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Aspartic proteinases: physiology and pathology hardback Routledge Revivals Series

Langue : Anglais

Auteurs :

Couverture de l’ouvrage Aspartic proteinases: physiology and pathology hardback
In this text the advantages and limitations of using aspartic proteinases in human pathology are examined. Topics covered include: physiologic functions of digestive enzymes, participation in patho-physiology of malaria, renin blood pressure control, and cathepsin D in breast cancer development.
INTRODUCTION. ASPARTIC PROTEINASES-AN OVERVIEW. Aspartic Proteinases. Family of Aspartic Proteinases-Characteristic Properties. Evolution of Aspartic Proteinases-Their Primary, Secondary, and Tertiary Structures. Catalytic Mechanism of Aspartic Proteinases. Specificity of the Proteinase Action. Inhibition of Aspartic Proteinases. Propeptides of Aspartic Proteinases and Activation of Zymogens. Concluding Remarks. PEPSIN A AND GASTRICSIN AND THEIR ZYMOGENS. Introduction. Nomenclature. Localization of Pepsin A and Gastricsin and Their Physiological Role. Localization of Pepsinogen A and Progastricsin in the Human Body. Intracellular Synthesis of Pepsinogen A and Progastricsin. Secretion of Pepsinogen A and Progastricsin. Activation of Zymogens. Age Dependent Changes in Gastric Enzyme. Seminal Progastricsin. Sequence and Expression. Sequences-Pepsinogen A and Progastricsin. Polymorphism of Pepsinogen A and Progastricsin. Three-Dimensional Structure. Overall Shape-Pepsinogen A. Phosphoserine 68. Active Site. Comparison of Pepsin and Pepsinogen Structures. Proteolytic Activity. Pepsin A and Gastricsin and Patho-Physiological Conditions. Determination of Serum Pepsinogen and Gastricsin. Normal Levels. Serum Pepsinogen A and Progastricsin and Patho-Physiological States. Concluding Remarks. RENIN. Introduction. Localization, Secretion, and Physiological Function of Renin. Localization of Renin and Prorenin. Mammalian Secretory Pathways and Regulation of Renin Secretion. The Proteolytic Cleavage of Angiotensinogen-Basic Physiological Function of Renin. Sequence and Posttranslational Modifications. Gene Structure. Primary Structure. The Posttranslational Modifications. Three-Dimensional Structure. Overall Shape. Active Site. Specificity of Renin Catalysis. The Clinical Potential of Renin Inhibition. Introduction. Renin Specific Antibodies. Synthetic Renin Inhibitors. Pharmacology of Renin Inhibition. Concluding Remarks. CATHEPSIN D. Introduction. Physiological Functions. Intracellular Catabolism. Processing of Antigens and Peptide Hormones. Tissue Remodeling. Sequence and Regulation of Expression. Sequence of Cathepsin D. Regulation of the Expression. Cellular Targeting, Processing and Localization of Cathepsin D. Targeting of Cathepsin D to the Lysosomes. Posttranslational Modifications of Cathepsin D. Localization of Cathepsin D. Three-Dimensional Structure. Overall Shape, Processed Loop. Targeting, Recognition Signal. The Active Site. Catalytic Properties. Characterization of Subsite Preferences. Patho-Physiological Involvement of Cathepsin D. Involvement of Cathepsin D in Neurodegenerative Diseases. Involvement of Cathepsin D in Neoplastic Diseases. Conclusions. CATHEPSIN E. Introduction. Localization of Cathepsin E. Subcellular Localization of Cathepsin E. Physiologic Function. Primary Structure of Cathepsin E and its Molecular Forms. Catalytic Properties of Cathepsin E. Cathepsin E and Gastric Cancers. Concluding Remarks. ASPARTIC PROTEINASES OF CANDIDA YEASTS. Introduction. Candida Yeasts: An Opportunistic Pathogen. The Aspartic Proteinase: Virulence Factor of Candidal Infections. The Biochemistry of Candida Aspartic Proteinases. Conditions for Proteinase Secretion-Induction by Substrate and pH. Complex Genetic of Candida Aspartic Proteinases and Their Primary Structures. Three-Dimensional Structures of Candida Aspartic Proteinases. Specificity of Proteinases and Inhibitor Design. Concluding Remarks. ASPARTIC PROTEINASE OF PLASMODIUM FALCIPARUM. Introduction. The Life-Cycle of Plasmodium falciparum Parasite. The Production of Aspartic Proteinase. Sequence of Plasmodium Aspartic Proteinases. Specificity of the Proteinases an
Pharmacologists, immunologists, crystallographers, analytical biochemists, cell biologists, physiologists

Martin Fusek, Ph.D. is a member of the Department of Biochemistry of the Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences in Prague, Czech Republic.

Vaclac Vetvicka, Ph.D. is an Assistant Professor at the Department of Pathology, Division of Experimental Immunology and Immunopathology of the School of Medicine, University of Lousiville, Louisville, Kentucky.

Date de parution :

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Date de parution :

15.6x23.4 cm

Disponible chez l'éditeur (délai d'approvisionnement : 12 jours).

Prix indicatif 222,92 €

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