Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. This volume in the Methods in Enzymology series comprehensively covers this topic. With an international board of authors, this volume covers subjects such as Crystallography of serpins and serpin complexes, Serpins as hormone transporters, and Production of serpins using cell free systems. This volume in the Methods in Enzymology series comprehensively covers the topic of serpins With an international board of authors, this volume covers subjects such as Crystallography of serpins and serpin complexes, Serpins as hormone transporters, and Production of serpins using cell free systems
Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. This volume in the Methods in Enzymology series comprehensively covers this topic. With an international board of authors, this volume covers subjects such as Crystallography of serpins and serpin complexes, Serpins as hormone transporters, and Production of serpins using cell free systems. This volume in the Methods in Enzymology series comprehensively covers the topic of serpins With an international board of authors, this volume covers subjects such as Crystallography of serpins and serpin complexes, Serpins as hormone transporters, and Production of serpins using cell free systems
The serpins constitute a superfamily of proteins that fold into a conserved tertiary structure and employ a sophisticated, irreversible suicide-mechanism of inhibition. More than 6000 serpins have been identified, occurring in all three forms of the life - the eukaryotes, the prokaryotes and the archea. Vertebrate serpins can be conveniently classified into six groups (V1 - V6), based on three independent biological features - gene organization, diagnostic amino acid sites and rare indels. In the present work, the phylogenetic relationships of serpins from Nematostella vectensis, Strongylocentrotus purpuratus, Ciona intestinalis, and selected vertebrates were investigated. With some deviations, all vertebrate serpin genes fit into one of the six exon/intron gene classes previously identified, dating the existence and maintenance of these gene organizations before or close to the divergence of fishes. Multiple intron acquisition events have occurred in selected serpins during diversification of a lineage of actinopterygian fishes, whose genome underwent compaction. The novel introns were acquired within a limited time interval (on an evolutionary timescale) and only in these fishes.
Proteases refer to a group of enzymes whose catalytic function is to hydrolyse (cleavage) peptide bonds of proteins. Proteases occur naturally in all organisms and are involved in a multitude of physiological reactions from simple digestion of food proteins to highly regulated cascades. In this book, the authors discuss the maturation and stabilisation mechanisms of two hyperthermostable subtilisin-like serine proteases from thermococcus kodakarensis; serine protease-related innate immunity; fungal and bacterial serine proteases; and the physiological function and pathology of neurosin/kallikrein 6 in the central nervous system.
Proteases refer to a group of enzymes whose catalytic function is to hydrolyze(cleavage) peptide bonds of proteins. Proteases occur naturally in all organisms and are involved in a multitude of physiological reactions from simple digestion of food proteins to highly regulated cascades. In this book, the authors discuss the maturation and stabilization mechanisms of two hyperthermostable subtilisin-like serine proteases from thermococcus kodakarensis; serine protease-related innate immunity; fungal and bacterial serine proteases; and the physiological function and pathology of neurosin/kallikrein 6 in the central nervous system.
Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. The acronym serpin was originally coined because many serpins inhibit chymotrypsin-like serine proteases. This volume of Methods in Ezymology is split into 2 parts and comprehensively covers the subject.
This volume explores the latest methods used to study and define serpin molecular structure, basic protease inhibition, serpin targets, and the roles of serpin in biology and disease using animal models. The chapters in this book cover topics such as crystallography and phage display, peptide design, phospholipid binding, and thrombus formation to microbiome analysis and development. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Cutting edge and authoritative, Serpins: Methods and Protocols is a valuable resource for researchers and scientists interested in learning more about this evolving field.
The book provides an comprehensive overview on biology, genetics and cellular functions of serpins (serine protease inhibitors) in health and disease. With over 1000 members serpins are the most diverse family of protease inhibitors. Latest groundbreaking research findings are presented and broaden the understanding on inhibitory and non-inhibitory serpins, not only in mammalian organisms but also in insects, worms, plants and viruses.
International experts present innovative therapeutic strategies to treat cancer patients and prevent disease progression Extracellular Targeting of Cell Signaling in Cancer highlights innovative therapeutic strategies to treat cancer metastasis and prevent tumor progression. Currently, there are no drugs available to treat or prevent metastatic cancer other than non-selective, toxic chemotherapy. With contributions from an international panel of experts in the field, the book integrates diverse aspects of biochemistry, molecular biology, protein engineering, proteomics, cell biology, pharmacology, biophysics, structural biology, medicinal chemistry and drug development. A large class of proteins called kinases are enzymes required by cancer cells to grow, proliferate, and survive apoptosis (death) by the immune system. Two important kinases are MET and RON which are receptor tyrosine kinases (RTKs) that initiate cell signaling pathways outside the cell surface in response to extracellular ligands (growth factors.) Both kinases are oncogenes which are required by cancer cells to migrate away from the primary tumor, invade surrounding tissue and metastasize. MET and RON reside on both cancer cells and the support cells surrounding the tumor, called the microenvironment. MET and RON are activated by their particular ligands, the growth factors HGF and MSP, respectively. Blocking MET and RON kinase activation and downstream signaling is a promising therapeutic strategy for preventing tumor progression and metastasis. Written for cancer physicians and biologists as well as drug discovery and development teams in both industry and academia, this is the first book of its kind which explores novel approaches to inhibit MET and RON kinases other than traditional small molecule kinase inhibitors. These new strategies target key tumorigenic processes on the outside of the cell, such as growth factor activation by proteases. These unique strategies have promising potential as an improved alternative to kinase inhibitors, chemotherapy, or radiation treatment.
