Lactoferrin : interactions and biological functions
著者
書誌事項
Lactoferrin : interactions and biological functions
（Experimental biology and medicine, 28）
Humana Press, c1997
- : alk. paper
大学図書館所蔵 全4件
注記
Based on the Second International Symposium on Lactoferrin: Interactions and Biological Functions, held in Honolulu, Hawaii, 1995
Includes bibliographical references and index
内容説明・目次
内容説明
The number of investigators focusing their attention on lactoferrin has increased dramatically in recent years. Lactoferrin is a protein with more than one known structure and a number of proposed biological functions, including several with important regulatory consequences. In many ways it has been an easy pro tein to investigate; however, there have been difficulties under standing specific structure / function relationships, particularly as it functions in vivo. Research funding dedicated to this protein has previously been limited, but is now increasing. As lactoferrin begins to emerge formally as a protein of significance to the medi and industry, it is more important than ever to coor cal profession dinate and integrate research efforts whenever possible and to share the results of these efforts within the expanding array of medical and scientific diSciplines involved. It was our intention to provide a forum to summarize and disseminate the most recent advances in this field. Included in Lactoferrin: Interactions and Biological Functions are selected presentations representing the many disciplines involved in defining lactoferrin function in terms of its known structural features, including its carbohydrate side-chains, receptor binding sites, its capacity to bind different metal ions, and other newly discovered bioactive domains. Several of the possible physiologi cal functions of lactoferrin are described and summarized in detail, including the role of laetoferrin in bacterial killing, its in volvement in cell growth and proliferation, in the modulation of immune function, and in iron absorption.
目次
Part I: Lactoferrin Structure and Function. Lactoferrin Structure-Function Relationships: An Overview, Jeremy H. Brock. Altered Domain Closure and Iron Binding in Lactoferrin Mutants, H. Rick Faber, Bryan F. Anderson, Heather M. Baker, Tony Bland, Catherine L. Day, Hale Nicholson, Steven Shewry, John W. Tweedie, and Edward N. Baker. Affinity Mass Spectrometry: Probes with Surfaces Enhanced for Affinity Capture (SEAC) of Lactoferrin, Tai-Tung Yip and T. William Hutchens. Part II: Lactoferrin Gene Expression. Variants and Biotechnological Use of the Bovine Lactoferrin-Encoding Gene, Hans-Martin Seyfert, Uta Klussmann, Uta Maria Steinhoff, Jens Vanselow, Dirk Koczan, and Gerd Hobom. Posttranscriptional Regulation of Bovine and Human Lactoferrin: Species Differences and Influence of mRNA Regions, Floyd L. Schanbacher, Surapon Pattanajitvilai, and Margaret C. Neville. Mutagenesis of Human Lactoferrin and Expression in Baby Hamster Kidney Cells, John W. Tweedie, Edward N. Baker, Catherine L. Day, Bhavwanti Sheth, and H. Hale Nicholson. Structural Determination of Two N-Linked Glycans Isolated from Recombinant Human Lactoferrin Expressed in BHK Cells, Dominique Legrand, Valerie Salmon, Bernadette Coddeville, Monique Benaissa,Yves Plancke, and Genevieve Spik. Distribution of the Iron-Binding Protein Lactoferrin in the Pathological Lesions of Neurodegenerative Diseases, Beatrice Leveugle, Genevieve Spik, Daniel P. Perl, Constantin Bouras, Howard M. Fillit, and Patrick R. Hof. Lactoferrin Almost Absent from Lactating Rat Mammary Gland Is Replaced by Transferrin, Annick Pierce, Hector Escriva, Bernadette Coddeville, Monique Benaissa, Didier Leger, Genevieve Spik, and Mercedes Pamblanco. Estrogen Regulation of Human Lactoferrin Gene Activity: Transcriptional Synergism Between Estrogen Receptorand Related Orphan Receptor, Christina T. Teng and Nengyu Yang. Expression and Functional Analysis of Recombinant Human Lactoferrin, Pauline P. Ward, Christopher S. Piddington,Grainne Cunningham, Xiaodong Zhou, Roger D. Wyatt, and Orla M. Conneely. Structural and Functional Flexibility of Lactoferrin, Edward N. Baker, Bryan F. Anderson, Heather M. Baker, Rick Faber, Clyde A. Smith, and Andrew J. Sutherland-Smith. Difference in Binding and Fate of Lactotransferrin in Jurkat Human Lymphoblastic T-Cells and in T-47D Human Breast Cancer Cells, Bao Yuan Bi, Elisabeth Elass, Dominique Legrand, Florence Deplace, Genevieve Spik, and Joel Mazurier. The Impact of Phagocyte-Lactoferrin Interactions on Inflammation, Bradley E. Britigan, Troy S. Lewis, Oyebode Olakanmi, Michael L. McCormick, and Rachel A. Miller. Regulation of Lymphocyte Proliferation by Lactoferrin, Jeremy H. Brock and Abdelhakim Djeha. Recombinant Human Lactoferrin and Its Variants: Receptor Binding in Human Intestinal Brush-Border Membranes, Suhasini Iyer, Bo Loennerdal, Catharine Day, Edward N. Baker, John Tweedie, Tai-Tung Yip, and T. William Hutchens. Part III: Functions Related to Lactoferrin Interactions with Prokaryotic and Eukaryotic Cells. Influence of Lactoferrin on Host-Microbe Interactions, Satyanarayan Naidu and Roland R. Arnold. Bacterial Lactoferrin Receptors in the Neisseriaceae, Robert A. Bonnah, Rong-hua Yu, and Anthony B. Schryvers. Bacteriostatic Effects of Orally Administered Bovine Lactoferrin on Intestinal Bacteria in the Gut of Mice Fed Bovine Milk, Susumu Teraguchi, Kouichirou Shin, Kazuhiro Ozawa, Satoko Nakamura, Yasuo Fukuwatari, Seiichi Shimamura, and Mamoru Tomita. Functional Significance of the Binding of Lactoferrin to DNA, Philip Furmanski, Jianglin He, Li Ying, Joann Bezault, Ramesh Bhimani, and Kinfan Ho. Specific Binding of Ferrilactoferrin and Ferritransferrin in the Protozoan Leishmania chagasi, Michael L. McCormick, Mary E. Wilson, Troy S. Lewis, Robert W. Vorhies, and Bradley E. Britigan. Part IV: Lactoferrin Metabolism. Observations on the Metabolism and Cellular Interactions of Lactoferrin, Erwin Regoeczi. Lactoferrin as a Possible
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