scholarly journals Cotransfected human chondrocytes: over-expression of IGF-I and SOX9 enhances the synthesis of cartilage matrix components collagen-II and glycosaminoglycans

2015 ◽  
Vol 48 (12) ◽  
pp. 1063-1070 ◽  
Author(s):  
M. Simental-Mendía ◽  
J. Lara-Arias ◽  
E. Álvarez-Lozano ◽  
S. Said-Fernández ◽  
A. Soto-Domínguez ◽  
...  
Keyword(s):  
Cartilage Matrix ◽  
Human Chondrocytes ◽  
Over Expression ◽  
Igf I ◽  
Collagen Ii ◽  
Matrix Components

A critical role for collagen II in cartilage matrix degradation: Collagen II induces pro-inflammatory cytokines and MMPs in primary human chondrocytes

2009 ◽  
Vol 27 (1) ◽  
pp. 65-70 ◽  
Author(s):  
Andreas R. Klatt ◽  
Brigitte Paul-Klausch ◽  
Gabriele Klinger ◽  
Getrud Kühn ◽  
Joerg H. Renno ◽  
...  
Keyword(s):  
Inflammatory Cytokines ◽  
Critical Role ◽  
Cartilage Matrix ◽  
Human Chondrocytes ◽  
Matrix Degradation ◽  
Collagen Ii ◽  
Pro Inflammatory Cytokines

scholarly journals Influence of Conditioned Media on the Re-Differentiation Capacity of Human Chondrocytes in 3D Spheroid Cultures

2020 ◽  
Vol 9 (9) ◽  
pp. 2798
Author(s):  
Annett Klinder ◽  
Sophie Kussauer ◽  
Bettina Hiemer ◽  
Andreas Wree ◽  
Rainer Bader ◽  
...  
Keyword(s):  
Conditioned Medium ◽  
Culture Media ◽  
Ex Vivo ◽  
Cartilage Matrix ◽  
Human Chondrocytes ◽  
Growth Media ◽  
Cell Cultivation ◽  
Cell Based Therapy ◽  
Tgf Β1

A major challenge of cell-based therapy for cartilage lesions is the preservation of the chondrogenic phenotype during ex vivo cell cultivation. In this in vitro study, the chondro-inductive capacity of two different hyaline cartilage-conditioned cell culture media on human chondrocytes in 3D spheroids was determined. Media were conditioned by incubation of 200 mg/mL vital or devitalized cartilage matrix in growth media over 35 days. The media were analyzed for the content of soluble procollagen type (Col) II and glycosaminoglycans (GAGs) as well as released TGF-β1, IGF-1 and IGFBP3. Unconditioned medium served as a negative control while the positive medium control was supplemented with TGF-β1 and IGF-1. Spheroid cultures prepared from human chondrocytes were cultivated at 37 °C, 5% CO2 and 21% O2 in the respective media and controls. After 14 and 35 days, the deposition of ECM components was evaluated by histological analysis. Vital cartilage-conditioned medium contained significantly higher levels of Col II and active TGF-β1 compared to medium conditioned with the devitalized cartilage matrix. Despite these differences, the incubation with vital as well as devitalized cartilage conditioned medium led to similar results in terms of deposition of proteoglycans and collagen type II, which was used as an indicator of re-differentiation of human chondrocytes in spheroid cultures. However, high density 3D cell cultivation showed a positive influence on re-differentiation.

Human chondrocytes proliferate and produce matrix components in microcarrier suspension culture

Biomaterials ◽  
1996 ◽  
Vol 17 (9) ◽  
pp. 879-888 ◽  
Author(s):  
C. Frondoza ◽  
A. Sohrabi ◽  
D. Hungerford
Keyword(s):  
Suspension Culture ◽  
Human Chondrocytes ◽  
Matrix Components

scholarly journals INFLUENCE OF EXTERNAL POTASSIUM ON THE SYNTHESIS AND DEPOSITION OF MATRIX COMPONENTS BY CHONDROCYTES IN VITRO

1974 ◽  
Vol 63 (3) ◽  
pp. 843-854 ◽  
Author(s):  
Jon C. Daniel ◽  
Robert A. Kosher ◽  
James E. Hamos ◽  
James W. Lash
Keyword(s):  
Culture Medium ◽  
Hyaline Cartilage ◽  
Cell Layer ◽  
Potassium Concentration ◽  
Cartilage Matrix ◽  
High Potassium ◽  
External Potassium ◽  
Matrix Components ◽  
High Potassium Concentration

The effect of a high external potassium concentration on the synthesis and deposition of matrix components by chondrocytes in cell culture was determined. There is a twofold increase in the amount of chondroitin 4- and 6-sulfate accumulated by chondrocytes grown in medium containing a high potassium concentration. There is also a comparable increase in the production of other sulfated glycosaminoglycans (GAG) including heparan sulfate and uncharacterized glycoprotein components. The twofold greater accumulation of GAG in the high potassium medium is primarily the result of a decrease in their rate of degradation. In spite of this increased accumulation of GAG, the cells in high potassium fail to elaborate appreciable quantities of visible matrix, although they do retain the typical chondrocytic polygonal morphology. Although most of the products are secreted into the culture medium in the high potassium environment, the cell layer retains the same amount of glycosaminoglycan as the control cultures. The inability of chondrocytes grown in high potassium to elaborate the typical hyaline cartilage matrix is not a consequence of an impairment in collagen synthesis, since there is no difference in the total amount of collagen synthesized by high potassium or control cultures. There is, however, a slight increase in the proportion of collagen that is secreted into the medium by chondrocytes in high potassium. Synthesis of the predominant cartilage matrix molecules is not sufficient in itself to ensure that these molecules will be assembled into a hyaline matrix.

scholarly journals SOMITE CHONDROGENESIS

1973 ◽  
Vol 56 (1) ◽  
pp. 27-50 ◽  
Author(s):  
Ronald R. Minor
Keyword(s):  
Spinal Cord ◽  
Cell Death ◽  
Nutrient Medium ◽  
Horse Serum ◽  
Light And Electron Microscopy ◽  
Fibrous Tissue ◽  
Calf Serum ◽  
Cartilage Matrix ◽  
Structured Matrix ◽  
Matrix Components

Light and electron microscopy are used in this study to compare chondrogenesis in cultured somites with vertebral chondrogenesis These studies have also characterized some of the effects of inducer tissues (notochord and spinal cord), and different nutrient media, on chondrogenesis in cultured somites Somites from stage 17 (54–60 h) chick embryos were cultured, with or without inducer tissues, and were fed nutrient medium containing either horse serum (HS) and embryo extract (EE), or fetal calf serum (FCS) and F12X Amino acid analyses were also utilized to determine the collagen content of vertebral body cartilage in which the fibrils are homogeneously thin (ca. 150 Å) and unbanded. These analyses provide strong evidence that the thin unbanded fibrils in embryonic cartilage matrix are collagen. These thin unbanded collagen fibrils, and prominent 200–800 Å protein polysaccharide granules, constitute the structured matrix components of both developing vertebral cartilage and the cartilage formed in cultured somites Similar matrix components accumulate around the inducer tissues notochord and spinal cord. These matrix components are structurally distinct from those in embryonic fibrous tissue The synthesis of matrix by the inducer tissues is associated with the inductive interaction of these tissues with somitic mesenchyme. Due to the deleterious effects of tissue isolation and culture procedures many cells die in somitic mesenchyme during the first 24 h in culture. In spite of this cell death, chondrogenic areas are recognized after 12 h in induced cultures, and through the first 2 days in all cultures there are larger accumulations of structured matrix than are present in equivalently aged somitic mesenchyme in vivo. Surviving chondrogenic areas develop into nodules of hyaline cartilage in all induced cultures, and in most non-induced cultures fed medium containing FCS and F12X There is more cell death, less matrix accumulation, and less cartilage formed in cultures fed medium containing HS and EE. The inducer tissues, as well as nutrient medium containing FCS and F12X, facilitate cell survival, the synthesis and accumulation of cartilage matrix, and the formation of cartilage nodules in cultured somites.

ALK1 Opposes ALK5/Smad3 Signaling and Expression of Extracellular Matrix Components in Human Chondrocytes

2008 ◽  
Vol 23 (6) ◽  
pp. 896-906 ◽  
Author(s):  
Kenneth W Finnson ◽  
Wendy L Parker ◽  
Peter ten Dijke ◽  
Midory Thorikay ◽  
Anie Philip
Keyword(s):  
Extracellular Matrix ◽  
Human Chondrocytes ◽  
Extracellular Matrix Components ◽  
Matrix Components

Eel insulin: isolation, characterization and stimulatory actions on [35S]sulphate and [3H]thymidine uptake in the branchial cartilage of the eel in vitro

1992 ◽  
Vol 133 (2) ◽  
pp. 221-230 ◽  
Author(s):  
C. Duan ◽  
T. Noso ◽  
S. Moriyama ◽  
H. Kawauchi ◽  
T. Hirano
Keyword(s):  
Bovine Insulin ◽  
Cartilage Matrix ◽  
Common Mechanism ◽  
Thymidine Uptake ◽  
Dependent Manner ◽  
Matrix Synthesis ◽  
Sulphate Uptake ◽  
Igf I ◽  
Dose Dependent

ABSTRACT Our previous studies have shown that mammalian and salmon insulins stimulate sulphate uptake by cultured eel cartilage, suggesting the possible involvement of insulin in the regulation of cartilage matrix synthesis. In the present study, homologous eel insulin was isolated and characterized, and its effects on cartilage matrix synthesis and DNA synthesis were examined in vitro. Insulin was extracted from eel pancreas with acid–ethanol, and subsequently purified by isoelectric precipitation at pH 5·3, gel filtration on Sephadex G-50, and reversed-phase high-performance liquid chromatography. The amino acid composition and complete sequence (50 residues) of eel insulin revealed high homology to teleostean and mammalian insulins. The isolated eel insulin produced a more pronounced and longer lasting hypoglycaemic effect than bovine insulin in the eel. Homologous eel insulin, like bovine insulin-like growth factor (IGF-I) and insulin, stimulated sulphate uptake by cultured eel cartilage in a dose-dependent manner (16–1000 ng/ml). Combination experiments using maximal concentrations of bovine IGF-I (250 ng/ml) and increasing amounts of eel insulin (10–250 ng/ml) showed no additive effects of insulin on sulphate uptake, suggesting that insulin and IGF-I may share a common mechanism(s) of action. Eel insulin and bovine IGF-I also enhanced thymidine incorporation by eel cartilage in a dose-dependent manner (4–1000 ng/ml); eel insulin was equipotent with bovine IGF-I. These results suggest that insulin, like IGF-I, may exert direct growth-promoting actions in branchial cartilage of the eel. Journal of Endocrinology (1992) 133, 221–230

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