Fibrinogen. Proceedings/ Workshop on Fibrinogen. / Vol. 3, : Structural variants and interactions ; Stockholm, Sweden, July 9–10, 1983 / / hrsg. von A. Henschen.

• Superior document: Title is part of eBook package: De Gruyter DGBA Medicine and Life Sciences - <1990
• MitwirkendeR: Agam, G.,; Amrani, H. L.,; Armstrong, D. J.,; Assouline, Z.,; Baba, M.,; Balconi, G.,; Belew, M.,; Bertina, R. M.,; Blohn, G. von,; Blombäck, B.,; Caen, J.,; Carrell, N.,; Chang, G.,; Comeau, C. M.,; Courtois, G.,; Crabtree, G. R.,; Dauden, V. M.,; Deguchi, K.,; Dejana, E.,; Dunn, F.,; Eisenhut, M.,; Fasold, H.,; Fowlkes, D. M.,; Francis, J. L.,; Galanakis, D. K.,; Godal, H. C.,; Gollwitzer, R.,; Graeff, H.,; Haber, E.,; Hafter, R.,; Harenberg, J.,; Haverkate, F.,; Hawiger, J.,; Hellstern, P.,; Hensc, A.,; Henschen, A.,; Hermann, H. -J.,; Heymann, E.,; Hoegee-de Nobel, B.,; Holm, B.,; Homandberg, G. A.,; Hugo, R. von,; Hui, K. Y.,; Ireland, H.,; Jelenska, M.,; Kahn, A.,; Kaiser, C.,; Kaminski, M.,; Klaubert, W.,; Kloczewiak, M.,; Kluft, C.,; Koopman, J.,; Kopec, M.,; Lane, D. A.,; Languino, L. R.,; Lijnen, R.,; Livne, A.,; Lukas, T. J.,; Luria, R.,; Mannucci, P. M.,; Marguerie, G.,; Matsuda, M.,; Matsueda, G. R.,; McDonagh, J.,; Mentlein, R.,; Mihalyi, E.,; Mirshahi, M.,; Miyashita, C.,; Morimoto, K.,; Mosesson, M. W.,; Mullis, N. T.,; Müller-Berghaus, G.,; Nakamikawa, C.,; Nieuwenhuizen, W.,; Ohlsson, K.,; Peerschke, E. I. B.,; Preissner, K. T.,; Rochowska, M.,; Rotker, J.,; Saldeen, K.,; Saldeen, T.,; Samama, M.,; Schwamborn, J.,; Selmayr, E.,; Seydewitz, H. H.,; Shainoff, J. R.,; Shoshani, L.,; Simmonds, V. J.,; Skurzak, H.,; Soria, C.,; Soria, J.,; Southan, C.,; Stehle, G.,; Struckhoff, G.,; Tanaka, K.,; Thompson, E.,; Timmons, S.,; Traas, D. W.,; Traas, D.,; Uzan, G.,; Verheijen, J. H.,; Verheijen, J.,; Voskuilen, M.,; Vries, J. X. de,; Waibel, S.,; Wallin, R.,; Watanabe, K.,; Watson, N. J.,; Wenzel, E.,; Witt, I.,; d’Angelo, A.,
• HerausgeberIn: Henschen, A.,
• Place / Publishing House: Berlin ;, Boston : : De Gruyter, , [2019]; ©1985
• Year of Publication: 2019
• Edition: Reprint 2019
• Language: German
• Series: Fibrinogen. Proceedings/ Workshop on Fibrinogen ; Vol. 3
• Physical Description: 1 online resource (418 p.) :; Num. figs.

Table of Contents

• Frontmatter
• Preface
• Contents
• I. A HISTORICAL NOTE
• Two thousand years of fibrinogen research and evidence for fibrin being the first protein
• II. GENE ANALYSIS
• Fibrinogen evolution - The structure and evolution of fibrinogen: The coiled coil region
• Absence of gross defect of fibrinogen genes in one patient with congenital afibrinogenemia
• III. FIBRINOGEN-FIBRIN CONVERSION
• Fibrinogen to fibrin - an overview
• Fibrin - specific monoclonal antibodies are elicited by immunization with a synthetic fibrin-like peptide
• Enhancement of fibrin polymerization by active site - inhibited thrombin
• Peptides released from human fibrinogen by thrombic enzymes
• The analysis of fibrinopeptide release from S--carboxymethylated fibrinogen chains using high-performance liquid chromatography
• Moaification of the fibrin a-chain by dipeptidyl peptidase IV
• IV. FIBRINOGEN-FIBRIN INTERACTION
• Analysis of composition of soluble fibrinogen/fibrin complexes by differential ultracentrifugation
• Reversible interactions of fibrin and fibrinogen: an ultracentrifugation study
• V. NORMAL FIBRINOGEN VARIANTS
• Evidence that the amount of heparin precipitable fraction is influenced by fibrinogen quality
• The location of a second in vivo phosphorylation site in the Aa-chain of human fibrinogen
• Evidence that the y chain population of human platelet fibrinogen lacks the y' variant that is present in plasma fibrinogen
• Differences and similarities between human adult and fetal fibrinogen fragments D1
• VI. ABNORMAL FIBRINOGEN VARIANTS
• Functional defects in abnormal fibrinogens
• Study of 10 cases of congenital dysfibrinogenemia: clinical and molecular biological aspects
• Fibrinogens Sydney I and II, a kinetic study of (His16 )FPA cleavage and its effect on FPB cleavage
• Fibrinogens London I - IV, Manchester, Sydney I and II. Cleavage of fibrinopeptides by thrombin and expression of their polymerisation abnormalities
• Aspects of evaluation of fibrinogen Stony Brook - A defect resulting in failure to release fibrinopeptide A
• Fibrinogen Tokyo II: An abnormal fibrinogen with an impaired polymerization site on the aligned DD domain of fibrin molecules
• Fibrinogen Milan II: A congenital dysfibrinogenemia with a defective clotting by thrombin, normal clotting by arvin, reptilase and prothrombin-staphy1ocoagulase complex, associated with thrombotic episodes
• Preliminary report concerning two new cases of congenital dysfibrinogenemia (Homburg II and Homburg III)
• The effect of sodium citrate on fibrin polymerisation in patients with liver disease
• VII. FIBRINOGEN DEGRADATION PRODUCTS
• Studies of the proteolytic fragments of the C-terminal portion of the a-chain of human fibrinogen
• Biodistribution or human fibrinogen-derived peptides in rabbits
• Structure-function studies on a vasoactive pentapeptide derived from plasm in degradation of human fibrin(ogen)
• Purification and characteristics of a vasoactive peptide derived from elastase degradation of human fibrin(ogen)
• Relation of crosslinked to non crosslinked fibrin derivatives in tumor ascites compared to cirrhosis ascites
• VIII. INTERACTION WITH PLASMINOGEN AND ITS ACTIVATOR
• Study of the interaction between plasminogen and fibrinogen degradation products using immunoenzymological assay
• Fibrin and plasminogen structures involved in the tissue-type plasminogen activator catalyzed activation of plasminogen
• Kinetics of the tissue-type plasminogen activatormediated activation of plasminogen. Influence of CNBr fibrin(ogen) fragment FCB-2 and different forms of plasminogen
• IX. INTERACTION WITH CELLS
• Structural characterization of the recognition site for platelet receptors on human fibrinogen
• Binding or fibrinogen to ADP-treated platelets: Importance of the Aα-chain
• Inhibition of fibrinogen binding to activated platelets by oligoamines
• Specific interaction between fibrinogen-fibrin and endothelial cells
• Influence of fibrin, fibrinogen and fibrinogen degradation products on cultured endothelial cells
• Interaction of fibrin with malignant melanoma cells in long term culture
• AUTHOR INDEX
• SUBJECT INDEX
• Backmatter