Variable Effects of 3 Different Chondroitin Sulfate Compounds on Human Osteoarthritic Cartilage/Chondrocytes: Relevance of Purity and Production Process

2010 ◽  
Vol 37 (3) ◽  
pp. 656-664 ◽  
Author(s):  
STEEVE KWAN TAT ◽  
JEAN-PIERRE PELLETIER ◽  
FRANÇOIS MINEAU ◽  
NICOLAS DUVAL ◽  
JOHANNE MARTEL-PELLETIER
Keyword(s):  
Gene Expression ◽  
Chondroitin Sulfate ◽  
Collagen Type ◽  
Cartilage Explants ◽  
Gene Expression Level ◽  
Expression Level ◽  
Prostaglandin E ◽  
Type Ii ◽  
Collagen Type Ii ◽  
Catabolic Pathways

Objective.During osteoarthritis (OA), the altered metabolism of cartilage involves proinflammatory factors and matrix metalloprotease (MMP) activity. Studies showed that chondroitin sulfate (CS) may exert a positive effect on the cartilage. Because of differences in CS in terms of purity and the production/purification process, we compared the effects of 3 different types of CS on human OA cartilage.Methods.Three types of CS were tested: CS1 (porcine, purity 90.4%), CS2 (bovine, purity 96.2%), and CS3 (bovine, purity 99.9%). Treatment with CS at 200 and 1000 μg/ml was performed on human OA cartilage explants in the presence/absence of interleukin 1ß (IL-1ß), and the protein modulations of factors including prostaglandin E2 (PGE2), IL-6, and MMP-1 measured by ELISA. The CS effect on the expression of collagen type II was also investigated on OA chondrocytes using quantitative polymerase chain reaction.Results.In the presence of IL-1ß, CS2 at 1000 μg/ml significantly inhibited IL-6 and PGE2 production, and CS3 at 200 μg/ml markedly reduced the level of IL-6. CS1 was much less efficient at reducing the catabolic markers and in the absence of IL-1ß, it significantly increased IL-6 and MMP-1. IL-1ß significantly inhibited the gene expression level of collagen type II; only CS3 was able to limit this inhibition. CS1, in the presence or absence of IL-1ß, further markedly decreased collagen type II expression.Conclusion.Our data indicate that among the 3 tested CS, CS1 increased production of some catabolic pathways and inhibited the gene expression level of collagen type II. Our study provides new information in the context of prescribing CS for alleviating OA symptoms, as the purity and/or production/purification of the CS compound could orient the current OA disease process toward increased catabolic pathways.

POTENCY OF ORAL UN-DENATURED TYPE II COLLAGENIN THE TREATMENT OF OSTEOARTHRITIS, WITH SPECIFICAL RELATIONSHIP TO KNEE JOINT- A META-ANALYTIC REVIEW

2021 ◽  
pp. 6-10
Author(s):  
R K Guhan ◽  
Saran Karthik.S ◽  
Ashwin V Y ◽  
Venkatachalam. K ◽  
Yokesh M ◽  
...  
Keyword(s):  
Knee Joint ◽  
Chondroitin Sulfate ◽  
Collagen Type ◽  
Joint Disease ◽  
Primary Data ◽  
Type Ii ◽  
Collagen Type Ii ◽  
Number Of Patients ◽  
Analytic Review ◽  
Native Collagen

Introduction: One of the chronic progressive diseases of the elderly is Osteoarthritis. There is a wide spectrum of Nutraceuticals, for Osteoarthritis, but there does not exist, a convincing literature based evidence, in support of their denitive and specic rationale of utility. We here in, aim to evaluate the evidence in literature hither to available, for establishing the potency and efcaciousness of the indigenous type II collagen variant. Methods: st st A schematic search was performed of Pub Med, Scopus and the Google Scholar, from dates (1 December 2009 to 1 December 2020), with the search terms: 'Osteoarthritis', 'Nutraceuticals', 'Oral Collagen', 'Glucosamine', 'Chondroitin Sulfate', 'Acetaminophen' and 'Native Collagen'. Articles containing the following were included in the study: Randomized Control Trial and Clinical Trial, Primary data, OA and Oral Collagen studies related to joint disease. Total number of patients studied, the number of patients who were treated by Native Collagen Type II variant, Denatured Collagen Type II variant, Glucosamine, Chondroitin Sulfate and Acetaminophen.A number of studies using various scoring systems were incorporated in our study. Finally, all the functional outcomes, according to the VAS and WOMAC scores, were cumulatively tabulated, and analyzed schematically and their results deduced. Results: Multiple researches have been executed, to elucidate upon the efcacy and the safety, of Oral Collagen of the type II variant, in the medicaments prescribed for OA, especially relating to the Knee joint. Oral Collagen is administered, either in a Denatured or an Undenatured form .The results indicate , that out of all the Nutraceuticals, Undenatured/Native collagen of the type II variant, proved to be by far the most safe and signicantly more efcacious, compared to other Nutraceuticals. Although all the suggested treatments reduced the WOMAC and the VAS scores, here in UC II, showed more efciency and sustenance of the pain reduction, in both the assessment scores, in comparison with other orally administrated Nutraceuticals. Conclusion: Our Meta-Analysis concludes that, Type II Undenatured Collagen, is a relatively safe and also signicantly more efcient, in improving the joint function, ROM and for the alleviation of bone joint pain, in OA knee (Genu OA) patients.

scholarly journals Increased TGF-β and BMP Levels and Improved Chondrocyte-Specific Marker Expression In Vitro under Cartilage-Specific Physiological Osmolarity

2019 ◽  
Vol 20 (4) ◽  
pp. 795 ◽  
Author(s):  
Ufuk Tan Timur ◽  
Marjolein Caron ◽  
Guus van den Akker ◽  
Anna van der Windt ◽  
Jenny Visser ◽  
...  
Keyword(s):  
Gene Expression ◽  
Mrna Expression ◽  
Protein Secretion ◽  
Collagen Type ◽  
Articular Chondrocytes ◽  
Human Articular Chondrocytes ◽  
Type Ii ◽  
Collagen Type Ii ◽  
Reporter Assay

During standard expansion culture (i.e., plasma osmolarity, 280 mOsm) human articular chondrocytes dedifferentiate, making them inappropriate for autologous chondrocyte implantation to treat cartilage defects. Increasing the osmolarity of culture media to physiological osmolarity levels of cartilage (i.e., 380 mOsm), increases collagen type II (COL2A1) expression of human articular chondrocytes in vitro, but the underlying molecular mechanism is not fully understood. We hypothesized that TGF-β superfamily signaling may drive expression of COL2A1 under physiological osmolarity culture conditions. Human articular chondrocytes were cultured in cytokine-free medium of 280 or 380 mOsm with or without siRNA mediated TGF-β2 knockdown (RNAi). Expression of TGF-β isoforms, and collagen type II was evaluated by RT-qPCR and immunoblotting. TGF-β2 protein secretion was evaluated using ELISA and TGF-β bioactivity was determined using an established reporter assay. Involvement of BMP signaling was investigated by culturing human articular chondrocytes in the presence or absence of BMP inhibitor dorsomorphin and BMP bioactivity was determined using an established reporter assay. Physiological cartilage osmolarity (i.e., physosmolarity) most prominently increased TGF-β2 mRNA expression and protein secretion as well as TGF-β bioactivity. Upon TGF-β2 isoform-specific knockdown, gene expression of chondrocyte marker COL2A1 was induced. TGF-β2 RNAi under physosmolarity enhanced TGF-β bioactivity. BMP bioactivity increased upon physosmotic treatment, but was not related to TGF-β2 RNAi. In contrast, dorsomorphin inhibited COL2A1 mRNA expression in human articular chondrocytes independent of the osmotic condition. Our data suggest a role for TGF-β superfamily member signaling in physosmolarity-induced mRNA expression of collagen type II. As physosmotic conditions favor the expression of COL2A1 independent of our manipulations, contribution of other metabolic, post-transcriptional or epigenetic factors cannot be excluded in the underlying complex and interdependent regulation of marker gene expression. Dissecting these molecular mechanisms holds potential to further improve future cell-based chondral repair strategies.

scholarly journals Gene Expression of GSK3 in Type II Diabetics Compared to Non-Diabetics (ex vivo)

2020 ◽  
Vol 10 (1) ◽  
pp. 30-37
Author(s):  
Somayeh A.H. Khorami ◽  
Mohd S. Abd Mutalib ◽  
Mohammad F. Shiraz ◽  
Joseph A. Abdullah ◽  
Zulida Rejali ◽  
...  
Keyword(s):  
Gene Expression ◽  
Insulin Resistance ◽  
Glycogen Synthase ◽  
Ex Vivo ◽  
Glycogen Synthesis ◽  
Gene Expression Level ◽  
Expression Level ◽  
Type Ii ◽  
Cross Sectional ◽  
Significant Difference

Background: GSK3 is a serine/threonine kinase that is involved in the storage of glucose into glycogen through the negative regulation of glycogen synthase. Defects in GSK3 and glycogen synthase function are early stages of the development of insulin resistance, which may cause impaired glycogen synthesis in Type II diabetes. Methods: In this cross-sectional study, the gene expression level of GSK3 from Type II diabetic and non-diabetic participants was compared via real-time RT-PCR. To investigate the relationships between GSK3 expression and indicators of insulin resistance, Pearson's correlation analysis was performed. To compare the differences between GSK3 expression levels based on BMI categories, one-way ANOVA was used. Results: Gene expression of GSK3 was slightly higher in diabetic participants compared to non-diabetics, but it was statistically insignificant. Also, no significant difference was found based on BMI categories in the two groups. No significant association between GSK3 expression and indicators of insulin resistance was observed in non-diabetic participants. There was only a positive significant correlation between GSK3 expression and FBS in diabetic participants. Conclusion: These results indicate that the regulation of GSK3 may occur at the translation level, as gene expression level was unaltered between diabetic and non-diabetic participants. Also, since circulating levels of both glucose and insulin regulate GSK3 activity, tissue specificity for the expression and post-translation regulations of GSK3 may exist, which cause hyperactivation or overexpression in some target tissues in diabetes. Furthermore, it is probable that glycogen synthase activity is also regulated by non-insulin mediated mechanisms like exercise or allosteric changes, independent of GSK3 expression.

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