 days for all genes. TGF-ß3 was found to be more efficient at promoting chondrogenesis than IGF-1. By western blot, we also found that after 3 weeks, the expression of type II collagen was greater in micromass culture with TGF-ß3.Conclusion.TGF-ß3 used in micromass culture is the best growth factor for promoting the proliferation and differentiation of mesenchymal cells from umbilical cord blood during chondrogenesis. This approach may provide an alternative to autologous grafting.


2000 ◽  
Vol 662 ◽  
Author(s):  
Lin-Shu Liu ◽  
Andrea Thompson ◽  
Robin Daverman ◽  
James W. Poser ◽  
Robert C. Spiro

AbstractWe have developed a novel bilayer matrix composed of a porous type I collagen layer that transitions into a hyaluronate gel layer. This study evaluates the potential of the bilayer matrix to support the in vitro and in vivo formation of both bone and cartilage tissue. In the presence of recombinant human growth and differentiation factor-5, fetal rat calvarial cells cultured in the HA layer grew in a round, aggregated, chondrocyte-like morphology, while those in the collagen layer grew flattened and spread. Biochemical analysis demonstrated that cells in the collagen layer expressed higher levels of alkaline phosphatase activity, and lower levels of sulfated glycosaminoglycans and type II collagen when compared to cells in the HA layer. Intramuscular implants of the bilayer matrix with growth factor retrieved at 28 days revealed the presence of bone and cartilage tissue in the collagen and hyaluronate layers, respectively. These results demonstrate that the differentiation of cells in response to a single growth factor can be guided by specific compositional changes of the extracellular matrix.


2021 ◽  
Vol 57 (4) ◽  
pp. 166-180
Author(s):  
Maria-Minodora Marin ◽  
Madalina Georgiana Albu Kaya ◽  
George Mihail Vlasceanu ◽  
Jana Ghitman ◽  
Ionut Cristian Radu ◽  
...  

Type II collagen has been perceived as the indispensable element and plays a crucial role in cartilage tissue engineering. Thus, materials based on type II collagen have drawn farther attention in both academic and research for developing new systems for the cartilage regeneration. The disadvantage of using type II collagen as a biomaterial for tissue repairing is its reduced biomechanical properties. This can be solved by physical, enzymatic or chemical cross-linking processes, which provide biomaterials with the required mechanical properties for medical applications. To enhance type II collagen properties, crosslinked collagen scaffolds with different cross-linking agents were prepared by freeze-drying technique. The present research work studied the synthesis of type II collagen biomaterials with and without crosslinking agents. Scaffolds morphology was observed by MicroCT, showing in all cases an appropriate microstructure for biological applications, and the mechanical studies were performed using compressive tests. DSC showed an increase in denaturation temperature with an increase in cross-linking agent concentration. FTIR suggested that the secondary structure of collagen is not affected after the cross-linking; supplementary, to confirm the characteristic triple-helix conformation of collagen, the CD investigation was performed. The results showed that the physical-chemical properties of type II collagen were improved by cross-linking treatments.


Sign in / Sign up

Export Citation Format

Share Document