Acute Phase Proteins in the Acute Phase Response

Buch | Softcover

210 Seiten

2012 | Softcover reprint of the original 1st ed. 1989
Springer London Ltd (Verlag)
978-1-4471-1741-4 (ISBN)

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The discovery of C-reactive protein in the laboratory of O. T. Avery at Rockefeller University in 1929-30 was the first specific obser- vation of the acute phase plasma protein response (Tillett and Francis 1930). This was one of three contributions of fundamental importance which emerged from that laboratory, the other two being the recognition that polysaccharides could act as antigens and that DNA transmits genetic information. In the course of charac- terization of pneumococcal carbohydrate antigens, a somatic poly- saccharide common to all Rand S forms of pneumococci was identified and designated Fraction "C" (Tillet et al. 1930). Testing of sera from patients with pneumococcal infection revealed the presence of material which precipitated with the C-polysaccharide but which differed from antibody in that calcium was required for the reaction. Furthermore, the amount of reactive material was greatest when patients were acutely ill and decreased in the convalescent phase, the precise opposite of specific anti-pneumo- coccal antibodies.
Subsequently, the C-reactive material was shown to be a protein and to be present in the sera of individuals who were acutely ill with other, non-pneumococcal infections and tissue damaging conditions, hence Avery coined the term "acute phase" and called the protein "acute phase protein" (Abernethy and Avery 1941; MacLeod and Avery 1941). At that time methods were too insensitive to detect C-reative protein (CRP) in sera of healthy subjects and it was considered to be a pathological product.

1 Interleukin-1 in the Acute Phase Response.- The Acute Phase Response.- Structure of IL-1.- Synthesis and Regulation of IL-1.- IL-1 Receptor.- Pleotropic Actions of IL-1.- IL-1 and Acute Phase Reactions.- IL-1 and Other Cytokines.- In Vivo Action of IL-1.- Summary.- 2 Regulation of Human SAA Gene Expression by Cytokines.- In Vitro Expression of Human SAA.- Cis-acting Sequences Responsible for PMA Induction of SAA.- Cytokine Control of SAA Expression.- 3 Transcriptional Regulation of Acute Phase Response Genes with Emphasis on the Human C-reactive Protein Gene.- The Physiological Role of the Acute Phase Response.- Systems for the Study of the Acute Phase Response.- Monokines Responsible for the Modulation of Liver-specific Gene Expression.- Transcriptional Regulation — the Mechanism.- Conclusions and Perspectives.- 4 Organization, Structure and Expression of Pentraxin Genes.- The Structure of Pentraxin Proteins.- The Structure of Pentraxin Genes.- Elements Responding to Cytokines.- Genetics.- 5 ApoSSA: Structure, Tissue Expression and Possible Functions.- SAA is an Apolipoprotein.- Where are SAAs Made and Where do They go?.- 6 Regulation of Biosynthesis and Secretion of Human C-reactive Protein and Serum Amyloid A.- Regulation of Biosynthesis.- Heterogeneity in the Acute Phase Response.- Regulation of CRP Secretion.- CRP is Specifically Retained Within the Endoplasmic Reticulum.- Conclusions.- 7 Molecular Regulation of the Acute Phase Complement Proteins.- Factor B.- The Second Component, C2.- Constitutive Expression of Factor B and C2.- Regulated Gene Expression.- Interleukin-1 and Interferon-?.- Tumor Necrosis Factor and Interleukin-6.- Summary.- 8 Biosynthesis of Acute Phase Proteins by the Liver Cells.- Role of Hepatocytes in the In Vivo Biosynthesis of APR.-Role of Sinusoidal Cells in the In Vivo Biosynthesis of APR.- Summary.- 9 The Plasma Serine Protease Inhibitors (Serpins): Structural Modifications in Inflammation.- The Serpins.- Antitrypsin.- The Reactive Centre.- The SR Conformational Change.- Other Structural Modifications in Inflammation.- Conclusions.- 10 The Three Dimensional Structure of SAP.- 11 Structure, Metabolism and Function of Acute Phase High Density Lipoprotein.- Apo-SAA in Plasma.- Structure of Apo-SAA.- Structure of Acute Phase HDL.- Metabolic Function of Normal HDL.- Synthesis of Apo-SAA.- Plasma Clearance of Apo-SAA.- Cellular Association and Degradation of Apo-SAA.- Functions of Apo-SAA.- Concluding Remarks.- 12 Clinical Measurement of Acute Phase Proteins to Detect and Monitor Infectious Diseases.- Microbial Growth and AP Protein Response.- Monitoring Disease Activity Using AP Protein Response.- Immunomodulation and AP Protein Response.- 13 C-reactive Protein: Clinical Aspects.- The Acute Phase Proteins.- The Erythrocyte Sedimentation Rate as an Indirect Indicator for the Acute Phase Reaction.- C-reactive Protein as a Direct Indicator of the Acute Phase Reaction.- Conclusion.- 14 Pathogenesis of AA Amyloidosis.- Definition and Classification of Amyloidosis.- Serum and Tissue Amyloid A Proteins.- Structure of SAA and AA.- Formation and Deposition of AA Amyloid.- Summary of Some Current Hypotheses Regarding AA Amyloid Formation.- 15 Serum Amyloid P Component: A Specific Molecular Targeting Vehicle in Amyloidosis.- Serum Amyloid P Component.- SAP and Amyloidosis.- Scintigraphic Imaging of Amyloid Deposits In Vivo.- Radiolabeled SAP Studies in Man.- Conclusions.

Reihe/Serie	Argenteuil Symposia
Zusatzinfo	XVIII, 210 p.
Verlagsort	England
Sprache	englisch
Maße	170 x 242 mm
Themenwelt	Sachbuch/Ratgeber ► Gesundheit / Leben / Psychologie ► Lebenshilfe / Lebensführung
	Medizin / Pharmazie ► Medizinische Fachgebiete ► Dermatologie
	Studium ► 2. Studienabschnitt (Klinik) ► Humangenetik
	Studium ► 2. Studienabschnitt (Klinik) ► Pathologie
	Studium ► Querschnittsbereiche ► Infektiologie / Immunologie
	Naturwissenschaften ► Biologie ► Biochemie
	Naturwissenschaften ► Biologie ► Genetik / Molekularbiologie
ISBN-10	1-4471-1741-7 / 1447117417
ISBN-13	978-1-4471-1741-4 / 9781447117414
Zustand	Neuware