Search

Paul Shapiro gives you a “captivating” (John Mackey, former CEO of Whole Foods Market) front-row seat for the race to create and commercialize cleaner, safer, sustainable meat—real meat—without the animals.Since the dawn of Homo sapiens some quarter million years ago, animals have satiated our species'desire for meat. But with a growing global popula­tion and demand for meat, eggs, dairy, leather, and more, raising such massive numbers of farm animals is woefully inefficient and takes an enormous toll on the planet, public health, and certainly the animals themselves. But what if we could have our meat and eat it, too? The next great scientific revolution is underway—“a future where the cellular agricultural revolution helps lower rates of foodborne illness, greatly improves environmental sustainability, and allows us to continue to enjoy the food we love” (Kathleen Sebelius, former US Secretary of Health and Human Services). Enter clean meat—real, actual meat grown (or brewed!) from animal cells—as well as other clean foods that ditch animal cells altogether and are simply built from the molecule up. Whereas our ancestors domesticated wild animals into livestock, today we're beginning to domesticate their cells, leaving the animals out of the equation. From one single cell of a cow, you could feed an entire village. And “in this important book that could just save your life” (Michael Greger, MD, author of How Not to Die), the story of this coming second domestica­tion is anything but tame.

Myosin: Biosynthesis, Classes and Function opens with a discussion on class I myosins, the most varied members of the myosin superfamily and a remarkable group of molecular motor proteins that move actin filaments and produce force. Class I myosin molecules have various physiological roles including maintenance of normal intestinal brush border structure, glucose homeostasis, glomerular filtration, immune function, and tumor promotion and suppression, and new studies are revealing that mutations may lead to diseases including cancer and kidney disease. Thus, the authors review the structure and function of the eight myosin-I isoforms (Myo1a-Myo1h) that are expressed in mammals. Next, the book discusses muscle contractile function and its association with the activity of the protein complex actomyosin, in which myosin exhibits enzyme activity, namely the ability to hydrolyze ATP. The demonstrated ability of calix[4]arenes C-97, C-99, C-90 and thiacalix[4]arenes C-798 and C-800 can be used for further research aimed at the use of these compounds as novel pharmacological agents able to efficiently restore normal contractile function of myometrium by inhibition or activation of this function, or the eliminating negative effects of heavy metal cations. Following this, the authors present the results of their experiments on studying the effects of different isotopes of magnesium and zinc on the enzymatic activity of myosin, namely the catalytic subfragment-1 of myosin, isolated from myometrium muscle. It has been revealed that the rate of the enzymatic ATP hydrolysis is 2–2.5 times higher in the reaction media enriched with the magnetic isotope, 25Mg, as compared to the activity of the same enzyme in the reaction media enriched with the nonmagnetic isotopes, 24Mg or 26Mg or MgCl2 of natural isotope abundance. Continuing, precipitation/extraction methods and MALDI TOF/TOF mass spectrometry were used in order to and identify, for the first time, a protein with the molecular mass of 48 kDa as a fragment of human unconventional myosin 1c isoform b in a blood serum of multiple sclerosis patients. Western-blot analysis using commercial monospecific anti-human Myo1c antibodies has shown that the molecular mass of this protein obtained from a blood serum of different human sources varied in between 46-48 kDa. Thus, the authors name the 46-48 kDa proteins revealed in a blood serum as a short form of the human unconventional myosin 1c (sMyo 1C).

Myostatin, also known as growth and differentiation factor-8, is a member of the TGF-â family member and is mainly produced by skeletal muscle. Myostatin circulates in the serum in a latent form, whereas it acts almost exclusively on skeletal muscle. Chapter One of this book discusses the role of myostatin and related factors in muscle hypertrophy and atophy. Chapter Two concentrates on specific alterations of positive and negative regulators of muscle mass in patients with chronic kidney disease. Chapter Three examines the potential benefits of the myostatin gene polymorphisms in livestock animals. Chapter Four studies myostatin functions in fish.

Muscle contraction is a vital biological activity. In three centuries of scientific pursuit since Leeuwenhoek and Croone observed the cellular structure of striated muscles, the knowledge gained from extensive studies has formed a detailed understanding of muscle function at the molecular and atomic level. Contractions of vertebrate skeletal and cardiac muscles are controlled by Ca2+ signaling through the troponin complex in the sarcomeres, which are contractile machinery consisting of interactive myofilaments. Since the discovery and biochemical characterization of troponin and its three subunit proteins over four decades ago, intensive research from protein structure and genetic diversity to post-translational modification and pathological mutations have comprehensively established the molecular structure of troponin and the mechanistic details of its function in the regulation of muscle contractions. The advanced knowledge from troponin research has contributed significantly to the current understanding of cardiac and skeletal muscle function in health and diseases. It is a timely necessity to comprehensively, yet concisely, summarize the current knowledge and look toward the future direction of troponin research. Contributions to this book have been made by leading experts in troponin studies, and its contents include chapters that describe milestone discoveries and recent research advances. This wonderful collection provides a unique reference for students and research investigators who have an interest in muscles, protein structure-function relationships and molecular evolution, as well as cardiac function and myopathies. Readers will not only obtain an in-depth state-of-the-science understanding of troponin structure and function, they will also be exposed to visions that will lead them toward future investigations and the advancement of troponin research.

Fish and marine invertebrates are important sources of nutrients for the world's population, and many species have exceptionally high market value because of their exquisite sensory properties. Both the utilization of the available catch in different forms and the market price are affected by the quality of the fish. Proteins and nonprotein nitroge­ nous compounds playa crucial role in the nutritional value and sensory quality of seafoods as well as in the suitability of different species to various forms of processing, preservation, and use in other branches of the food industry. This role of proteins results from their basic chemical and biochemical properties and functions in different tissues. A presenta­ tion of the actual state of knowledge on seafood nitrogenous compounds in one volume may contribute to a better understanding of the involve­ ment of these components in all stages of handling and processing fish. It has been possible to prepare this text thanks to the cooperative effort of an international group of specialists. The editors of the book are greatly indebted to all colleagues who have willingly contributed to this volume, sharing their knowledge and experience, as well as to all persons who have granted permission to use their previously published materials. viii Preface ix A large part of the book has been prepared during my sabbatical in the Department of Marine Food Science, National Taiwan Ocean University (NTOU) in Keelung, Taiwan.

The general aim of this book is to provide a comprehensive summary of the characteristics of exercise-induced muscle damage and the mechanisms of tissue inflammation. The authors present a large amount of our own original data and have summarized the research of others. This book will be of interest to students, researchers and practitioners in the field of exercise physiology, physiotherapy and occupational therapy.

Few would have predicted 20 years ago that myosins constitute a superfamily with at least two-dozen classes and that these molecular motors are involved in a multitude of intracellular activities including cell division, cell movement, intracellular transport and signal transduction. Application of state-of-the-art cellular and molecular biological, structural biological, genetic, biochemical and biophysical techniques has provided and continues to provide critical information regarding the structure–function relationship; and the cellular roles of various myosins in organisms as diverse as protozoa, yeast, plants and higher animals. The association of myosins with diseases including neurological disorders, immu- deficiencies, cardiomyopathies, hearing and vision loss testify to the importance of understanding the biochemical properties and cellular roles of myosins. The 16 chapters in this volume summarize the tremendous progress made in studying members of the myosin superfamily in recent years and offer critical insight into what future research will yield. I would like to express my sincere gratitude to the authors of this volume. It was a pleasure to work with each of you and I thank you for the considerable efforts in making this international endeavor possible. I also thank John Trinick from the University of Leeds, UK, for the elegant montage of images of single molecules of myosins on the cover, which beautifully shows the structures of some of these amazing molecules. The able assistance of Marlies Vlot from Springer and Indumadhi Srinivasan from Integra Software Services for production of the book is greatly appreciated.

Methods for Obtaining X-Ray Diffraction Patterns from Drosophila 198 Diffraction Patterns from Drosophila IFM 203 Concluding Remarks 211 Note Added in Proof 211 17. Functional and Ecological Effects of Isoform Variation in Insect Flight Muscle 214 James H. Marden Abstract 214 Introduction 215 Nature's Versatile Engine 215 The Underlying Genetics: An Underinflated Genome and a Hyperinflated Transcriptome and Proteome 216 Functional Effects of Isoform Variation 219 Alternative Splicing and the Generation of Combinatorial Complexity 220 Functional Consequences of Naturally Occurring Isoform Variation 220 18. Muscle Systems Design and Integration 230 Fritz- OlafLehmann Abstract 230 Power Requirements for Flight 230 Power Reduction 233 Power Constraints on Steering Capacity 234 Balancing Power and Control 236 Changes in Muscle Efficiency in Vivo 238 Concluding Remarks 239 From the Inside Out 19. Molecular Assays for Acto-Myosin Interactions 242 John C. Sparrow and Michael A. Geeves Abstract 242 Introduction 242 Myosin Purification and Preparation of the SI Fragment 243 Purification of Flight Muscle Actin 244 Assays of Myosin and Acto-Myosin 244 Major Conclusions Relating to the Enzymatic Properties of Insect Flight Muscle Acto-Myosin 247 Major Questions about Insect Flight Muscle Acto-Myosin Kinetics That Remain 249 20.

This book was originally published in 2002. Elastic proteins occur in a wide range of biological systems where they have evolved to fulfil precise biological roles. The best known include proteins in vertebrate muscles and connective tissues, such as titin, elastin and fibrillin, and spider silks. However, other examples include byssus and abductin from bivalve molluscs, resilin from arthropods and gluten from wheat. Interest in elastomeric proteins has been high for several reasons. Firstly, their biological and medical significance, particularly in human disease. Secondly, the unusual properties of proteins such as spider silks provide opportunities to develop materials. Thirdly, the development of scanning probe microscopy makes it possible to study structures and biomechanical properties of these proteins at the single molecule level. This book will be of value to anyone with an interest in the various aspects of elastomeric proteins.

Muscle and Meat Biochemistry teaches the different concepts and topics under the eponymous subject. The book covers the gross and detailed composition and structure of muscles and the relationship of the nervous system with the muscular system; muscle cell differentiation and growth; proteins of the thick filament; and the molecular structure and enzymatic activity of myosin. The text also discusses the proteins found in the thin filament - actin, troponin, and myosin; skeletal muscle growth; protein metabolism; and fiber types. The book also encompasses cardiac and smooth muscle; sarcoplasmic proteins; the connective tissues - collagen, elastin, and ground substance; and the postmortem changes during conversion of muscle to meat. The text is recommended for advanced undergraduate and graduate students, as well as for scientists who would like to know more about muscle biology, muscle physiology, and meat science.