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4. Effects of cryopreservation on the proliferation and anticoagulant activity of human saphenous vein endothelial cells

Author

Bambang, L.S., Mazzucotelli, J.P., Moczar, M., Beaujean, F., and Loisance, D.

Subjects
Von Willebrand factor, Dimethyl sulfoxide, Protein C, Endothelium, Health
Abstract

Byline: L.S. Bambang (a), J.P. Mazzucotelli (a), M. Moczar (a), F. Beaujean (a), D. Loisance (a ) Abstract: Human saphenous veins were cryopreserved in 4% human albumin and 10% dimethyl sulfoxide. The effect of cryopreservation on endothelial cells was studied in terms of the anticoagulant activity of thrombomodulin and in terms of cell proliferation. After storage for 2 weeks at -150[degrees]C, 0.45 [+ or -] 0.07 x 10.sup.5 endothelial cells/cm.sup.2 were detected in cryopreserved veins and 1.03 [+ or -] 0.04 x 10.sup.5 endothelial cells/cm.sup.2 in fresh veins (p < 0.01). The thrombin-catalyzed activation of protein C decreased after cryopreservation, indicating altered thrombomodulin activity in the endothelial cells. On a cell number basis, the release of soluble thrombomodulin was three times higher from the cryopreserved endothelium than from the fresh endothelium (p < 0.05). The amount of spontaneous release of von Willebrand factor from the endothelial surface was not significantly different between fresh and cryopreserved veins. Endothelial cells were cultured from fresh veins and from their cryopreserved counterparts. On plating of endothelial cells in primary culture, the number of adhered cells was 0.9 [+ or -] 0.09 x 10.sup.3 cells/cm.sup.2 from fresh veins and 0.25 [+ or -] 0.0 x 10.sup.3 cells/cm.sup.2 from cryopreserved veins (p < 0.01). The positive immunohistochemical stain for von Willebrand factor indicated that the endothelial cell character was maintained after cryopreservation. The endothelial desquamation with loss of anticoagulant function and the slow proliferation of surviving cells in vitro suggest an impaired endothelial healing in vivo. The loss of anticoagulant activity complicates the problems of the exposure of thrombogenic subendothelial matrix to blood in implanted cryopreserved veins. Author Affiliation: (a ) Centre de Recherches Chirurgicales Henri Mondor, CNRS URA 1431, Creteil, France (a) Centre Departemental de Transfusion Sanguine, CHU Henri Mondor, Creteil, France Article History: Received 12 August 1994; Accepted 23 December 1994

Published
1995

8. Late abstracts 186–187

Author

Jaehne, J., Meyer, H. -J., Wittekind, Ch., Maschek, H., Pichlmayr, R., Jacobi, G., Weiermann, G., Vitzthum, H. Gräfin, Schwabe, D., Manegold, Ch., Krempien, B., Kaufmann, M., Bailly, M., Doré, J. -F., Fodstad, Ø., Kjønniksen, I., Brøgger, A., Flørenes, V. A., Pihl, A., Aamdal, S., Nesland, J. M., Geldof, A. A., Rao, B. R., De Giovanni, C., Lollini, P. -L., Del Re, B., Scotlandi, K., Nicoletti, G., Nanni, P., Van Muijen, G. N. P., Van Der Wiel-Miezenbeek, J. M., Cornelissen, L. M. H. A., Jansen, C. F. J., Ruiter, D. J., Kieler, J., Oda, Y., Tokuriki, Y., Tenang, E. M., Lamb, J. F., Galante, E., Zanoni, F., Galluzzi, D., Cerrotta, A., Martelli, G., Guzzon, A., Reduzzi, D., Barberá-Guillem, E., Barceló, J. R., Urcelay, B., Alonso-Varona, A. I., Vidal-Vanaclocha, F., Bassukas, I. D., Maurer-Schultze, B., Storeng, R., Manzotti, C., Pratesi, G., Schachert, G., Fidler, I. J., Grimstad, I. A., Rutt, G. Th., Riesinger, P., Frank, J., Neumann, G., Wissler, J. H., Bastert, G., Liebrich, W., Lehner, B., Gonzer, S., Schlag, P., Vehmeyer, K., Hajto, T., Gabius, H. -J., Funke, I., Schlimok, G., Bock, B., Dreps, A., Schweiberer, B., Riethmüller, G., Nicolai, U., Vykoupil, K. -F., Wolf, M., Havemann, K., Georgii, A., Bertrand, S., N'Guyen, M. -J., Siracky, J., Kysela, B., Siracka, E., Pflüger, E., Schirrmacher, V., Boyano, M. D., Hanania, N., Poupon, M. F., Sherbet, G. V., Lakshmi, M. S., Van Roy, F., Vleminckx, K., Fiers, W., Dragonetti, C., De Bruyne, G., Messiaen, L., Mareel, M., Kuhn, S., Choritz, H., Schmid, U., Bihl, H., Griesbach, A., Matzku, S., Eccles, S. A., Purvies, H. P., Miller, F. R., McEachern, D., Ponton, A., Waghorne, C., Coulombe, B., Kerbel, R. S., Breitman, M., Skup, D., Gingras, M. C., Jarolim, L., Wright, J. A., Greenberg, A. H., N'Guyen, M. J., Allavena, G., Melchiori, A., Aresu, O., Percario, M., Parodi, S., Schmidt, J., Kars, P., Chader, G., Albini, A., Zöller, M., Lissitzky, J. C., Bouzon, M., Martin, P. M., Grossi, I. M., Taylor, J. D., Honn, K. V., Koch, B., Baum, W., Giedl, J., Gabius, H. J., Kalden, J. R., Hakim, A. A., LadÁnyi, A., Timár, J., Moczar, E., Lapis, K., Müller, K., Wolf, M. F., Benz, B., Schumacher, K., Kemmner, W., Morgenthaler, J., Brossmer, R., Hagmar, B., Burns, G., Erkell§, L. J., Ryd, W., Paku, S., Rot, A., Hilario, E., Unda, F., Simón, J., Aliño, S. F., Sargent, N. S. E., Burger, M. M., Altevogt, P., Kowitz, A., Chopra, H., Bandlow, G., Nagel, G. A., Lotan, R., Carralero, D., Lotan, D., Raz, A., Skubitz, A. P. N., Koliakos, G. G., Furcht, L. T., Charonis, A. S., Hamann, A., Jablonski-Westrich, D., Jonas, P., Harder, R., Butcher, E. C., Thiele, H. G., Breillout, F., Antoine, E., Lascaux, V., Boxberger, H. -J., Paweletz, N., Bracke, M., Vyncke, B., Opdenakker, G., Castronovo, V., Foidart, J. -M., Camacho, M., Fras, A. Fabra, Llorens, A., Rutllant, M. L., Erkell, L. J., Brunner, G., Heredia, A., Imhoff, J. M., Burtin, P., Nakajima, M., Lunec, J., Parker, C., Fennelly, J. A., Smith, K., Roossien, F. F., La Rivière, G., Roos, E., Erdel, M., Trefz, G., Spiess, E., Ebert, W., Verhaegen, S., Remels, L., Verschueren, H., Dekegel, D., De Baetselier, P., Van Hecke, D., Hannecart-Pokorni, E., Falkvoll, K. H., Alonso, A., Baroja, A., Sebbag, U., Barbera-Guillem, E., Behrens, J., Mareel, M. M., Birchmeier, W., Waterhouse, P., Khokha, R., Chambers, A., Yagel, S., Lala, P. K., Denhardt, D. T., Hennes, R., Frantzen, F., Keller, R., Schwartz-Albiez, R., Fondaneche, M. C., Mignatti, P., Tsuboi, R., Robbins, E., Rifkin, D. B., Overall, C. M., Sacchi, A., Falcioni, R., Piaggio, G., Rizzo, M. G., Perrotti, N., Kennel, S. J., Girschick, H., Müller-Hermelink, H. K., Vollmers, H. P., Wenzel, A., Liu, S., Günthert, U., Wesch, V., Giles, M., Ponta, H., Herrlich, P., Stade, B., Hupke, U., Holzmann, B., Johnson, J. P., Sauer, A., Roller, E., Klumpp, B., Güttler, N., Lison, A., Walk, A., Redini, F., Moczar, M., Leoni, F., Da Dalt, M. G., Ménard, S., Canevari, S., Miotti, S., Tagliabue, E., Colnaghi, M. I., Ostmeier, H., Suter, L., Possati, L., Rosciani, C., Recanatini, E., Beatrici, V., Diambrini, M., Polito, M., Rothbächer, U., Eisenbach, L., Plaksin, D., Gelber, C., Kushtai, G., Gubbay, J., Feldman, M., Benke, R., Benedetto, A., Elia, G., Sala, A., Belardelli, F., Lehmann, J. M., Ladanyi, A., Hanisch, F. -G., Sölter, J., Jansen, V., Böhmer, G., Peter-Katalinic, J., Uhlenbruck, G., O'Connor, R., Müller, J., Kirchner, T., Bover, B., Tucker, G., Valles, A. M., Gavrilovic, J., Thiery, J. P., Kaufmann, A. M., Volm, M., Edel, G., Zühlsdorf, M., Voss, H., Wörmann, B., Hiddemann, W., De Neve, W., Van Den Berge, D., Van Loon, R., Storme, G., Zacharski, L. R., Wojtukiewicz, M. Z., Memoli, V., Kisiel, W., Kudryk, B. J., Stump, D., Piñol, G., Gonzalez-Garrigues, M., Fabra, A., Marti, F., Rueda, F., Lichtner, R. B., Khazaie, K., Timar, J., Greenzhevskaya, S. N., Shmalko, Yu. P., Hill, S. E., Rees, R. C., MacNeil, S., Millon, R., Muller, D., Eber, M., Abecassis, J., Betzler, M., Bahtsky, K. P., Umansky, V. Yu., Krivorotov, A. A., Balitskaya, E. K., Pridatko, O. E., Smelkova, M. I., Smirnov, I. M., Korczak, B., Fisher, C., Thody, A. J., Young, S. D., Hill, R. P., Frixen, U., Gopas, J., Segal, S., Hammerling, G., Bar-Eli, M., Rager-Zisman, B., Har-Vardi, I., Alon, Y., Hämmerling, G. J., Perez, M., Algarra, I., Collado, Ma. D., Peran, E., Caballero, A., Garrido, F., Turner, G. A., Blackmore, M., Stern, P. L., Thompson, S., Levin, I., Kuperman, O., Eyal, A., Kaneti, J., Notter, M., Knuth, A., Martin, M., Chauffert, B., Caignard, A., Hammann, A., Martin, F., Dearden, M. T., Pelletier, H., Dransfield, I., Jacob, G., Rogers, K., Pérez-Yarza, G., Cañavate, M. L., Lucas, R., Bouwens, L., Mantovani, G., Serri, F. G., Macciò, A., Zucca, M. V., Del Giacco, G. S., Pérez, M., Kärre, K., Apt, D., Traversari, C., Sensi, M., Carbone, G., Parmiani, G., Hainaut, P., Weynants, P., Degiovanni, G., Boon, T., Marquardt, P., Stulle, K., Wölfel, T., Herin, M., Van den Eynde, B., Klehmann, E., Büschenfelde, K. -H. Meyer zum, Samija, M., Gerenčer, M., Eljuga, D., Bašić, I., Heacock, C. S., Blake, A. M., D'Aleo, C. J., Alvarez, V. L., Gresser, I., Maury, C., Moss, J., Woodrow, D., von Ardenne, M., Krüger, W., Möller, P., Schachert, H. K., Itaya, T., Frost, P., Rodolfo, M., Salvi, C., Bassi, C., Huland, E., Huland, H., Sersa, G., Willingham, V., Hunter, N., Milas, L., Schild, H., von Hoegen, P., Mentges, B., Bätz, W., Suzuki, N., Mizukoshi, T., Sava, G., Ceschia, V., Zabucchi, G., Farkas-Himsley, H., Schaal, O., Klenner, T., Keppler, B., Alvarez-Diaz, A., Bizzari, J. P., Barbera-Guillem, F., Osterloh, B., Bartkowski, R., LÖhrke, H., Schwahn, E., Schafmayer, A., Goerttler, K., Cillo, C., Ling, V., Giavazzi, R., Vecchi, A., Luini, W., Garofalo, A., Iwakawa, M., Arundel, C., Tofilon, P., Giraldi, T., Perissin, L., Zorzet, S., Piccini, P., Pacor, S., Rapozzi, V., Fink, U., Zeuner, H., Dancygier, H., Classen, M., Lersch, C., Reuter, M., Hammer, C., Brendel, W., Mathé, G., Bourut, C., Chenu, E., Kidani, Y., Mauvernay, Y., Schally, A. V., Reizenstein, P., Gastiaburu, J., Comaru-Schally, A. M., Cupissol, D., Jasmin, C., Missot, J. L., Wingen, F., Schmähl, D., Pauwels-Vergely, C., Poupon, M. -F., Gasic, T. B., Ewaskiewicz, J. I., Gasic, G. J., Pápay, J., Mauvernay, R., Schally, A., Keiling, R., Hagipantelli, R., Busuttil, M., VoVan, M. L., Misset, J. L., Lévi, F., Musset, M., Ribaud, P., Hilgard, P., Reissmann, T., Stekar, J., Voegeli, R., Den Otter, W., Maas, H. A., Dullens, H. F. J., Merriman, R. L., Tanzer, L. R., Shackelford, K. A., Bemis, K. G., Campbell, J. B., and Matsumoto, K.

Published
1988
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15. Effect of an alpha-blocker (Nicergoline) and of a beta-blocker (Acebutolol) on the in vitro biosynthesis of vascular extracellular matrix

Author

Moczar M, Alexandre Robert, B. Jacotot, and Ladislas Robert

Subjects
Proline, Lysine, Adrenergic beta-Antagonists, Tritium, Acebutolol, Muscle, Smooth, Vascular, Glycosaminoglycan, chemistry.chemical_compound, Hydroxyproline, Biosynthesis, Glucosamine, Culture Techniques, Animals, Carbon Radioisotopes, Hyaluronic Acid, Adrenergic alpha-Antagonists, Aorta, Glycosaminoglycans, Extracellular Matrix Proteins, Nicergoline, biology, General Medicine, Arteries, chemistry, Biochemistry, Proteoglycan, biology.protein, Collagen, Heparitin Sulfate, Rabbits, Elastin
Abstract

The effect of an α -blocking agent and of a β -blocking agent on the biosynthesis of extracellular matrix macromolecules of the arterial wall was investigated. Rabbit aorta explants were cultured up to 48 hours with radioactive proline, lysine or glucosamine. In presence of these drugs, at concentration shown to be effective for the inhibition of platelet-endothelial cell interactions (10 –7 M), the incorporation of 14 C proline in total macromolecular proline was higher than in macromolecular hydroxyproline suggesting a relatively higher rate of biosynthesis of non-collagenous proteins as compared to collagens. The α -blocking increased the incorporation of 14 C proline in collagenous and non-collagenous proteins after 18 hours of incubation. β -blocking also increased the incorporation of proline in macromolecular proline and hydroxyproline as compared to control cultures. Both increased the incorporation of 3 H glucosamine in newly synthesised glycosaminoglycans. β -blocking increased mainly the neosynthesis of heparan sulphate, α -blocking that of hyaluronan. The incorporation of 14 C-lysine in crosslinked, insoluble elastin was not modified. These experiments confirm that α and β -blocking agents can influence not only the tonus of aortic smooth muscle cells but also the relative rates of biosynthesis of extracellular matrix macromolecules. This effect should be taken in consideration for the evaluation of the long range effect of α and β -blocking drugs on the vascular wall.

Published
2001

23. Inflammatory response to cardiopulmonary bypass using two different types of heparin-coated extracorporeal circuits.

Author

Baufreton, C., Moczar, M., Jansen, P.G.M., te Velthuis, H., Le Besnerais, P., Farcet, J.P., and Wildevuur, C.R.H.

Subjects
*INFLAMMATION, *CARDIOPULMONARY bypass, *CELL adhesion molecules
Abstract

Previous reports have highlighted the disparity in biocompatibility of two differently engineered heparin coatings during the cardiopulmonary bypass (CPB) procedure. The aim of this prospective study was to evaluate the impact of the difference in haemocompatibility provided by either the Duraflo II equipment or the Carmeda equipment in the terminal inflammatory response observed after coronary artery surgery. Thirty patients were randomly allocated to two groups to be operated on using either Duraflo II equipment (group I) or Carmeda equipment (group 2) for extracorporeal circulation (ECC). Initial inflammatory response was assessed by terminal complement complex activation (SC5b-9). The late inflammatory response observed in the postoperative period was assessed by measuring cytokine production (tumour factor necrosis (TNFα), interleukin IL-6, interleukin IL-8) and circulating concentrations of adhesion molecules (ELAM-1, ICAM-1). The release of SC5b-9 after CPB and after protamine administration was lower in group 2 than in group 1 (p = 0.0002 and p = 0.006, respectively). A significant production of cytokines was detected in both groups with peak values observed within the time range of 4–6 h after the start of CPB. However, no difference was observed between the groups except for the IL-8 level in group 2, which was lower 2 h after the start of CPB (p = 0.01). Plasma levels of adhesion molecules were similar in both groups within the investigation period. Although the Carmeda equipment was more effective in reducing complement activation, the late inflammatory response was similar using either the Duraflo II or Carmeda equipment for extracorporeal circulation as reflected by the changes of cytokine and circulating adhesion molecule levels. [ABSTRACT FROM AUTHOR]

Published
1998
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28. Études sur les fractions glucidiques de la trame fibreuse insoluble du stroma cornéen.

Author

Moczar, E., Robert, L., and Moczar, M.

Subjects
CORNEA, COLLAGENASES, GLYCOPEPTIDES, GEL permeation chromatography, ELECTROPHORESIS, AMINO acid analysis
Abstract

Calf corneas were extracted with a buffer containing M CaCl2, 0.05 M Tris and 0.02 M citric acid, at pH 7.5. The residual stroma was digested successively by colagenase and pronase. The glycopeptides obtained were separated by gel filtration and high voltage electrophoresis. The sugar and amino acid content of the isolated glycopeptides was determined. Two types of sugar chains were detected: (a) chains with a more complicated structure, containing galactose, glucose, mannose and glucosamine; (b) disaccharidic and monosaccharidic side chains containing galactose and glucose or galactose alone and linked O-glycosidically to the OH groups of hydroxylysine. The Hyl-Gal-Glc compoud was isolated and identified with the compound isolated by Butler and Cunningham from calf skin collagen, by the study of its composition, thin layer chromatography and high voltage electrophoresis. The stroma of the calf cornea contains about 4 times more hexoses in the small glycopeptides of type b (di- and monosaccharides) than in the higher molecular weight mannose-containing chains. [ABSTRACT FROM AUTHOR]

Published
1968
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29. Isolation and characterization of lung connective-tissue glycoproteins

Author

Lafuma, C, Moczar, M, and Robert, L

Abstract

1. Glycoproteins of hamster, rat and baboon lung parenchyma were investigated by using [14C]glucosamine incorporation in vitro followed by sequential extraction of the macromolecular components and characterization of the glycoproteins in the extracts. 2. Slices of lung parenchyma maintained in vitro incorporated [U-14C]glucosamine linearly with time into non-diffusible macromolecules for up to 5h. All the macromolecule-associated 14C label was present as [14C]glucosamine. 3. These 14C-labelled macromolecules were extracted from previously delipidated and salt-extracted lung by 5M-guanidinium chloride in the presence of dithiothreitol and proteinase inhibitors before (extract A1) and after (extract A2) hydrolysis of the collagen by collagenase. The [14C]glucosamine-labelled glycoproteins in extracts A1 and A2 contained 55 and 5% respectively of the total [14C]glucosamine incorporated in the lung of all three species studied. 4. The [14C]glucosamine-labelled glycoproteins were analysed by gel-filtration chromatography, sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and isoelectric focusing. The major [14C]glucosamine-labelled glycoproteins of baboon lung parenchyma had apparent mol.wts. of about 400 000, 140 000 and 65 000 with isoelectric points respectively of 4.8, 5.4 and 5.4. The hamster lung glycoproteins with isoelectric points of 4.1 and 5.8 were devoid of hydroxyproline and contained galactose, mannose and N-acetylglucosamine. These experiments indicate that several distinct glycoproteins are synthesized in situ by the cells of pulmonary parenchyma and may well play a role in its structure and function.

Published
1982
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30. Proteoglycans from pig aorta. Comparative study of their interactions with lipoproteins

Author

Wegrowski, J, Moczar, M, and Robert, L

Abstract

Different proteoglycans (PGs) were isolated from pig aorta for aggregation studies with hyaluronic acid and human low-density lipoproteins (LDL). Extraction of the intima-media with 4M-guanidinium chloride and digestion of the residue with collagenase solubilized 91% of aortic hexuronic acid content. From the guanidinium chloride extract two PGs were isolated by ion-exchange and gel-permeation chromatography: proteochondroitin sulphate (PGI) with a protein-core apparent Mr of 250 000 and proteodermatan-chondroitin sulphate (PGII) with a protein-core apparent Mr of 55 000. Only PGI forms high-Mr aggregates with hyaluronic acid. From the collagenase digest two other PGs were isolated: proteoheparan sulphate and proteochondroitin sulphate (PGIII and PGIV respectively). PGIV had a smaller hydrodynamic size than PGI. PGI and PGII formed insoluble complexes with human LDL in the presence of Ca2+. PGIII or PGIV did not form precipitates with the LDL. PGI and PGII, but neither PGIII nor PGIV, were bound to LDL-Sepharose. The main peaks of PGI and PGII were eluted from LDL-Sepharose with 60 mM- and 90 mM-NaCl respectively. The results indicate that aortic PGs have different interacting potentials with lipoproteins, depending on their Mr and their glycosaminoglycan composition.

Published
1986
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31. Structural glycoproteins from rabbit aortic media

Author

Moczar, M, Phan-Dinh-Tuy, B, Moczar, E, and Robert, L

Abstract

Rabbit aortic intima-media fragments were incubated with [14C]mannose and [3H]fucose for 6 h to detect glycoproteins synthesized in situ. The radioactively labelled and the non-labelled samples were extracted with 0.2 mM-CaCl2/0.5 mM-dithiothreitol/0.5 mM-ATP and chloroform/methanol/water (4:4:1, by vol.). The delipidated residue was extracted with 5 M-guanidinium chloride/0.05 M-dithiothreitol/0.1 M-Tris/0.4% Na2EDTA, pH 7.5, before (extract 1) and after hydrolysis with collagenase (extract 2). The proteins in extracts 1 and 2 were S-carboxamidomethylated and separated by molecular-sieve chromatography, polyacrylamide-gel electrophoresis and isoelectric focusing in sucrose gradients in urea. The apparent molecular weights of glycoproteins were 36 000 (glycoprotein I) from extract 1, 50 000 (glycoprotein II) and 130 000 (glycoprotein III) from extract 2. The molecular weights of the non-labelled and radioactively labelled glycoproteins were identical. Glycoproteins I, II and III contain large amounts of polar amino acids and methionine. They contain neither hydroxyproline nor 3-methylhistidine. A hydroxyproline-containing component of 160 000-apparent-mol.wt. relatively rich in polar amino acids and labelled with incorporated sugars was isolated from extract 1. The incorporation in vitro of radioactive sugars into glycoproteins I, II, III and collagenous glycoproteins indicates that they are synthesized in the surviving aorta by the smooth-muscle cells.

Published
1983
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32. Biosynthesis of skin collagens in normal and diabetic mice

Author

Kern, P, Moczar, M, and Robert, L

Abstract

Synthesis of collagens in vitro was studied on minced mouse skins incubated with [3H]-proline in organ-culture conditions. A comparative study was carried out on genetically diabetic mice (KK strain) and control mice (Swiss strain). After incubation, neutral-salt-soluble and acid-soluble collagens were extracted. The insoluble dermis was digested by pepsin and type I and type III collagens separated by differential precipitation in neutral salt solutions. Type I and Type III collagens were characterized by ion-exchange and molecular-sieve chromatography, amino acid analysis and by the characterization of CNBr peptides. In diabetic-mouse skin, the relative proportion of type III collagen was significantly higher than in control-mouse skin. The incorporation of radioactively labelled proline into hydroxyproline of type III collagen was significantly faster in diabetic-mouse skin than in control-mouse skin. No significant modifications in the total collagen content of the skin or of their rates of synthesis were observed between the two strains. Alteration in the ratio of type III to type I collagen in the diabetic-mouse skin can be interpreted as a sign of alteration of the regulation of collagen biosynthesis and may be related to the structural alterations observed in the diabetic intercellular matrix.

Published
1979
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