scholarly journals Nitric oxide inhibits the synthesis of type-II collagen without altering Col2A1 mRNA abundance: prolyl hydroxylase as a possible target

1997 ◽  
Vol 324 (1) ◽  
pp. 305-310 ◽  
Author(s):  
M. CAO ◽  
A. WESTERHAUSEN-LARSON ◽  
C. NIYIBIZI ◽  
K. KAVALKOVICH ◽  
H. I. GEORGESCU ◽  
...  
Keyword(s):  
Collagen Synthesis ◽  
Articular Chondrocytes ◽  
Type Ii Collagen ◽  
Suppressive Effect ◽  
Prolyl Hydroxylase ◽  
Type Ii ◽  
Independent Manner ◽  
No Donor ◽  
Triple Helices ◽  
Important Enzyme

The addition of human recombinant interleukin-1β (IL-1β) to cultures of lapine articular chondrocytes provoked the synthesis of large amounts of NO and reduced the production of type-II collagen. NG-Monomethyl-l-arginine (L-NMA), an inhibitor of NO synthase, strongly suppressed the production of NO and partially relieved the inhibition of collagen synthesis in response to IL-1β. The NO donor S-nitrosoacetylpenicillamine (SNAP), on the other hand, inhibited collagen production. IL-1 lowered the abundance of Col2A1 mRNA in an NO-independent manner. Collectively, these data indicate that IL-1 suppresses collagen synthesis at two levels: a pretranslational level which is NO-independent, and a translational or post-translational level which is NO-mediated. These effects are presumably specific as L-NMA and SNAP had no effect on total protein synthesis or on the distribution of newly synthesized proteins between the cellular and extracellular compartments. Prolyl hydroxylase is an important enzyme in the post-translational processing of collagen, and its regulation and cofactor requirements suggest possible sensitivity to NO. Extracts of cells treated with IL-1 or SNAP had lower prolyl hydroxylase activity, and L-NMA was partially able to reverse the effects of IL-1. These data suggest that prolyl hydroxylase might indeed be a target for NO. Because underhydroxylated collagen monomers fail to anneal into stable triple helices, they are degraded intracellularly. Inhibition of prolyl hydroxylase by NO might thus account for the suppressive effect of this radical on collagen synthesis.

Doxycycline Inhibits Collagen Synthesis by Differentiated Articular Chondrocytes

1998 ◽  
Vol 12 (1) ◽  
pp. 63-67 ◽  
Author(s):  
J.M. Tekoppele ◽  
B. Beekman ◽  
N. Verzijl ◽  
J.L. Koopman ◽  
J. Degroot ◽  
...  
Keyword(s):  
Collagen Synthesis ◽  
Articular Chondrocytes ◽  
Cruciate Ligament ◽  
Type Ii Collagen ◽  
Transcriptional Level ◽  
Mrna Levels ◽  
Type Ii ◽  
Chondrocyte Phenotype ◽  
Experimental Osteoarthritis

Doxycycline (DOX) profoundly inhibited collagen synthesis by differentiated articular chondrocytes. At 25 μM, the rate of collagen synthesis was suppressed by more than 50% without affecting cell proliferation (DNA levels) and general protein synthesis (35S-Met and 35S-Cys incorporation). Steady-state mRNA levels of type II collagen were also reduced, indicating that DOX may have an effect at the transcriptional level of type II collagen. The IC50 value of DOX to downregulate collagen synthesis (17 μM) is close to DOX levels attained in vivo (< 10 μM), and it is more than ten-fold lower than the IC50 values to inhibit the activity of most matrix metalloproteinases (MMPs). As such, these findings support the hypothesis that the reduced severity of OA observed in the dog anterior cruciate ligament model resulting from prophylactic treatment with DOX may involve mechanisms other than MMP inhibition alone. Our findings suggest that prevention of changes in the chondrocyte phenotype may be involved in the beneficial effect of doxycycline in experimental osteoarthritis. for differentiated chondrocytes in early stages of osteoarthritis exhibit elevated collagen synthesis.

A Comparison of 3 Bioinks for 3D Bioprinting of Articular Cartilage

2021 ◽  
Author(s):  
Christel Henrionnet ◽  
Océane Messaoudi ◽  
Léa Pourchet ◽  
Pierre Gillet ◽  
Damien Loeuille ◽  
...  
Keyword(s):  
Collagen Synthesis ◽  
Type Ii Collagen ◽  
Type Ii ◽  
3D Bioprinting ◽  
Matrix Synthesis ◽  
Cartilage Engineering ◽  
Low Viscosity ◽  
Promising Tool ◽  
Marrow Mesenchymal Stem Cells ◽  
Hematoxylin Eosin

Background: 3D printing has become a promising tool for cartilage engineering, combining 3D deposition of cells seeded in supporting biomaterials. Objective: Our goal was to evaluate the chondrogenic properties of three different bioinks, seeded with human bone marrow mesenchymal stem cells (bMSCs). Methods: The three different tested bioinks are seeded with 2 × 106 cells/mL bMSCs. The bioink#1 is composed of gelatin, fibrinogen, and very low viscosity alginate. The bioink#2 has the same composition, excepted for the alginate that is a low viscosity one. The bioink#3 is manufactured by CELLINK®. The cartilaginous substitutes were cultivated for 28 days in the presence of ITS vs TGF-ß1. The extracellular matrix synthesis is evaluated at D28 by histology (Hematoxylin-Eosin-Saffron & Alcian Blue) and immunostaining (type II collagen). Results: The bioink#1 better promoted type II collagen synthesis, although the three bioink were equipotent in terms of proteoglycan content. Despite its universal characteristics, the bioink#3 failed to encourage the hyaline-like matrix synthesis. Conclusion: The bioink#1 containing gelatin, fibrinogen, and very low viscosity seems to be the fittest of the three bio-inks to obtain a cartilaginous substitute presenting a remarkable matrix synthesis. This study confirms the importance of the choice of bioink for cartilage engineering.

scholarly journals Regulation of type II collagen expression by cyclin-dependent kinase 6, cyclin D1, and p21 in articular chondrocytes

IUBMB Life ◽  
2007 ◽  
Vol 59 (2) ◽  
pp. 90-98 ◽  
Author(s):  
Sang-Gu Hwang ◽  
Sung-Min Song ◽  
Jeong-Ran Kim ◽  
Chun-Shik Park ◽  
Woo-Keun Song ◽  
...  
Keyword(s):  
Cyclin D1 ◽  
Articular Chondrocytes ◽  
Type Ii Collagen ◽  
Type Ii ◽  
Cyclin Dependent Kinase ◽  
Collagen Expression

SOX9 expression does not correlate with type II collagen expression in adult articular chondrocytes

2003 ◽  
Vol 22 (4) ◽  
pp. 363-372 ◽  
Author(s):  
Thomas Aigner ◽  
Pia Margarethe Gebhard ◽  
Erik Schmid ◽  
Brigitte Bau ◽  
Vincent Harley ◽  
...  
Keyword(s):  
Articular Chondrocytes ◽  
Type Ii Collagen ◽  
Type Ii ◽  
Sox9 Expression ◽  
Collagen Expression

Influence of 17β-estradiol and insulin on type II collagen and protein synthesis of articular chondrocytes

Bone ◽  
2006 ◽  
Vol 39 (2) ◽  
pp. 310-317 ◽  
Author(s):  
Horst Claassen ◽  
Matthias Schlüter ◽  
Michael Schünke ◽  
Bodo Kurz
Keyword(s):  
Protein Synthesis ◽  
Articular Chondrocytes ◽  
Type Ii Collagen ◽  
Type Ii ◽  
17Β Estradiol
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