scholarly journals Collagen Synthesis in Tenocytes, Ligament Cells and Chondrocytes Exposed to a Combination of Glucosamine HCl and Chondroitin Sulfate

2007 ◽  
Vol 4 (2) ◽  
pp. 219-224 ◽  
Author(s):  
Louis Lippiello
Keyword(s):  
Chondroitin Sulfate ◽  
Collagen Synthesis ◽  
Tissue Response ◽  
Synthetic Activity ◽  
Specific Marker ◽  
Sensitive Material ◽  
Joint Tissue ◽  
Tissue Trauma

Clinical testing of the nutraceuticals glucosamine (glcN) and chondroitin sulfate (CS) has shown efficacy in providing relief from symptoms in osteoarthritic patients.In vitroandin vivostudies support existence of a synergistic relationship upregulating synthetic activity in chondrocytes. A combination of glcN and CS may also be useful as adjunct therapy in sports-related injuries if similar upregulation of collagen synthesis is elicited in accessory ligament and tendon joint tissue. Collagen and non-collagenous protein (NCP) synthesis in cultures of bovine tenocytes, ligament cells and chondrocytes exposed to glcN + CS were assayed by uptake of radiolabeled proline into collagenase-sensitive material. Assay of radiolabel in hydroxyproline (a specific marker for collagen synthesis) following HPLC isolation confirmed the specificity of the metabolic effect. Synthesis of total collagenase-sensitive material was maximally upregulated at physiologically obtainable doses of glcN + CS. Tissue response followed the sequence ligament cells (+69%) > chondrocytes (+56%) > tenocytes (+22%). Labeled hydroxyproline increased by 132% in ligament cells, 27% in tenocytes and 49% in epitendon cells after a 48 h exposure to 5 μg ml−1glcN + 4 μg ml−1CS. Low dose combinations of glcN and CS effectively stimulatein vitrocollagen and NCP synthesis by ligament cells, tenocytes and chondrocytes. Hence, therapeutic use following accessory joint tissue trauma may help augment repair processes.

scholarly journals [3H]proline incorporation and hydroxyproline concentration in articular cartilage during the development of osteoarthritis caused by immobilization. A study in vivo with rabbits

1981 ◽  
Vol 200 (2) ◽  
pp. 435-440 ◽  
Author(s):  
T Videman ◽  
I Eronen ◽  
T Candolin
Keyword(s):  
Total Protein ◽  
Collagen Synthesis ◽  
Weight Bearing ◽  
Specific Radioactivity ◽  
Collagen Content ◽  
Synthetic Activity ◽  
Synthesis Rate ◽  
Hydroxyproline Concentration ◽  
Proline Incorporation

Proline metabolism in vivo was studied during the development of immobilization osteoarthritis in rabbits. Collagen content was measured as the hydroxyproline concentration of the tissue in question. The incorporation of [3H]proline was used as the indicator for total protein synthesis; collagen synthesis rate was estimated from measurements of the specific radioactivity of hydroxyproline. Cartilage samples from knee and hip joints were analysed after 3, 7, 11, 18, 35 and 56 days of immobilization. The total protein and collagen synthesis rates of the immobilized legs increased and reached a maximum after 11-35 days. Although they decreased thereafter, these rates remained elevated to the end of the experiment. A slight increase in the synthetic activity of the non-immobilized contralateral legs was also detected after 7--18 days of immobilization. The isotope incorporation was markedly higher in tibial marginal tissue than in weight-bearing cartilage. In spite of the increased synthesis, no clear changes were found in the collagen content of the tissues studied during the experiment.

scholarly journals Cartilage Extracellular Matrix Scaffold With Kartogenin-Encapsulated PLGA Microspheres for Cartilage Regeneration

2020 ◽  
Vol 8 ◽  
Author(s):  
Yanhong Zhao ◽  
Xige Zhao ◽  
Rui Zhang ◽  
Ying Huang ◽  
Yunjie Li ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Composite Scaffold ◽  
Rabbit Model ◽  
Cartilage Tissue ◽  
Cartilage Defects ◽  
Specific Marker ◽  
Molecular Compound ◽  
Plga Microspheres

Repair of articular cartilage defects is a challenging aspect of clinical treatment. Kartogenin (KGN), a small molecular compound, can induce the differentiation of bone marrow-derived mesenchymal stem cells (BMSCs) into chondrocytes. Here, we constructed a scaffold based on chondrocyte extracellular matrix (CECM) and poly(lactic-co-glycolic acid) (PLGA) microspheres (MP), which can slowly release KGN, thus enhancing its efficiency. Cell adhesion, live/dead staining, and CCK-8 results indicated that the PLGA(KGN)/CECM scaffold exhibited good biocompatibility. Histological staining and quantitative analysis demonstrated the ability of the PLGA(KGN)/CECM composite scaffold to promote the differentiation of BMSCs. Macroscopic observations, histological tests, and specific marker analysis showed that the regenerated tissues possessed characteristics similar to those of normal hyaline cartilage in a rabbit model. Use of the PLGA(KGN)/CECM scaffold may mimic the regenerative microenvironment, thereby promoting chondrogenic differentiation of BMSCs in vitro and in vivo. Therefore, this innovative composite scaffold may represent a promising approach for acellular cartilage tissue engineering.

scholarly journals Myocyte-Derived Hsp90 Modulates Collagen Upregulation via Biphasic Activation of STAT-3 in Fibroblasts during Cardiac Hypertrophy

2016 ◽  
Vol 37 (6) ◽  
Author(s):  
Ritwik Datta ◽  
Trisha Bansal ◽  
Santanu Rana ◽  
Kaberi Datta ◽  
Ratul Datta Chaudhuri ◽  
...  
Keyword(s):  
Cardiac Hypertrophy ◽  
Collagen Synthesis ◽  
Cardiac Fibroblasts ◽  
Heat Shock Protein 90 ◽  
Signaling Mechanism ◽  
Content Type ◽  
Collagen Expression ◽  
Significant Difference

ABSTRACT Signal transducer and activator of transcription 3 (STAT-3)-mediated signaling in relation to upregulated collagen expression in fibroblasts during cardiac hypertrophy is well defined. Our recent findings have identified heat shock protein 90 (Hsp90) to be a critical modulator of fibrotic signaling in cardiac fibroblasts in this disease milieu. The present study was therefore intended to analyze the role of Hsp90 in the STAT-3-mediated collagen upregulation process. Our data revealed a significant difference between in vivo and in vitro results, pointing to a possible involvement of myocyte-fibroblast cross talk in this process. Cardiomyocyte-targeted knockdown of Hsp90 in rats (Rattus norvegicus) in which the renal artery was ligated showed downregulated collagen synthesis. Furthermore, the results obtained with cardiac fibroblasts conditioned with Hsp90-inhibited hypertrophied myocyte supernatant pointed toward cardiomyocytes' role in the regulation of collagen expression in fibroblasts during hypertrophy. Our study also revealed a novel signaling mechanism where myocyte-derived Hsp90 orchestrates not only p65-mediated interleukin-6 (IL-6) synthesis but also its release in exosomal vesicles. Such myocyte-derived exosomes and myocyte-secreted IL-6 are responsible in unison for the biphasic activation of STAT-3 signaling in cardiac fibroblasts that culminates in excess collagen synthesis, leading to severely compromised cardiac function during cardiac hypertrophy.

scholarly journals Some biochemical effects of triamcinolone acetonide on rat liver and muscle

1970 ◽  
Vol 116 (3) ◽  
pp. 349-355 ◽  
Author(s):  
R. F. Peters ◽  
M. C. Richardson ◽  
Margaret Small ◽  
A. M. White
Keyword(s):  
Amino Acids ◽  
Triamcinolone Acetonide ◽  
Time Course ◽  
Muscle Protein ◽  
Specific Radioactivity ◽  
Synthetic Activity ◽  
Tissue Homogenate ◽  
Glycogen Concentration

1. The powerful anti-inflammatory glucocorticoid triamcinolone acetonide, administered to rats at 20 and 2.5mg/kg, leads to a decrease in the incorporation in vivo of [3H]uridine and [32P]orthophosphate into hind-limb skeletal muscle. 2. At the higher dose, this decrease in the rate of incorporation of precursors into RNA precedes a decrease in the incorporating ability of muscle ribosomes, which commences about 4–5h after drug administration, but is unaccompanied by any changes in the concentration of tissue ATP or free amino acids. 3. The ribosomal dysfunction extends to polyribosomes, which can only be successfully isolated from the muscle of triamcinolone-treated animals after the addition of α-amylase to the tissue homogenate to remove glycogen. 4. The specific radioactivity of muscle protein labelled in vivo with 14C-labelled amino acids does not decrease progressively after triamcinolone administration. After 2h there is an apparent stimulation of incorporation which leads to an overall discrepancy between measurements of protein-synthetic activity made in vivo and in vitro. 5. There is a significant increase in muscle-glycogen concentration between 8 and 12h after the administration of triamcinolone acetonide (20mg/kg), although a significant decrease occurs after 4h. The fall in glycogen concentration may be due to a decrease in the rate of synthesis of protein essential for glucose uptake into the tissues. 6. As judged by (a) incorporation of 14C-labelled amino acids into protein, (b) [3H]uridine and [32P]-orthophosphate incorporation into RNA, (c) the rate of induction of tryptophan pyrrolase and (d) changes in the pool sizes of taurine and tryptophan, the responses in liver followed the same time-course as those in muscle after administration of the drug.

scholarly journals Emergence of three myelin proteins in oligodendrocytes cultured without neurons.

1986 ◽  
Vol 102 (2) ◽  
pp. 384-392 ◽  
Author(s):  
M Dubois-Dalcq ◽  
T Behar ◽  
L Hudson ◽  
R A Lazzarini
Keyword(s):  
Optic Nerve ◽  
Proteolipid Protein ◽  
Defined Medium ◽  
Myelin Proteins ◽  
Specific Marker ◽  
The Central Nervous System ◽  
Double Label ◽  
Myelin Associated Glycoprotein

Oligodendrocytes, the myelin-forming cells of the central nervous system, were cultured from newborn rat brain and optic nerve to allow us to analyze whether two transmembranous myelin proteins, myelin-associated glycoprotein (MAG) and proteolipid protein (PLP), were expressed together with myelin basic protein (MBP) in defined medium with low serum and in the absence of neurons. Using double label immunofluorescence, we investigated when and where these three myelin proteins appeared in cells expressing galactocerebroside (GC), a specific marker for the oligodendrocyte membrane. We found that a proportion of oligodendrocytes derived from brain and optic nerve invariably express MBP, MAG, and PLP about a week after the emergence of GC, which occurs around birth. In brain-derived oligodendrocytes, MBP and MAG first emerge between the fifth and the seventh day after birth, followed by PLP 1 to 2 d later. All three proteins were confined to the cell body at that time, although an extensive network of GC positive processes had already developed. Each protein shows a specific cytoplasmic localization: diffuse for MBP, mostly perinuclear for MAG, and particulate for PLP. Interestingly, MAG, which may be involved in glial-axon interactions, is the first myelin protein detected in the processes at approximately 10 d after birth. MBP and PLP are only seen in these locations after 15 d. All GC-positive cells express the three myelin proteins by day 19. Simultaneously, numerous membrane and myelin whorls accumulate along the oligodendrocyte surface. The sequential emergence, cytoplasmic location, and peak of expression of these three myelin proteins in vitro follow a pattern similar to that described in vivo and, therefore, are independent of continuous neuronal influences. Such cultures provide a convenient system to study factors regulating expression of myelin proteins.

scholarly journals NO modulates myocardial O2consumption in the nonhuman primate: an additional mechanism of action of amlodipine

1999 ◽  
Vol 276 (6) ◽  
pp. H2069-H2075 ◽  
Author(s):  
Paul R. Forfia ◽  
Xiaoping Zhang ◽  
Delvin R. Knight ◽  
Andrew H. Smith ◽  
Christopher P. A. Doe ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Oxygen Consumption ◽  
Nonhuman Primate ◽  
Myocardial Oxygen Consumption ◽  
Channel Blocker ◽  
Tissue Response ◽  
Canine Heart ◽  
Additional Mechanism

Recent evidence from our laboratory and others suggests that nitric oxide (NO) is a modulator of in vivo and in vitro oxygen consumption in the murine and canine heart. Therefore, the goal of our study was twofold: to determine whether NO modulates myocardial oxygen consumption in the nonhuman primate heart in vitro and to evaluate whether the seemingly cardioprotective actions of amlodipine may involve an NO-mediated mechanism. Using a Clark-type O2 electrode, we measured oxygen consumption in cynomologous monkey heart at baseline and after increasing doses of S-nitroso- N-acetylpenicillamine (SNAP; 10−7–10−4M), bradykinin (10−7–10−4M), ramiprilat (10−7–10−4M), and amlodipine (10−7–10−5M). SNAP (−38 ± 5.8%), bradykinin (−19 ± 3.9%), ramiprilat (−28 ± 2.3%), and amlodipine (−23 ± 4.5%) each caused significant ( P < 0.05) reductions in myocardial oxygen consumption at their highest dose. Preincubation of tissue with nitro-l-arginine methyl ester (10−4 M) blunted the effects of bradykinin (−5.4 ± 3.2%), ramiprilat (−4.8 ± 5.0%), and amlodipine (−5.3 ± 5.0%) but had no effect on the tissue response to SNAP (−38 ± 5.8%). Our results indicate that NO can reduce oxygen consumption in the primate myocardium in vitro, and they support a role for the calcium-channel blocker amlodipine as a modulator of myocardial oxygen consumption via a kinin-NO mediated mechanism.

scholarly journals Schistosoma mansoni in Susceptible and Resistant Snail Strains Biomphalaria tenagophila: In Vivo Tissue Response and In Vitro Hemocyte Interactions

PLoS ONE ◽  
2012 ◽  
Vol 7 (9) ◽  
pp. e45637 ◽  
Author(s):  
Rafael Nacif-Pimenta ◽  
Ana Carolina Alves de Mattos ◽  
Alessandra da Silva Orfanó ◽  
Luciene Barbosa ◽  
Paulo Filemon Paolucci Pimenta ◽  
...  
Keyword(s):  
Schistosoma Mansoni ◽  
Tissue Response

Chondroitin sulfate activates B cells in vitro, expands CD138+cells in vivo, and interferes with established humoral immune responses

2014 ◽  
Vol 96 (1) ◽  
pp. 65-72 ◽  
Author(s):  
Hilke Brühl ◽  
Josef Cihak ◽  
Nicole Goebel ◽  
Yvonne Talke ◽  
Kerstin Renner ◽  
...  
Keyword(s):  
B Cells ◽  
Immune Responses ◽  
Chondroitin Sulfate ◽  
Humoral Immune ◽  
Humoral Immune Responses

scholarly journals THE LOSS OF PHENOTYPIC TRAITS BY DIFFERENTIATED CELLS

1966 ◽  
Vol 28 (3) ◽  
pp. 473-487 ◽  
Author(s):  
Joan Abbott ◽  
Howard Holtzer
Keyword(s):  
Dna Synthesis ◽  
Chondroitin Sulfate ◽  
Collagen Synthesis ◽  
Dna Interaction ◽  
Cell Multiplication ◽  
Phenotypic Traits ◽  
Embryonic Chick ◽  
Differentiated Cells ◽  
Genetically Determined

Observations were made on the behavior of chondrocytes grown under various conditions in vitro. The chondrocytes in 10-day embryonic chick vertebrae were grown as cultures of intact vertebrae, as pellets of chondrocytes liberated from their matrix, and as monodispersed cells plated out on plasma clots. Cartilage matrix was stained metachromatically with toluidine blue. Radioautographs were made of incorporated H3-thymidine, H3-proline, and S35-sulfate to determine the extent of DNA synthesis, collagen synthesis, and chondroitin sulfate synthesis, respectively. Chondrocytes in intact vertebrae or in pellets are rounded and actively synthesizing chondroitin sulfate and collagen. There is little DNA synthesis by cells in either vertebrae or pellets. Chondrocytes grown as monodisperse cells rapidly cease synthesizing cytologically detectable chondroitin sulfate and are induced to synthesize DNA and divide. There is a change in the shape of these chondrocytes from a rounded to a more stellate condition which accompanies the shift in metabolic activity. Conversely, when the cells attain a certain cell density, they reacquire a rounded shape, cease dividing, and again synthesize chondroitin sulfate. Clusters of chondrocytes synthesize more chondroitin sulfate than isolated chondrocytes. It is concluded that most chondrocytes synthesizing chondroitin sulfate do not concurrently synthesize DNA. Interaction between associated chondrocytes is important in inducing and maintaining chondroitin sulfate synthesis in genetically determined chondrocytes. Failure of interaction between chondrocytes leads to DNA synthesis and cell multiplication.

Comparison of In Vitro and In Vivo Rates of Collagen Synthesis in Normal and Damaged Lung Tissue

1986 ◽  
Vol 10 (2) ◽  
pp. 187-201 ◽  
Author(s):  
James P. Kehrer ◽  
Yu-Chen C. Lee ◽  
Suzanne M. Solem
Keyword(s):  
Lung Tissue ◽  
Collagen Synthesis
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