Eicosanoids, Apolipoproteins, Lipoprotein Particles, and Atherosclerosis

Herausgegeben:Malmendier, Claude L.; Alaupovic, Petar

• Broschiertes Buch

Produktbeschreibung

Plasma lipoproteins constitute a unique macromolecular system of lipid-protein complexes responsible for the transport of lipids from their sites of origin to their sites of utilization either as metabolic fuel or as structural components of cell membranes. Although studies on the role of lipoproteins in the mechanism of lipid transport are meritorious in their own right, the ever-increasing interest in chemical and functional properties of this remarkable class of conjugated proteins stems from the impressive evidence of their direct involvement in the genesis and develop ment of atherosclerotic lesions. The initial emphasis on neutral lipids and phospholipids as the most characteristic constituents of operationally defined lipoprotein classes has shifted in recent years to their protein moieties or apolipoproteins. The discovery of a number of apolipoproteins and characterization of familial hypolipoproteinemias as apolipoprotein deficiency disorders indicated that apolipoproteins play an essential role in maintaining the structural stability and integrity of lipoprotein particles. In addition to their role in the formation of lipoproteins, apolipoproteins were shown to perform a variety of functions in metabolic conversion of lipoproteins and their interactions with cellular surfaces. Results from several laboratories have demonstrated that the chemical and metabolic heterogeneity of operationally-defined lipoprotein classes is due to the presence of several discrete lipoprotein particles with similar physical properties but different and characteristic apolipoprotein composition. Thus, the apolipoproteins have emerged not only as essential structural and functional constituents of lipoproteins but also as unique chemical markers for identifying and classifyinglipoprotein particles.

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Produktdetails

• Advances in Experimental Medicine and Biology 243
• Verlag: Springer / Springer US / Springer, Berlin
• Artikelnr. des Verlages: 978-1-4612-8055-2
• 1988
• Seitenzahl: 376
• Erscheinungstermin: 18. Oktober 2011
• Englisch
• Abmessung: 244mm x 170mm x 21mm
• Gewicht: 648g
• ISBN-13: 9781461280552
• ISBN-10: 1461280559
• Artikelnr.: 39677523

Inhaltsangabe

Eicosanoids.- Prostacyclin, EDRF and Atherosclerosis.- Control of Prostacyclin Production by Vascular Cells: Role of Adenine Nucleotides and Serotonin.- Prostacyclin and Atherosclerosis - Experimental and Clinical Approaches.- Platelet-Neutrophil Interactions in the Eicosanoid Pathway.- Arterial Cell Interactions: Mechanistic Studies Related to Eicosanoid and Growth Factor-Induced Alterations in Cholesterol Metabolism.- Effects of Plasma Lipoproteins on Eicosanoid Metabolism by Cultured Vascular Smooth Muscle Cells.- Eicosanoid Synthesis in Platelet-Derived Growth Factor-Stimulated Fibroblasts.- Genetics of Apolipoproteins.- Genetic HDL Deficiency States.- Apolipoprotein A-I: Deficiency in Tangier Disease.- Apolipoprotein C-II Deficiencies: In Vivo Models for Assessing the Significance of Defective Lipolysis on Lipoprotein Metabolism 7.- Genetic Variation in the Apolipoproteins C-II and C - III.- The Effect of Apolipoprotein E Allele Substitutions on Plasma Lipid and Apolipoprotein Levels.- Molecular Genetics of Coronary Heart Disease.- STRUCTURE OF APOLIPOPROTEINS AND LIPOPROTEINS.- Molecular Biology of Human Apolipoprotein B and Related Diseases.- Secondary and Tertiary Structure of Apolipoproteins.- Prediction of the Tertiary Structure of Apolipoprotein A-II by Computer Modeling.- Relationship between Structure and Metabolism of HDL Apolipoproteins: Study with Synthetic Peptides.- Heterogeneity in the Conformation of Apo A-I on the Surface of HDL Particles.- Structural Properties of the Heparin-Binding Domains of Human Apolipoprotein E.- Characterization and Metabolism of Glycated High Density Lipoproteins in Diabetic Patients.- Control of Spontaneous Lipid and Protein Transport.- Modifications in the Chemical Composition and Thermometric Behavior of LDL and HDLby Probucol in Type Ila Hyperlipoproteinemia.- Acute Phase Apolipoproteins.- Serum Amyloid A (SAA) - The Precursor of Protein AA in Secondary Amyloidosis.- Modulation of Serum Amyloid A Gene Expression by Cytokines and Bacterial Cell Wall Components.- Protein S and SAA : Genetics, Structure and Metabolism. Are They Apolipoproteins and Identical?.- LIPID TRANSFER PROTEINS.- Plasma Cholesteryl Ester and Phospholipid Transfer Proteins and Their Regulation.- The Human Plasma Cholesteryl Ester Transfer Protein: Structure, Function and Physiology.- Cholesterol Ester Transfer Protein. Characterization of Monoclonal Antibodies against the Human Antigen.- Cholesterol Esterification and Net Mass Transfer of Cholesterylesters and Triglycerides in Plasma from Healthy Subjects and Hyperlipidemic Coronary Heart Disease Patients.- Lecithin: Cholesterol Acyltransferase and Its Action on Different Substrates.- In Vivo Evidence for Cholesterol Ester and Triglyceride Exchange between High Density Lipoprotein and Infused Triglyceride Rich Particles in Abetalipoproteinemia 2.- Enhanced Cholesteryl Ester Transfer Activity in Cyclophosphamide-Treated Rabbits: Relationship with Lipolytic Enzymes.- Role of Apolipoprotein A IV in the Interconversion of HDL Subclasses.- LIPOPROTEIN PARTICLES.- HDL Receptor and Reverse Cholesterol Transport in Adipose Cells.- Molecular Analysis of Atherogenic Lipoprotein Particles in Adequately Controlled Type I Diabetes Mellitus.- Quantitative Abnormalities of Lipoprotein Particles in Chronic Hemodialysis Patients....283.- HYPERTRIGLYCERIDEMIA.- Lipoprotein Particles in Hypertriglyceridemic States.- In Vivo Metabolism of Apolipoproteins C-II and C-III in Normal and Hypertriglyceridemic Sub jects.- Pathogenesis of Hypertriglyceridemia: Implications forCoronary Heart Disease and Therapy.- Increased VLDL.- Exchange and Transfer of Apolipoproteins and Lipids: Impact on Lipoprotein Metabolism.- Hypertriglyceridemia and Omega-3 Fatty Acids.- Contributors.