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1.
Diabetes Metab ; 35(3): 228-32, 2009 Jun.
Article in English | MEDLINE | ID: mdl-19349202

ABSTRACT

AIM: One objective of Ophdiat, a telemedical network using digital non-mydriatic cameras in Ile-de-France, is to develop a comprehensive screening programme that provides access to annual fundus examinations to all diabetic patients. The aim of this study was to evaluate the benefits of this programme in a hospital setting. METHODS: A retrospective analysis of 500 case reports of diabetic patients hospitalized before and after Ophdiat setup was performed in five reference hospital centres. At each centre, 100 case reports (50 before, 50 after) of patients aged greater than 18 years, hospitalized for their annual check-up, with no known diabetic retinopathy (DR) before hospitalization and with the last fundus examination performed greater than 11 months previously, were randomly selected. The primary endpoint was the proportion of patients whose fundus examinations were performed during hospitalization; secondary endpoints were the number of cases of DR found and the time taken by ophthalmologists to make the diagnosis. RESULTS: The mean proportion of patients with fundus examinations was 50.4% and 72.4% before and after, respectively, Ophdiat (P<0.01). The prevalence of DR was 11.1% before and 12.7% after (not significant). The mean time taken by an ophthalmologist per diagnosis of DR was 0.90 half-day before and 0.32 half-day after Ophdiat. CONCLUSION: This evaluation shows that Ophdiat, combined with the availability of modern and effective devices, has improved DR screening in diabetology departments in hospitals. Additional human resources would certainly ensure more effective use of the system.


Subject(s)
Telemedicine/methods , Adult , Aged , Aged, 80 and over , Diabetes Mellitus, Type 1/complications , Diabetes Mellitus, Type 2/complications , Diabetic Retinopathy/epidemiology , Diabetic Retinopathy/prevention & control , Female , France/epidemiology , Humans , Male , Mass Screening/methods , Middle Aged , Retrospective Studies , Young Adult
2.
Pathol Biol (Paris) ; 39(4): 277-82, 1991 Apr.
Article in French | MEDLINE | ID: mdl-2062552

ABSTRACT

The effect of procyanidole oligomers (PCOs) on the morphology of cultured human skin fibroblasts (FB) and swine aorta smooth muscle cells (SMC) was studied. Exposure to PCOs induced dose-dependent changes in the size, shape and arrangement of cultured fibroblasts. Smooth muscle cells did not exhibit similar changes. These findings demonstrate that procyanidole oligomers interact with fibroblasts membrane and cytoskeletal constituents. With smooth muscle cells the main site of action of procyanidole oligomers may be the basement membrane surrounding the cells, which is lacking in fibroblasts. Thus, in addition to their action on extracellular matrix constituents, i.e., collagen and elastin fibers, procyanidole oligomers affect structural components of cells, i.e., the cell membrane and cytoskeleton. This twofold action of procyanidole oligomers on mesenchymatous cells and their extracellular matrix may be a significant component of the pharmacologic action of procyanidole oligomers.


Subject(s)
Antihypertensive Agents/pharmacology , Biflavonoids , Catechin/analogs & derivatives , Cell Nucleus/drug effects , Fibroblasts/cytology , Muscle, Smooth, Vascular/cytology , Proanthocyanidins , Adolescent , Animals , Catechin/pharmacology , Cells, Cultured , Fibroblasts/drug effects , Fibroblasts/ultrastructure , Humans , Male , Muscle, Smooth, Vascular/drug effects , Muscle, Smooth, Vascular/ultrastructure , Swine
3.
Matrix ; 9(6): 479-85, 1989.
Article in English | MEDLINE | ID: mdl-2635761

ABSTRACT

Extracellular matrix macromolecules are involved in many aspects of cell biology. The knowledge concerning the presence, the distribution and the role of these macromolecules in the central nervous system has not yet received sufficient attention. In the present work we studied by indirect immunohistochemical methods the localisation of five extracellular matrix macromolecules in the spinal cord of rats: three collagens: type I, type III, and type IV, and two structural glycoproteins: laminin and fibronectin. We found that all five macromolecules are present in the spinal cord of normal animals. They are localised exclusively in the connective type tissues: the meningeal sheets and the vascular walls. Only type I and type III collagens and fibronectin could be demonstrated around the epithelial cells of the ependyma.


Subject(s)
Collagen/metabolism , Extracellular Matrix/metabolism , Fibronectins/metabolism , Laminin/metabolism , Spinal Cord/metabolism , Animals , Immunohistochemistry , Male , Rats , Rats, Inbred Strains , Spinal Cord/cytology
4.
Biochem Biophys Res Commun ; 153(2): 690-8, 1988 Jun 16.
Article in English | MEDLINE | ID: mdl-3132918

ABSTRACT

In rabbit articular chondrocytes, phorbol myristate acetate (PMA), 1,2-dioctanoyl-sn-glycerol (DG) and calcium ionophore (A23187), reduced the proteoglycan synthesis, in a dose-dependent manner. The combined treatment by PMA and A23187 resulted in an enhanced inhibition of proteoglycan production, indicating a synergistic effect. In presence of PMA or A23187, the release of prostaglandin E2 (PGE2) was dramatically increased. The addition of indomethacin and BW755c to chondrocytes stimulated by PMA or A23187, suppressed the liberation of PGE2, but did not stop the decrease of proteoglycan synthesis.


Subject(s)
Calcimycin/pharmacology , Cartilage, Articular/metabolism , Prostaglandins E/metabolism , Proteoglycans/biosynthesis , Tetradecanoylphorbol Acetate/pharmacology , 4,5-Dihydro-1-(3-(trifluoromethyl)phenyl)-1H-pyrazol-3-amine , Animals , Arachidonic Acids/physiology , Diglycerides/pharmacology , Dinoprostone , Drug Synergism , Indomethacin/pharmacology , Pyrazoles/pharmacology , Rabbits
5.
Biochim Biophys Acta ; 927(1): 34-42, 1987 Jan 19.
Article in English | MEDLINE | ID: mdl-3098300

ABSTRACT

Cultured human synovial cells treated with an interleukin-1-like mononuclear cell factor incorporated more 35S in proteoglycans than control cultures, but the radioactivity distribution between medium and cell layer was not modified. Proteoglycans were synthesized essentially in monomeric form and the mononuclear cell factor increased the molecular weight of these monomers. The [3H]hexosamine/[14C]serine ratio in purified proteoglycans on the one hand, and the study of [35S]glycosaminoglycan molecular weight, on the other hand, indicated that this increase is not modulated through enhanced synthesis of core protein but by an increase in the glycosaminoglycan chain length. After enzyme hydrolysis, dermatan sulfate (62% of the total glycosaminoglycans) and chondroitin 4/6-sulfate (30%) were found to be the major glycosaminoglycans synthesized by cultured synovial cells, and the existence of 8% heparan sulfate was evidenced by nitrous acid treatment. In the presence of the mononuclear cell factor, the dermatan sulfate synthesis was decreased (47%), with a concomitant increase of chondroitin sulfate synthesis (45%).


Subject(s)
Proteins/pharmacology , Proteoglycans/biosynthesis , Synovial Membrane/metabolism , Aged , Cells, Cultured , Chondroitin Sulfates/biosynthesis , Female , Glycosaminoglycans/biosynthesis , Hexosamines/metabolism , Humans , Male , Middle Aged , Molecular Weight , Monokines , Serine/metabolism , Synovial Membrane/drug effects
6.
Biochem Biophys Res Commun ; 134(2): 539-49, 1986 Jan 29.
Article in English | MEDLINE | ID: mdl-3484951

ABSTRACT

A partially purified monocyte factor, with Interleukin-1 properties (MCF/IL-1), enhances the proteoglycan synthesis of human neonatal articular chondrocytes in culture, and changes the repartition of these macromolecules between medium and cell layer. The size of the proteoglycan monomers, the length of the glycosaminoglycan chains and the respective levels of chondroitin-6-sulfate, chondroitin-4-sulfate and non sulfated chondroitin remain unchanged under MCF/IL-1 exposures. The addition of indomethacin reduces the stimulation effect by 60-70% only, suggesting that the MCF/IL-1 action is partially dependent on prostaglandins but seems also related to mechanisms distinct from the cyclooxygenase pathway.


Subject(s)
Cartilage, Articular/metabolism , Interleukin-1/pharmacology , Monocytes/physiology , Proteoglycans/biosynthesis , Cartilage, Articular/cytology , Cells, Cultured , Glycosaminoglycans/analysis , Humans , Indomethacin/pharmacology , Molecular Weight , Monocytes/analysis , Monokines , Prostaglandins/physiology , Proteins/pharmacology , Proteoglycans/analysis
7.
Exp Cell Res ; 160(1): 9-18, 1985 Sep.
Article in English | MEDLINE | ID: mdl-3930273

ABSTRACT

Treatment of cultured human synovial cells with a mononuclear cell factor (MCF) enhanced their ability to synthesize glycosaminoglycans (GAG), but GAG repartition between extracellular, pericellular and intracellular compartments was found to be the same as in control. Hyaluronic acid (HA) production, which represents 80-90% of all secreted GAG, was stimulated 2 1/2-3-fold, but the HA molecular weight was not modified. The MCF increased the hyaluronate synthetase activity of synovial cells in similar proportions. Actinomycin D inhibited the increase in hyaluronate synthetase activity produced by MCF, indicating that this increase involves new synthesis of mRNA. Stimulation of both HA synthesis and hyaluronate synthetase activity by MCF was suppressed by 10(-4)-10(-5) M indomethacin (an inhibitor of cyclo-oxygenase), suggesting that MCF effect is prostaglandin-dependent.


Subject(s)
Glycosyltransferases , Hyaluronic Acid/biosynthesis , Membrane Proteins , Proteins/pharmacology , Synovial Membrane/metabolism , Transferases , Xenopus Proteins , Aged , Cells, Cultured , Dactinomycin/pharmacology , Female , Glucosamine/metabolism , Glucuronosyltransferase/metabolism , Humans , Hyaluronan Synthases , Indomethacin/pharmacology , Male , Middle Aged , Molecular Weight , Monokines , Synovial Membrane/drug effects , Synovial Membrane/enzymology
8.
FEBS Lett ; 186(2): 233-40, 1985 Jul 08.
Article in English | MEDLINE | ID: mdl-4007165

ABSTRACT

Addition of ascorbic acid (25, 50 100 micrograms/ml) to cultures of rabbit articular chondrocytes did not change the total amount of proteoglycans produced. However, it induced an increased retention of these macromolecules in the pericellular fraction. The size of the proteoglycan subunits and the length of glycosaminoglycan chains, released in the medium, were not modified on exposure to ascorbic acid (25 micrograms/ml). On the other hand, the rate of non-sulfated chondroitin was increased 2.5-fold, whereas chondroitin-4-sulfate was depressed 1.5-fold.


Subject(s)
Ascorbic Acid/pharmacology , Cartilage, Articular/metabolism , Proteoglycans/metabolism , Animals , Cartilage, Articular/drug effects , Cells, Cultured , Culture Media , Glycosaminoglycans/biosynthesis , Glycosaminoglycans/isolation & purification , Glycosaminoglycans/metabolism , Kinetics , Rabbits
9.
Biochem Biophys Res Commun ; 119(2): 499-508, 1984 Mar 15.
Article in English | MEDLINE | ID: mdl-6585202

ABSTRACT

A monocyte cell factor (MCF) inhibited the incorporation of (3H)proline into collagen of rabbit articular chondrocytes in culture, without significant effect on non-collagen protein. In addition, MCF produced a new compartmental repartition of collagen between cell layer and medium. No MCF-induced shift was observed in the relative proportion of collagens synthesized, type II remaining the major collagenous product. The inhibitory effect of MCF was not completely suppressed when prostaglandin synthesis was blocked by indomethacin. Addition of PGE2 at 12.5-25 micrograms/ml to the cultures resulted in a decrease of total collagen. Lower concentrations (0.42-0.85 microgram/ml) did not affect the total synthesis of collagen but changed its distribution between cells and medium in the same way as MCF. These results suggest that the MCF-stimulated release of PGE2 may be partially involved in the inhibitory effect observed on collagen synthesis.


Subject(s)
Cartilage, Articular/metabolism , Collagen/biosynthesis , Monocytes/metabolism , Prostaglandins E/pharmacology , Animals , Cartilage, Articular/drug effects , Cells, Cultured , Collagen/isolation & purification , Dinoprostone , Indomethacin/pharmacology , Kinetics , Proline/metabolism , Protein Biosynthesis , Rabbits , Tritium
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