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Immunochemical Techniques, Part M: Chemotaxis and Inflammation
Volume 163: Immunochemical Techniques Part M
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Main description:FROM THE PREFACE: Chemotaxis and inflammation, like as other biological processes, can be divided into humoral and cellular components. In this simplest sense soluble activators or mediators of host or external origin interact with cells that respond to signals received and transmitted via specific membrane receptors. The biological consequences are dramatic, and the biochemical mechanisms are complex and interrelated through a series of cascades that may involve several chemical messengers of different chemical classes. Volumes 162 and 163 of Methods in Enzymology cover in Vi...
Main description:
FROM THE PREFACE: Chemotaxis and inflammation, like as other biological processes, can be divided into humoral and cellular components. In this simplest sense soluble activators or mediators of host or external origin interact with cells that respond to signals received and transmitted via specific membrane receptors. The biological consequences are dramatic, and the biochemical mechanisms are complex and interrelated through a series of cascades that may involve several chemical messengers of different chemical classes. Volumes 162 and 163 of Methods in Enzymology cover in Vitro and in Vivo methodology that has been developed for the purpose of studying the biochemistry of these active humoral factors and the biology of the cells and their receptors that respond to the various signals....The literature dealing with chemotaxis and inflammation is extensive and new techniques are constantly being developed. Therefore, some selection has been necessary to include the most commonly used and generally applicable techniques. Newer methods often involve significant modifications of established procedures, and these innovations have been included.
Review quote:
Praise for the Series
"The Methods in Enzymology series represents the gold-standard."
--NEUROSCIENCE
"Incomparably useful."
--ANALYTICAL BIOCHEMISTRY
"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page."
--BIO/TECHNOLOGY
"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection."
--CHEMISTRY IN INDUSTRY
"The appearance of another volume in that excellent series, Methods in Enzymology, is always a cause for appreciation for those who wish to successfully carry out a particular technique or prepare an enzyme or metabolic intermediate without the tiresome prospect of searching through unfamiliar literature and perhaps selecting an unproven method which is not easily reproduced."
--AMERICAN SOCIETY OF MICROBIOLOGY NEWS
"If we had some way to find the work most often consulted in the laboratory, it could well be the multi-volume series Methods in Enzymology...a great work."
--ENZYMOLOGIA
"A series that has established itself as a definitive reference for biochemists."
--JOURNAL OF CHROMATOGRAPHY
Table of contents:
Methods for the Study of the Biochemistry of Inflammation. A.P. Kaplan and M. Silverberg, Mediators of Inflammation: An Overview. M. Di Rosa, L. Sautebin, and R. Carnuccio, Phospholipase A2, Lipocortins, and Antiphospholipase Proteins. P.F. Weller, Human Eosinophil Lysophospholipase. R.L. Wykle, J.T. O'Flaherty, and M.J. Thomas, Platelet-Activating Factor. K. Fujikawa, Bovine Hageman Factor and Its Fragments. M. Silverberg and A.P. Kaplan, Human Hageman Factor and Its Fragments. G. Dooijewaard, C. Kluft, and J.J.L. van Iersel, Measurement of Contact-Activation Patterns of Human Plasma Samples with Synthetic Substrates. M. Silverberg and A.P. Kaplan, Prekallikrein. J. Spragg, Latent Kallikrein from Human Urine. R. Geiger and W. Miska, Human Tissue Kallikrein. G.S. Bailey, Rat Pancreas Kallikrein. J. Chao and L. Chao, Rat Urinary Kallikrein. T. Berg, Immunochemical Viewing of Kallikrein in Tissues. J.W. Ryan, Use of 125I- Labeled Aprotinin in the Assay of Glandular Kallikreins. C. Kluft, Synthetic Substrates for the Assay of Prekallikrein and Factor XII. M. Schapira, A. de Agostini, and R.W. Colman, C*ae1 Inhibitor: The Predominant Inhibitor of Plasma Kallikrein. J.W. Ryan, Arginine Carboxypeptidase and Its Inhibitors. J.W. Ryan, Angiotensin-Converting Enzyme, Dipeptidyl Carboxypeptidase I, and Its Inhibitors. D. Regoli and J. Barab*aae, Kinin Receptors. N. Kitamura, H. Nawa, Y. Takagaki, S. Furuto-Kato, and S. Nakanishi, Cloning of cDNAs and Genomic DNAs for High-Molecular-Weight and Low-Molecular-Weight Kininogens. W. M ller-Esterl, D.A. Johnson, G. Salvesen, and A.J. Barrett, Human Kininogens. F. Fiedler and R. Geiger, Separation of Kinins by High-Performance Liquid Chromatography. G. Drapeau and D. Regoli, Synthesis of Bradykinin Analogs. L.M. Greenbaum and H. Okamoto, T-Kinin and T-Kininogen. J. Barabe and D. Regoli, Kinin Antagonists. D.J. Loskutoff and R.R. Schleef, Plasminogen Activators and Their Inhibitors. J.H. Verheijen, Tissue-Type Plasminogen Activator and Fast-Acting Plasminogen Activator Inhibitor in Plasma. R.F. Rest, Human Neutrophil and Mast Cell Proteases Implicated in Inflammation. I.U. Schraufstatter, W.A. Halsey, Jr., P.A. Hyslop, and C.G. Cochrane, In Vitro Models for the Study of Oxidant-Induced Injury of Cells in Inflammation. A.W. Ford-Hutchinson, S. Charleson, and J.F. Evans, Leukotriene B4 Receptors on Rat and Human Neutrophil Membranes. R.J. Soberman, 5- and 15(*gu-6)-Lipoxygenases from Human Polymorphonuclear Leukocytes. R.J. Soberman and R.T. Okita, Leukotriene B4 20-Hydroxylase of Human Polymorphonuclear Leukocytes. R.J. Soberman and T. Yoshimoto, Leukotriene C4 Synthase from Rat Basophilic Leukemia Cell Microsomes. M.B. Powell and M.I. Greene, In Vivo and in Vitro Delayed Hypersensitivity. Methods for the Study of Acute-Phase Reactants. I. Kushner, The Acute Phase Response: An Overview. S.S. Macintyre, C-Reactive Protein. P. Arnaud and C. Chapuis-Cellier, *ga1-Antitrypsin. P. Arnaud, L. Miribel, and A.F. Roux, *ga1-Acid Glycoprotein. P. Arnaud, L. Miribel, and D.L. Emerson, *ga2-HS Glycoprotein. P. Arnaud, E. Gianazza, and L. Miribel, Ceruloplasmin. B.H. Bowman, D.R. Barnett, J.B. Lum, and F. Yang, Haptoglobin. G.M. Fuller, R.J. Bunzel, and J.E. Nesbitt, Fibrinogen. H. Ishibashi, K. Hayashida, and H. Okubo, *ga2-Macroglobulin. C.A. Dinarello, Endogenous Pyrogens. E.P. Benditt, N. Eriksen, and R.L. Meek, Serum Amyloid A Protein. M. Skinner and A.S. Cohen, Amyloid P Component. U. Muller-Eberhard, Hemopexin. H. Baumann, Electrophoretic Analysis of Acute-Phase Plasma Proteins. B.M.R.N.J. Woloski and G.M. Fuller, Hepatocyte-Stimulating Factor. Methods for the Study of Repair Processes in Inflammation. S.M. Wahl, Hepatic Granuloma as a Model of Inflammation and Repair: An Overview. A.K. Harris, Fibroblasts and Myofibroblasts. M. Agelli and S.M. Wahl, Collagen Production by
FROM THE PREFACE: Chemotaxis and inflammation, like as other biological processes, can be divided into humoral and cellular components. In this simplest sense soluble activators or mediators of host or external origin interact with cells that respond to signals received and transmitted via specific membrane receptors. The biological consequences are dramatic, and the biochemical mechanisms are complex and interrelated through a series of cascades that may involve several chemical messengers of different chemical classes. Volumes 162 and 163 of Methods in Enzymology cover in Vitro and in Vivo methodology that has been developed for the purpose of studying the biochemistry of these active humoral factors and the biology of the cells and their receptors that respond to the various signals....The literature dealing with chemotaxis and inflammation is extensive and new techniques are constantly being developed. Therefore, some selection has been necessary to include the most commonly used and generally applicable techniques. Newer methods often involve significant modifications of established procedures, and these innovations have been included.
Review quote:
Praise for the Series
"The Methods in Enzymology series represents the gold-standard."
--NEUROSCIENCE
"Incomparably useful."
--ANALYTICAL BIOCHEMISTRY
"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page."
--BIO/TECHNOLOGY
"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection."
--CHEMISTRY IN INDUSTRY
"The appearance of another volume in that excellent series, Methods in Enzymology, is always a cause for appreciation for those who wish to successfully carry out a particular technique or prepare an enzyme or metabolic intermediate without the tiresome prospect of searching through unfamiliar literature and perhaps selecting an unproven method which is not easily reproduced."
--AMERICAN SOCIETY OF MICROBIOLOGY NEWS
"If we had some way to find the work most often consulted in the laboratory, it could well be the multi-volume series Methods in Enzymology...a great work."
--ENZYMOLOGIA
"A series that has established itself as a definitive reference for biochemists."
--JOURNAL OF CHROMATOGRAPHY
Table of contents:
Methods for the Study of the Biochemistry of Inflammation. A.P. Kaplan and M. Silverberg, Mediators of Inflammation: An Overview. M. Di Rosa, L. Sautebin, and R. Carnuccio, Phospholipase A2, Lipocortins, and Antiphospholipase Proteins. P.F. Weller, Human Eosinophil Lysophospholipase. R.L. Wykle, J.T. O'Flaherty, and M.J. Thomas, Platelet-Activating Factor. K. Fujikawa, Bovine Hageman Factor and Its Fragments. M. Silverberg and A.P. Kaplan, Human Hageman Factor and Its Fragments. G. Dooijewaard, C. Kluft, and J.J.L. van Iersel, Measurement of Contact-Activation Patterns of Human Plasma Samples with Synthetic Substrates. M. Silverberg and A.P. Kaplan, Prekallikrein. J. Spragg, Latent Kallikrein from Human Urine. R. Geiger and W. Miska, Human Tissue Kallikrein. G.S. Bailey, Rat Pancreas Kallikrein. J. Chao and L. Chao, Rat Urinary Kallikrein. T. Berg, Immunochemical Viewing of Kallikrein in Tissues. J.W. Ryan, Use of 125I- Labeled Aprotinin in the Assay of Glandular Kallikreins. C. Kluft, Synthetic Substrates for the Assay of Prekallikrein and Factor XII. M. Schapira, A. de Agostini, and R.W. Colman, C*ae1 Inhibitor: The Predominant Inhibitor of Plasma Kallikrein. J.W. Ryan, Arginine Carboxypeptidase and Its Inhibitors. J.W. Ryan, Angiotensin-Converting Enzyme, Dipeptidyl Carboxypeptidase I, and Its Inhibitors. D. Regoli and J. Barab*aae, Kinin Receptors. N. Kitamura, H. Nawa, Y. Takagaki, S. Furuto-Kato, and S. Nakanishi, Cloning of cDNAs and Genomic DNAs for High-Molecular-Weight and Low-Molecular-Weight Kininogens. W. M ller-Esterl, D.A. Johnson, G. Salvesen, and A.J. Barrett, Human Kininogens. F. Fiedler and R. Geiger, Separation of Kinins by High-Performance Liquid Chromatography. G. Drapeau and D. Regoli, Synthesis of Bradykinin Analogs. L.M. Greenbaum and H. Okamoto, T-Kinin and T-Kininogen. J. Barabe and D. Regoli, Kinin Antagonists. D.J. Loskutoff and R.R. Schleef, Plasminogen Activators and Their Inhibitors. J.H. Verheijen, Tissue-Type Plasminogen Activator and Fast-Acting Plasminogen Activator Inhibitor in Plasma. R.F. Rest, Human Neutrophil and Mast Cell Proteases Implicated in Inflammation. I.U. Schraufstatter, W.A. Halsey, Jr., P.A. Hyslop, and C.G. Cochrane, In Vitro Models for the Study of Oxidant-Induced Injury of Cells in Inflammation. A.W. Ford-Hutchinson, S. Charleson, and J.F. Evans, Leukotriene B4 Receptors on Rat and Human Neutrophil Membranes. R.J. Soberman, 5- and 15(*gu-6)-Lipoxygenases from Human Polymorphonuclear Leukocytes. R.J. Soberman and R.T. Okita, Leukotriene B4 20-Hydroxylase of Human Polymorphonuclear Leukocytes. R.J. Soberman and T. Yoshimoto, Leukotriene C4 Synthase from Rat Basophilic Leukemia Cell Microsomes. M.B. Powell and M.I. Greene, In Vivo and in Vitro Delayed Hypersensitivity. Methods for the Study of Acute-Phase Reactants. I. Kushner, The Acute Phase Response: An Overview. S.S. Macintyre, C-Reactive Protein. P. Arnaud and C. Chapuis-Cellier, *ga1-Antitrypsin. P. Arnaud, L. Miribel, and A.F. Roux, *ga1-Acid Glycoprotein. P. Arnaud, L. Miribel, and D.L. Emerson, *ga2-HS Glycoprotein. P. Arnaud, E. Gianazza, and L. Miribel, Ceruloplasmin. B.H. Bowman, D.R. Barnett, J.B. Lum, and F. Yang, Haptoglobin. G.M. Fuller, R.J. Bunzel, and J.E. Nesbitt, Fibrinogen. H. Ishibashi, K. Hayashida, and H. Okubo, *ga2-Macroglobulin. C.A. Dinarello, Endogenous Pyrogens. E.P. Benditt, N. Eriksen, and R.L. Meek, Serum Amyloid A Protein. M. Skinner and A.S. Cohen, Amyloid P Component. U. Muller-Eberhard, Hemopexin. H. Baumann, Electrophoretic Analysis of Acute-Phase Plasma Proteins. B.M.R.N.J. Woloski and G.M. Fuller, Hepatocyte-Stimulating Factor. Methods for the Study of Repair Processes in Inflammation. S.M. Wahl, Hepatic Granuloma as a Model of Inflammation and Repair: An Overview. A.K. Harris, Fibroblasts and Myofibroblasts. M. Agelli and S.M. Wahl, Collagen Production by