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216 results on '"Rauterberg J"'

1. The Pathogenesis of Atherosclerosis

Author

Cullen, P., Rauterberg, J., Lorkowski, S., Starke, K., editor, Born, G.V.R., editor, Eichelbaum, M., editor, Ganten, D., editor, Hofmann, F., editor, Rosenthal, W., editor, Rubanyi, G., editor, and von Eckardstein, Arnold, editor

Published
2005
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14. Hepatologie II

Author

Junge, U., Friedl, P., Staritz, M., Ewe, K., Meyer zum Büschenfelde, K.-H., Räth, U., Zuna, I., Schlaps, D., Limberg, B., Lorenz, A., van Kaick, G., Lorenz, W. J., Kommerell, B., Hoensch, H., Schreyer, I., Pott, G., Rauterberg, J., Schneider, M., Högemann, B., Eberhardt, G., Gerlach, U., Miehlke, Klaus, editor, and Bergmann, J. F.

Published
1984
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15. Diabetes I

Author

Hasslacher, Ch., Stech, W., Wahl, P., Ritz, E., Schmidt, H., Riemann, J. F., Schmid, A., Sailer, D., Högemann, B., Voss, B., Pott, G., Rauterberg, J., Gerlach, U., Schmülling, R.-M., Jakober, B., Sigmund, D., Margaritidou-Weber, D., Eggstein, M., Petzoldt, R., Miehlke, Klaus, editor, and Bergmann, J. F.

Published
1984
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16. Hepatologie

Author

Gmelin, K., Doerr, H. W., Stecher, J., Sann, G., Kommerell, B., Brattig, N. W., Hausch, F., Henning, H., Berg, P. A., Poralla, T., Hütteroth, T. H., Meyer zum Büschenfelde, K.-H., Hess, G., Arnold, W., Drescher, M., Ohlen, J., Korb, G., Selmair, H., Köhler, H., Renschin, G., Pausch, J., Rasenack, J., Häussinger, D., Gerok, W., Theilmann, L., Stollman, Y. R., Arias, I. M., Wolkoff, A. W., André, M., Hoensch, H., Limberg, B., Leimenstoll, G., Kamenisch, W. R., Moch, K. J., Homann, J., Matthes, K. J., Rössle, M., Herz, R., Lehmann, G., Luft, M., Egberts, E.-H., Hamster, W., Schomerus, H., Jürgens, P., Pape, G. R., Rieber, E. P., Eisenburg, J., Lohmeyer, J., Hoffmann, R., Thoenes, G. H., Knapp, W., Riethmüller, G., Nagai, S., Manns, M., Schultheiß, H.-P., Berg, P.-A., Klingenberg, M., Weckenmann, U., Weber, P., Stechemesser, E., Klöppel, G., Dancygier, H., Schneider, M., Leuschner, U., Hübner, K., Classen, M., Högemann, B., Pott, G., Voss, B., Rauterberg, J., Gerlach, U., Sixel, F., Doss, M., and Schlegel, Bernhard, editor

Published
1982
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27. Rupture of the atherosclerotic plaque: does a good animal model exist?

Author

Cullen, P., Baetta, R., Bellosta, S., Bernini, F., Chinetti, G., Cignarella, A., von Eckardstein, A., Exley, A., Goddard, M., Hofker, M.H., Hurt-Camejo, E., Kanters, E., Kovanen, P., Lorkowski, S., McPheat, W., Pentikainen, M., Rauterberg, J., Ritchie, A., Staels, B., Weitkamp, B., de Winther, M.P.J., MAFAPS, Consortium, Moleculaire Genetica, Moleculaire Celbiologie, RS: NUTRIM School of Nutrition and Translational Research in Metabolism, RS: CARIM School for Cardiovascular Diseases, and Other departments

Subjects
Pathology, medicine.medical_specialty, Arteriosclerosis, Swine, Mice, Animal model, Dogs, Species Specificity, Thromboembolism, Medicine, Animals, Humans, Thrombus, Columbidae, Aged, Rupture, Spontaneous, business.industry, Coronary Thrombosis, Plaque rupture, Middle Aged, medicine.disease, Rats, Models, Animal, Rabbits, Cardiology and Cardiovascular Medicine, business
Abstract

Rupture of the atherosclerotic plaque: does a good animal model exist?Cullen P, Baetta R, Bellosta S, Bernini F, Chinetti G, Cignarella A, von Eckardstein A, Exley A, Goddard M, Hofker M, Hurt-Camejo E, Kanters E, Kovanen P, Lorkowski S, McPheat W, Pentikainen M, Rauterberg J, Ritchie A, Staels B, Weitkamp B, de Winther M; MAFAPS Consortium.Institute of Arteriosclerosis Research, Domagkstrasse 3, D-48149 Muenster, Germany. cullen@uni-muenster.deBy its very nature, rupture of the atherosclerotic plaque is difficult to study directly in humans. A good animal model would help us not only to understand how rupture occurs but also to design and test treatments to prevent it from happening. However, several difficulties surround existing models of plaque rupture, including the need for radical interventions to produce the rupture, lack of direct evidence of rupture per se, and absence of convincing evidence of platelet- and fibrin-rich thrombus at the rupture site. At the present time, attention should therefore focus on the processes of plaque breakdown and thrombus formation in humans, whereas the use of animal models should probably be reserved for studying the function of particular genes and for investigating isolated features of plaques, such as the relationship between cap thickness and plaque stability.

Published
2003

28. Macrophage function and stability of the atherosclerotic plaque: progress report of a European project: Macrophage Function and Stability of Atherosclerotic Plaque Consortium

Author

Bellosta, S., Bernini, F., Chinetti, G., Cignarella, A., Cullen, P., von Eckardstein, A., Exley, A., Freeth, J., Goddard, M., Hofker, M.H., Kanters, E., Kovanen, P., Lorkowski, S., Pentikainen, M., Printen, J., Rauterberg, J., Ritchie, A., Staels, B., Weitkamp, B., de Winther, M.P.J., Moleculaire Genetica, Moleculaire Celbiologie, and RS: NUTRIM School of Nutrition and Translational Research in Metabolism

Published
2002

45. Acid Soluble Calf Skin Collagen.

Author

Rauterberg, J&uum;rgen and Kühn, Klaus

Subjects
*COLLAGEN, *SOLUBILITY, *ACIDS, *SKIN, *CYANOGEN compounds, *PEPTIDES, *ION exchange (Chemistry)
Abstract

The α1-chain of acid soluble calf skin collagen was cleaved with cyanogen bromide, and the resulting peptides were separated by ion exchange and molecular sieve chromatography. Eight different peptides could he isolated as expected from the seven methionyl residues of the chain. Their size was determined by gel filtration, dodecyl sulfate disc electrophoresis, measurement of electron micrographs of renatured peptides, and amino acid analysis. Peptides, differing m length between 19 and 270 residues were found. The C-terminal peptide α1-CB6 occurred in two variants (CB6a and CB6b), differing m size, chromatographic behaviour and amino acid composition. The results suggest that CB6a contains about 15 amino acid residues more than CB6b. The amino acid compositions of the peptides were in good agreement with the composition of the α1-chain. All CNBr-peptides, including the sum of CB6a and CB6b, were isolated in approximately equimolar amounts, thus excluding the possibility of repeating sequences within the chain. The order of the CNBr-peptides was established by electron microscopy and by comparative amino acid analysis of overlapping collagenase derived peptides and uncleaved CNBr-peptides. It was found to be the same as in α1 from rat skin collagen. [ABSTRACT FROM AUTHOR]

Published
1971
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46. The C-Terminal Non-Helical Portion of the Collagen Molecule

Author

Rauterberg J

Subjects
Chemical Phenomena, Protein Conformation, Stereochemistry, Bone and Bones, Tendons, Epitopes, Structure-Activity Relationship, Species Specificity, Animals, Humans, Orthopedics and Sports Medicine, Amino Acid Sequence, Amino Acids, Peptide Synthases, Skin, Sheep, Chemistry, General Medicine, Rats, Terminal (electronics), Antibody Formation, Collagen molecule, Electrophoresis, Polyacrylamide Gel, Surgery, Collagen, Rabbits, Peptides, Chickens, Peptide Termination Factors
Published
1973
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47. Neither collagen 8A1 nor 8A2 mutations play a major role in cervical artery dissection: A mutation analysis and linkage study.

Author

Kuhlenbäumer, Gregor, Müller, Uta S., Besselmann, Michael, Rauterberg, J&uumlrgen, Robenek, Horst, Hünermund, Gert, Brandt, Tobias, Ringelstein, E. Bernd, and Stögbauer, Florian

Subjects
LETTERS to the editor, ARTERIAL surgery
Abstract

Presents a letter to the editor about the role of collagen 8A genes in the pathogenesis of spontaneous cervical artery dissection.

Published
2004
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48. Platelet-reactive sites in collagen. Collagens I and III possess different aggregatory sites

Author

Morton, L F, Fitzsimmons, C M, Rauterberg, J, and Barnes, M J

Abstract

Collagen type III possesses a highly reactive platelet-aggregatory site at a locus which in type I is essentially inactive whilst the latter collagen possesses reactive sites absent in type III. It is proposed that platelet aggregation by collagen involves the sequence GK[or R]PG(EY)GPK[or R]G(EY) or, less favourably, GPK[or R]G(EY)G(XY)GK[or R]PG(EY), one basic residue acting in combination with the second in an adjacent alpha-chain.

Published
1987
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49. Basement Membrane Components (7S Collagen, Laminin PI) Are Increased in Sera of Diabetics and Activate Platelets in vitro

Author

Högemann, B., Balleisen, L., Rauterberg, J., Voss, B., and Gerlach, U.

Abstract

Serum concentrations of two basement membrane components (7S collagen and laminin P1) were detected by specific radioimmunoassays in 70 patients suffering from diabetes mellitus type I and II with and without clinical signs of microangiopathy. Serum levels of both antigens were increased compared to controls. 7S collagen concentrations were significantly different between the diabetics with signs of microvascular damage and those without small-vessel disease (p < 0.05). Laminin P1 concentrations were also elevated, but the difference between the two groups of diabetics was not significant (p < 0.2). Raised levels of circulating basement membrane proteins may indicate connective tissue activity and development of diabetic microangiopathy. In vitro 7S collagen is a moderate platelet activator inducing platelet spreading, aggregation, and malondialdehyde production. Laminin activates platelet spreading. As a part of the altered hemostatic system the activation of basement membrane components may contribute to the development of microvascular damage.

Published
1986
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50. Interaction of biglycan with type I collagen.

Author

Schönherr, E, Witsch-Prehm, P, Harrach, B, Robenek, H, Rauterberg, J, and Kresse, H

Abstract

The small proteoglycan decorin is known to interact with type I collagen fibrils, thereby influencing the kinetics of fibril formation and the distance between adjacent collagen fibrils. The structurally related proteoglycan biglycan has been proposed not to bind to fibrillar collagens. However, when osteosarcoma cells were cultured on reconstituted type I collagen fibrils, both decorin and biglycan were retained by the matrix. Immunogold labeling at the electron microscopic level showed that both proteoglycans were distributed along collagen fibrils not only in osteosarcoma cell-populated collagen lattices but also in human skin. Reconstituted type I collagen fibrils were able to bind in vitro native and N-glycan-free biglycan as well as recombinant biglycan core protein. From Scatchard plots dissociation, constants were obtained that were higher for glycanated biglycan (8.7 x 10(-8) mol/liter) than for glycanated decorin (7 x 10(-10) mol/liter and 3 x 10(-9) mol/liter, respectively). A similar number of binding sites for either proteoglycan was calculated. Recombinant biglycan and decorin were characterized by lower dissociation constants compared with the glycanated forms. Glycanated as well as recombinant decorin competed with glycanated biglycan for collagen binding, suggesting that identical or adjacent binding sites on the fibril are used by both proteoglycans. These data suggest that, because of its trivalency, biglycan could have a special organizing function on the assembly of the extracellular matrix.

Published
1995

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