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Proteases in Physiology and Pathology / edited by Sajal Chakraborti, Naranjan S. Dhalla.

SpringerLink Books Biomedical and Life Sciences 2017 Available online

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Format:
Book
Contributor:
Chakraborti, Sajal, editor.
Dhalla, Naranjan S., editor.
SpringerLink (Online service)
Language:
English
Subjects (All):
Medicine.
Cancer--Research.
Cancer.
Human physiology.
Molecular biology.
Pharmaceutical technology.
Biomedicine.
Local Subjects:
Biomedicine.
Physical Description:
1 online resource
Contained In:
Springer eBooks
Place of Publication:
Singapore : Springer Singapore : Imprint: Springer, 2017.
System Details:
text file PDF
Summary:
Using a multidisciplinary approach, this book describes the biochemical mechanisms associated with dysregulation of proteases and the resulting pathophysiological consequences. It highlights the role and regulation of different types of proteases as well as their synthetic and endogenous inhibitors. The role of proteases was initially thought to be limited to general metabolic digestion. However, we now know that the role of protein breakdown is much more complex, and proteases have multiple functions: they are coupled to turnover and can affect protein composition, function and synthesis. In addition to eliminating abnormal proteins, breakdown has many modulatory functions, including activating and inactivating enzymes, modulating membrane function, altering receptor channel properties, affecting transcription and cell cycles and forming active peptides. The ubiquity of proteases in nature makes them an important target for drug development. This in-depth, comprehensive is a valuable resource for researchers involved in identifying new targets for drug development. With its multidisciplinary scope, it bridges the gap between fundamental and translational research in the biomedical and pharmaceutical industries, making it thought-provoking reading for scientists in the field.
Contents:
Physiological and Pathological Functions of Mitochondrial Proteases
The Role of MMP2 and 9 in Embryonic Neural Crest Cells and their Derivatives
The matrix metalloproteinase and tissue inhibitors of metalloproteinase balance in physiologicaland pathological remodeling of skeletal muscles
Role of BMP1/ tolloid like proteases in bone morphogenesis and tissue remodeling
Role of proteases in the regulation of N-myristoyltransferase
Role of Tissue Factor-FVIIa Blood Coagulation Initiation complex in Cancer
Metalloproteases in adaptive cell responses
Proteases from protozoa and their role in infection.-Regulation of Extracellular Matrix Remodeling and Epithelial-Mesenchymal Transition by Matrix Metalloproteinases: Decisive Candidates in Tumor Progression.- Proteases and Protease Inhibitors in Male Reproduction
Physiological and Pathological Functions of Cysteine Cathepsins
Role of serine proteases and inhibitors in cancer
Role of Proteases in diabetes and diabetic complications.- Plant Latex Proteases: Natural Wound Healers
Emerging Role of Mitochondrial Serine Protease HtrA2 in Neurodegeneration
Functional Relevance of Deubiquitinases in Life and Disease
Sub-Mitochondrial Calpains in Pathophysiological Consequences.- Serine Proteases in the Lectin Pathway of the Complement System.- Pups, SAMPs and Prokaryotic Proteasomes.- Role of Proteases in Photoaging of Skin.- Insect proteases: Structural-functional outlook.- Protease-antiprotease interactions: an overview of the process from an in silico perspective
Snake venom proteases as toxins and tools.- The world of the proteases across micros, insects and medicinal trees.- Insight into the mode of interactions between bacterial proteases and their substrates.- The Ubiquitin Proteasome System with itsChecks and Balances.- A brief account of structure function relationship of the traditional cysteine protease inhibitor-cystatin with a special focus on human family 1 and 2 cystatins.- Solid Support Synthesis of a Dnp-labeled Peptide for Assay of Matrix Metalloproteinase-2.
Other Format:
Printed edition:
ISBN:
9789811025136
Access Restriction:
Restricted for use by site license.

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