Muscle Proteins: The protein constituents of muscle, the major ones being ACTINS and MYOSINS. More than a dozen accessory proteins exist including TROPONIN; TROPOMYOSIN; and DYSTROPHIN.Muscles: Contractile tissue that produces movement in animals.Muscle, Skeletal: A subtype of striated muscle, attached by TENDONS to the SKELETON. Skeletal muscles are innervated and their movement can be consciously controlled. They are also called voluntary muscles.Muscle, Smooth: Unstriated and unstriped muscle, one of the muscles of the internal organs, blood vessels, hair follicles, etc. Contractile elements are elongated, usually spindle-shaped cells with centrally located nuclei. Smooth muscle fibers are bound together into sheets or bundles by reticular fibers and frequently elastic nets are also abundant. (From Stedman, 25th ed)Methylhistidines: Histidine substituted in any position with one or more methyl groups.Phenylalanine: An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.Muscle Fibers, Skeletal: Large, multinucleate single cells, either cylindrical or prismatic in shape, that form the basic unit of SKELETAL MUSCLE. They consist of MYOFIBRILS enclosed within and attached to the SARCOLEMMA. They are derived from the fusion of skeletal myoblasts (MYOBLASTS, SKELETAL) into a syncytium, followed by differentiation.Muscle Development: Developmental events leading to the formation of adult muscular system, which includes differentiation of the various types of muscle cell precursors, migration of myoblasts, activation of myogenesis and development of muscle anchorage.Muscle, Smooth, Vascular: The nonstriated involuntary muscle tissue of blood vessels.Muscle Contraction: A process leading to shortening and/or development of tension in muscle tissue. Muscle contraction occurs by a sliding filament mechanism whereby actin filaments slide inward among the myosin filaments.Muscular Atrophy: Derangement in size and number of muscle fibers occurring with aging, reduction in blood supply, or following immobilization, prolonged weightlessness, malnutrition, and particularly in denervation.Leucine: An essential branched-chain amino acid important for hemoglobin formation.Amino Acids, Essential: Amino acids that are not synthesized by the human body in amounts sufficient to carry out physiological functions. They are obtained from dietary foodstuffs.Amino Acids: Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.Muscle Fibers, Fast-Twitch: Skeletal muscle fibers characterized by their expression of the Type II MYOSIN HEAVY CHAIN isoforms which have high ATPase activity and effect several other functional properties - shortening velocity, power output, rate of tension redevelopment. Several fast types have been identified.Quadriceps Muscle: The quadriceps femoris. A collective name of the four-headed skeletal muscle of the thigh, comprised of the rectus femoris, vastus intermedius, vastus lateralis, and vastus medialis.Muscle Denervation: The resection or removal of the innervation of a muscle or muscle tissue.Myofibrils: The long cylindrical contractile organelles of STRIATED MUSCLE cells composed of ACTIN FILAMENTS; MYOSIN filaments; and other proteins organized in arrays of repeating units called SARCOMERES .Muscle Fibers, Slow-Twitch: Skeletal muscle fibers characterized by their expression of the Type I MYOSIN HEAVY CHAIN isoforms which have low ATPase activity and effect several other functional properties - shortening velocity, power output, rate of tension redevelopment.Muscle Fatigue: A state arrived at through prolonged and strong contraction of a muscle. Studies in athletes during prolonged submaximal exercise have shown that muscle fatigue increases in almost direct proportion to the rate of muscle glycogen depletion. Muscle fatigue in short-term maximal exercise is associated with oxygen lack and an increased level of blood and muscle lactic acid, and an accompanying increase in hydrogen-ion concentration in the exercised muscle.Mitochondria, Muscle: Mitochondria of skeletal and smooth muscle. It does not include myocardial mitochondria for which MITOCHONDRIA, HEART is available.Insulin: A 51-amino acid pancreatic hormone that plays a major role in the regulation of glucose metabolism, directly by suppressing endogenous glucose production (GLYCOGENOLYSIS; GLUCONEOGENESIS) and indirectly by suppressing GLUCAGON secretion and LIPOLYSIS. Native insulin is a globular protein comprised of a zinc-coordinated hexamer. Each insulin monomer containing two chains, A (21 residues) and B (30 residues), linked by two disulfide bonds. Insulin is used as a drug to control insulin-dependent diabetes mellitus (DIABETES MELLITUS, TYPE 1).Connectin: A giant elastic protein of molecular mass ranging from 2,993 kDa (cardiac), 3,300 kDa (psoas), to 3,700 kDa (soleus) having a kinase domain. The amino- terminal is involved in a Z line binding, and the carboxy-terminal region is bound to the myosin filament with an overlap between the counter-connectin filaments at the M line.Sarcopenia: Progressive decline in muscle mass due to aging which results in decreased functional capacity of muscles.Amino Acids, Branched-Chain: Amino acids which have a branched carbon chain.Myocytes, Smooth Muscle: Non-striated, elongated, spindle-shaped cells found lining the digestive tract, uterus, and blood vessels. They are derived from specialized myoblasts (MYOBLASTS, SMOOTH MUSCLE).Muscle Weakness: A vague complaint of debility, fatigue, or exhaustion attributable to weakness of various muscles. The weakness can be characterized as subacute or chronic, often progressive, and is a manifestation of many muscle and neuromuscular diseases. (From Wyngaarden et al., Cecil Textbook of Medicine, 19th ed, p2251)Muscular Diseases: Acquired, familial, and congenital disorders of SKELETAL MUSCLE and SMOOTH MUSCLE.Neck Muscles: The neck muscles consist of the platysma, splenius cervicis, sternocleidomastoid(eus), longus colli, the anterior, medius, and posterior scalenes, digastric(us), stylohyoid(eus), mylohyoid(eus), geniohyoid(eus), sternohyoid(eus), omohyoid(eus), sternothyroid(eus), and thyrohyoid(eus).Oculomotor Muscles: The muscles that move the eye. Included in this group are the medial rectus, lateral rectus, superior rectus, inferior rectus, inferior oblique, superior oblique, musculus orbitalis, and levator palpebrae superioris.Leg: The inferior part of the lower extremity between the KNEE and the ANKLE.Muscle, Striated: One of two types of muscle in the body, characterized by the array of bands observed under microscope. Striated muscles can be divided into two subtypes: the CARDIAC MUSCLE and the SKELETAL MUSCLE.Muscle Spindles: Skeletal muscle structures that function as the MECHANORECEPTORS responsible for the stretch or myotactic reflex (REFLEX, STRETCH). They are composed of a bundle of encapsulated SKELETAL MUSCLE FIBERS, i.e., the intrafusal fibers (nuclear bag 1 fibers, nuclear bag 2 fibers, and nuclear chain fibers) innervated by SENSORY NEURONS.Muscle Relaxation: That phase of a muscle twitch during which a muscle returns to a resting position.Respiratory Muscles: These include the muscles of the DIAPHRAGM and the INTERCOSTAL MUSCLES.Muscle Cells: Mature contractile cells, commonly known as myocytes, that form one of three kinds of muscle. The three types of muscle cells are skeletal (MUSCLE FIBERS, SKELETAL), cardiac (MYOCYTES, CARDIAC), and smooth (MYOCYTES, SMOOTH MUSCLE). They are derived from embryonic (precursor) muscle cells called MYOBLASTS.Resistance Training: A type of strength-building exercise program that requires the body muscle to exert a force against some form of resistance, such as weight, stretch bands, water, or immovable objects. Resistance exercise is a combination of static and dynamic contractions involving shortening and lengthening of skeletal muscles.Papillary Muscles: Conical muscular projections from the walls of the cardiac ventricles, attached to the cusps of the atrioventricular valves by the chordae tendineae.Cachexia: General ill health, malnutrition, and weight loss, usually associated with chronic disease.Aging: The gradual irreversible changes in structure and function of an organism that occur as a result of the passage of time.TOR Serine-Threonine Kinases: A serine threonine kinase that controls a wide range of growth-related cellular processes. The protein is referred to as the target of RAPAMYCIN due to the discovery that SIROLIMUS (commonly known as rapamycin) forms an inhibitory complex with TACROLIMUS BINDING PROTEIN 1A that blocks the action of its enzymatic activity.Dietary Proteins: Proteins obtained from foods. They are the main source of the ESSENTIAL AMINO ACIDS.Exercise: Physical activity which is usually regular and done with the intention of improving or maintaining PHYSICAL FITNESS or HEALTH. Contrast with PHYSICAL EXERTION which is concerned largely with the physiologic and metabolic response to energy expenditure.Abdominal Muscles: Muscles forming the ABDOMINAL WALL including RECTUS ABDOMINIS, external and internal oblique muscles, transversus abdominis, and quadratus abdominis. (from Stedman, 25th ed)SKP Cullin F-Box Protein Ligases: A subset of ubiquitin protein ligases that are formed by the association of a SKP DOMAIN PROTEIN, a CULLIN DOMAIN PROTEIN and a F-BOX DOMAIN PROTEIN.Weight Lifting: A sport in which weights are lifted competitively or as an exercise.Masseter Muscle: A masticatory muscle whose action is closing the jaws.Myosin Heavy Chains: The larger subunits of MYOSINS. The heavy chains have a molecular weight of about 230 kDa and each heavy chain is usually associated with a dissimilar pair of MYOSIN LIGHT CHAINS. The heavy chains possess actin-binding and ATPase activity.Anabolic Agents: These compounds stimulate anabolism and inhibit catabolism. They stimulate the development of muscle mass, strength, and power.Time Factors: Elements of limited time intervals, contributing to particular results or situations.Facial Muscles: Muscles of facial expression or mimetic muscles that include the numerous muscles supplied by the facial nerve that are attached to and move the skin of the face. (From Stedman, 25th ed)Myostatin: A growth differentiation factor that is a potent inhibitor of SKELETAL MUSCLE growth. It may play a role in the regulation of MYOGENESIS and in muscle maintenance during adulthood.Protein Biosynthesis: The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.Masticatory Muscles: Muscles arising in the zygomatic arch that close the jaw. Their nerve supply is masseteric from the mandibular division of the trigeminal nerve. (From Stedman, 25th ed)Kinetics: The rate dynamics in chemical or physical systems.Oxandrolone: A synthetic hormone with anabolic and androgenic properties.Intercostal Muscles: Respiratory muscles that arise from the lower border of one rib and insert into the upper border of the adjoining rib, and contract during inspiration or respiration. (From Stedman, 25th ed)Hindlimb: Either of two extremities of four-footed non-primate land animals. It usually consists of a FEMUR; TIBIA; and FIBULA; tarsals; METATARSALS; and TOES. (From Storer et al., General Zoology, 6th ed, p73)Electromyography: Recording of the changes in electric potential of muscle by means of surface or needle electrodes.Rabbits: The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.Rats, Sprague-Dawley: A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company.Blood Glucose: Glucose in blood.Isometric Contraction: Muscular contractions characterized by increase in tension without change in length.HIV Wasting Syndrome: Involuntary weight loss of greater than 10 percent associated with intermittent or constant fever and chronic diarrhea or fatigue for more than 30 days in the absence of a defined cause other than HIV infection. A constant feature is major muscle wasting with scattered myofiber degeneration. A variety of etiologies, which vary among patients, contributes to this syndrome. (From Harrison's Principles of Internal Medicine, 13th ed, p1611).Satellite Cells, Skeletal Muscle: Elongated, spindle-shaped, quiescent myoblasts lying in close contact with adult skeletal muscle. They are thought to play a role in muscle repair and regeneration.Ribosomal Protein S6 Kinases, 70-kDa: A family of ribosomal protein S6 kinases that are considered the major physiological kinases for RIBOSOMAL PROTEIN S6. Unlike RIBOSOMAL PROTEIN S6 KINASES, 90KDa the proteins in this family are sensitive to the inhibitory effects of RAPAMYCIN and contain a single kinase domain. They are referred to as 70kDa proteins, however ALTERNATIVE SPLICING of mRNAs for proteins in this class also results in 85kDa variants being formed.Eukaryotic Initiation Factor-4E: A peptide initiation factor that binds specifically to the 5' MRNA CAP STRUCTURE of MRNA in the CYTOPLASM. It is a component of the trimeric complex EIF4F.Protein HydrolysatesSignal Transduction: The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.Protein Kinases: A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.Body Weight: The mass or quantity of heaviness of an individual. It is expressed by units of pounds or kilograms.Pectoralis Muscles: The pectoralis major and pectoralis minor muscles that make up the upper and fore part of the chest in front of the AXILLA.Myoblasts: Embryonic (precursor) cells of the myogenic lineage that develop from the MESODERM. They undergo proliferation, migrate to their various sites, and then differentiate into the appropriate form of myocytes (MYOCYTES, SKELETAL; MYOCYTES, CARDIAC; MYOCYTES, SMOOTH MUSCLE).Postprandial Period: The time frame after a meal or FOOD INTAKE.Biopsy: Removal and pathologic examination of specimens in the form of small pieces of tissue from the living body.Muscular Disorders, Atrophic: Disorders characterized by an abnormal reduction in muscle volume due to a decrease in the size or number of muscle fibers. Atrophy may result from diseases intrinsic to muscle tissue (e.g., MUSCULAR DYSTROPHY) or secondary to PERIPHERAL NERVOUS SYSTEM DISEASES that impair innervation to muscle tissue (e.g., MUSCULAR ATROPHY, SPINAL).Burns: Injuries to tissues caused by contact with heat, steam, chemicals (BURNS, CHEMICAL), electricity (BURNS, ELECTRIC), or the like.Energy Metabolism: The chemical reactions involved in the production and utilization of various forms of energy in cells.Actins: Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle.RNA, Messenger: RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.Phosphorylation: The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.Insulin-Like Growth Factor I: A well-characterized basic peptide believed to be secreted by the liver and to circulate in the blood. It has growth-regulating, insulin-like, and mitogenic activities. This growth factor has a major, but not absolute, dependence on GROWTH HORMONE. It is believed to be mainly active in adults in contrast to INSULIN-LIKE GROWTH FACTOR II, which is a major fetal growth factor.Rats, Wistar: A strain of albino rat developed at the Wistar Institute that has spread widely at other institutions. This has markedly diluted the original strain.Muscular Dystrophy, AnimalRegional Blood Flow: The flow of BLOOD through or around an organ or region of the body.Carbon Isotopes: Stable carbon atoms that have the same atomic number as the element carbon, but differ in atomic weight. C-13 is a stable carbon isotope.Ribosomal Protein S6 Kinases: A family of protein serine/threonine kinases which act as intracellular signalling intermediates. Ribosomal protein S6 kinases are activated through phosphorylation in response to a variety of HORMONES and INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS. Phosphorylation of RIBOSOMAL PROTEIN S6 by enzymes in this class results in increased expression of 5' top MRNAs. Although specific for RIBOSOMAL PROTEIN S6 members of this class of kinases can act on a number of substrates within the cell. The immunosuppressant SIROLIMUS inhibits the activation of ribosomal protein S6 kinases.Cells, Cultured: Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.Physical Endurance: The time span between the beginning of physical activity by an individual and the termination because of exhaustion.Metabolism: The chemical reactions that occur within the cells, tissues, or an organism. These processes include both the biosynthesis (ANABOLISM) and the breakdown (CATABOLISM) of organic materials utilized by the living organism.Organ Size: The measurement of an organ in volume, mass, or heaviness.Wasting Syndrome: A condition of involuntary weight loss of greater then 10% of baseline body weight. It is characterized by atrophy of muscles and depletion of lean body mass. Wasting is a sign of MALNUTRITION as a result of inadequate dietary intake, malabsorption, or hypermetabolism.Body Composition: The relative amounts of various components in the body, such as percentage of body fat.Physical Exertion: Expenditure of energy during PHYSICAL ACTIVITY. Intensity of exertion may be measured by rate of OXYGEN CONSUMPTION; HEAT produced, or HEART RATE. Perceived exertion, a psychological measure of exertion, is included.Parenteral Nutrition Solutions: Specialized solutions for PARENTERAL NUTRITION. They may contain a variety of MICRONUTRIENTS; VITAMINS; AMINO ACIDS; CARBOHYDRATES; LIPIDS; and SALTS.Dietary Supplements: Products in capsule, tablet or liquid form that provide dietary ingredients, and that are intended to be taken by mouth to increase the intake of nutrients. Dietary supplements can include macronutrients, such as proteins, carbohydrates, and fats; and/or MICRONUTRIENTS, such as VITAMINS; MINERALS; and PHYTOCHEMICALS.Nitrogen Isotopes: Stable nitrogen atoms that have the same atomic number as the element nitrogen, but differ in atomic weight. N-15 is a stable nitrogen isotope.Psoas Muscles: A powerful flexor of the thigh at the hip joint (psoas major) and a weak flexor of the trunk and lumbar spinal column (psoas minor). Psoas is derived from the Greek "psoa", the plural meaning "muscles of the loin". It is a common site of infection manifesting as abscess (PSOAS ABSCESS). The psoas muscles and their fibers are also used frequently in experiments in muscle physiology.Chickens: Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA.Diaphragm: The musculofibrous partition that separates the THORACIC CAVITY from the ABDOMINAL CAVITY. Contraction of the diaphragm increases the volume of the thoracic cavity aiding INHALATION.Hypertrophy: General increase in bulk of a part or organ due to CELL ENLARGEMENT and accumulation of FLUIDS AND SECRETIONS, not due to tumor formation, nor to an increase in the number of cells (HYPERPLASIA).Calcium: A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.Sarcomeres: The repeating contractile units of the MYOFIBRIL, delimited by Z bands along its length.GlycogenProteins: Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.Bed Rest: Confinement of an individual to bed for therapeutic or experimental reasons.Gene Expression Regulation: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.Temporal Muscle: A masticatory muscle whose action is closing the jaws; its posterior portion retracts the mandible.Glucose: A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement.Hormones: Chemical substances having a specific regulatory effect on the activity of a certain organ or organs. The term was originally applied to substances secreted by various ENDOCRINE GLANDS and transported in the bloodstream to the target organs. It is sometimes extended to include those substances that are not produced by the endocrine glands but that have similar effects.Radioactive Tracers: Radioactive substances added in minute amounts to the reacting elements or compounds in a chemical process and traced through the process by appropriate detection methods, e.g., Geiger counter. Compounds containing tracers are often said to be tagged or labeled. (Hawley's Condensed Chemical Dictionary, 12th ed)Ribosomal Protein S6: A ribosomal protein that may play a role in controlling cell growth and proliferation. It is a major substrate of RIBOSOMAL PROTEIN S6 KINASES and plays a role in regulating the translation (TRANSLATION, GENETIC) of RNAs that contain an RNA 5' TERMINAL OLIGOPYRIMIDINE SEQUENCE.Hindlimb Suspension: Technique for limiting use, activity, or movement by immobilizing or restraining animal by suspending from hindlimbs or tails. This immobilization is used to simulate some effects of reduced gravity and study weightlessness physiology.Proteasome Endopeptidase Complex: A large multisubunit complex that plays an important role in the degradation of most of the cytosolic and nuclear proteins in eukaryotic cells. It contains a 700-kDa catalytic sub-complex and two 700-kDa regulatory sub-complexes. The complex digests ubiquitinated proteins and protein activated via ornithine decarboxylase antizyme.Electric Stimulation: Use of electric potential or currents to elicit biological responses.Models, Biological: Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.Starvation: Lengthy and continuous deprivation of food. (Stedman, 25th ed)Immobilization: The restriction of the MOVEMENT of whole or part of the body by physical means (RESTRAINT, PHYSICAL) or chemically by ANALGESIA, or the use of TRANQUILIZING AGENTS or NEUROMUSCULAR NONDEPOLARIZING AGENTS. It includes experimental protocols used to evaluate the physiologic effects of immobility.Myocardium: The muscle tissue of the HEART. It is composed of striated, involuntary muscle cells (MYOCYTES, CARDIAC) connected to form the contractile pump to generate blood flow.Nutritional Physiological Phenomena: The processes and properties of living organisms by which they take in and balance the use of nutritive materials for energy, heat production, or building material for the growth, maintenance, or repair of tissues and the nutritive properties of FOOD.Nitrogen: An element with the atomic symbol N, atomic number 7, and atomic weight [14.00643; 14.00728]. Nitrogen exists as a diatomic gas and makes up about 78% of the earth's atmosphere by volume. It is a constituent of proteins and nucleic acids and found in all living cells.MyoD Protein: A myogenic regulatory factor that controls myogenesis. Though it is not clear how its function differs from the other myogenic regulatory factors, MyoD appears to be related to fusion and terminal differentiation of the muscle cell.Rats, Inbred Strains: Genetically identical individuals developed from brother and sister matings which have been carried out for twenty or more generations or by parent x offspring matings carried out with certain restrictions. This also includes animals with a long history of closed colony breeding.Pharyngeal Muscles: The muscles of the PHARYNX are voluntary muscles arranged in two layers. The external circular layer consists of three constrictors (superior, middle, and inferior). The internal longitudinal layer consists of the palatopharyngeus, the salpingopharyngeus, and the stylopharyngeus. During swallowing, the outer layer constricts the pharyngeal wall and the inner layer elevates pharynx and LARYNX.Tropomyosin: A protein found in the thin filaments of muscle fibers. It inhibits contraction of the muscle unless its position is modified by TROPONIN.Muscular Dystrophies: A heterogeneous group of inherited MYOPATHIES, characterized by wasting and weakness of the SKELETAL MUSCLE. They are categorized by the sites of MUSCLE WEAKNESS; AGE OF ONSET; and INHERITANCE PATTERNS.Deuterium: Deuterium. The stable isotope of hydrogen. It has one neutron and one proton in the nucleus.Eukaryotic Initiation Factor-2B: A guanine nucleotide exchange factor that acts to restore EUKARYOTIC INITIATION FACTOR-2 to its GTP bound form.Keto AcidsBlotting, Western: Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.Dystrophin: A muscle protein localized in surface membranes which is the product of the Duchenne/Becker muscular dystrophy gene. Individuals with Duchenne muscular dystrophy usually lack dystrophin completely while those with Becker muscular dystrophy have dystrophin of an altered size. It shares features with other cytoskeletal proteins such as SPECTRIN and alpha-actinin but the precise function of dystrophin is not clear. One possible role might be to preserve the integrity and alignment of the plasma membrane to the myofibrils during muscle contraction and relaxation. MW 400 kDa.Biomechanical Phenomena: The properties, processes, and behavior of biological systems under the action of mechanical forces.Animals, Newborn: Refers to animals in the period of time just after birth.Dietary Carbohydrates: Carbohydrates present in food comprising digestible sugars and starches and indigestible cellulose and other dietary fibers. The former are the major source of energy. The sugars are in beet and cane sugar, fruits, honey, sweet corn, corn syrup, milk and milk products, etc.; the starches are in cereal grains, legumes (FABACEAE), tubers, etc. (From Claudio & Lagua, Nutrition and Diet Therapy Dictionary, 3d ed, p32, p277)Creatine Kinase: A transferase that catalyzes formation of PHOSPHOCREATINE from ATP + CREATINE. The reaction stores ATP energy as phosphocreatine. Three cytoplasmic ISOENZYMES have been identified in human tissues: the MM type from SKELETAL MUSCLE, the MB type from myocardial tissue and the BB type from nervous tissue as well as a mitochondrial isoenzyme. Macro-creatine kinase refers to creatine kinase complexed with other serum proteins.Infusions, Intravenous: The long-term (minutes to hours) administration of a fluid into the vein through venipuncture, either by letting the fluid flow by gravity or by pumping it.Food Deprivation: The withholding of food in a structured experimental situation.Glucose Clamp Technique: Maintenance of a constant blood glucose level by perfusion or infusion with glucose or insulin. It is used for the study of metabolic rates (e.g., in glucose, lipid, amino acid metabolism) at constant glucose concentration.Sarcoplasmic Reticulum: A network of tubules and sacs in the cytoplasm of SKELETAL MUSCLE FIBERS that assist with muscle contraction and relaxation by releasing and storing calcium ions.Glutamine: A non-essential amino acid present abundantly throughout the body and is involved in many metabolic processes. It is synthesized from GLUTAMIC ACID and AMMONIA. It is the principal carrier of NITROGEN in the body and is an important energy source for many cells.Fasting: Abstaining from all food.Motor Neurons: Neurons which activate MUSCLE CELLS.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Lactic Acid: A normal intermediate in the fermentation (oxidation, metabolism) of sugar. The concentrated form is used internally to prevent gastrointestinal fermentation. (From Stedman, 26th ed)Mice, Inbred C57BLNeuromuscular Junction: The synapse between a neuron and a muscle.Phosphocreatine: An endogenous substance found mainly in skeletal muscle of vertebrates. It has been tried in the treatment of cardiac disorders and has been added to cardioplegic solutions. (Reynolds JEF(Ed): Martindale: The Extra Pharmacopoeia (electronic version). Micromedex, Inc, Englewood, CO, 1996)Calpain: Cysteine proteinase found in many tissues. Hydrolyzes a variety of endogenous proteins including NEUROPEPTIDES; CYTOSKELETAL PROTEINS; proteins from SMOOTH MUSCLE; CARDIAC MUSCLE; liver; platelets; and erythrocytes. Two subclasses having high and low calcium sensitivity are known. Removes Z-discs and M-lines from myofibrils. Activates phosphorylase kinase and cyclic nucleotide-independent protein kinase. This enzyme was formerly listed as EC 3.4.22.4.Adenosine Triphosphate: An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.Reference Values: The range or frequency distribution of a measurement in a population (of organisms, organs or things) that has not been selected for the presence of disease or abnormality.Desmin: An intermediate filament protein found predominantly in smooth, skeletal, and cardiac muscle cells. Localized at the Z line. MW 50,000 to 55,000 is species dependent.Random Allocation: A process involving chance used in therapeutic trials or other research endeavor for allocating experimental subjects, human or animal, between treatment and control groups, or among treatment groups. It may also apply to experiments on inanimate objects.Swine: Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA).Femoral Artery: The main artery of the thigh, a continuation of the external iliac artery.ValeratesMuscle Cramp: A sustained and usually painful contraction of muscle fibers. This may occur as an isolated phenomenon or as a manifestation of an underlying disease process (e.g., UREMIA; HYPOTHYROIDISM; MOTOR NEURON DISEASE; etc.). (From Adams et al., Principles of Neurology, 6th ed, p1398)Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Peptide Elongation Factor 2: Peptide Elongation Factor 2 catalyzes the translocation of peptidyl-tRNA from the A site to the P site of eukaryotic ribosomes by a process linked to the hydrolysis of GTP to GDP.Milk Proteins: The major protein constituents of milk are CASEINS and whey proteins such as LACTALBUMIN and LACTOGLOBULINS. IMMUNOGLOBULINS occur in high concentrations in COLOSTRUM and in relatively lower concentrations in milk. (Singleton and Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed, p554)Eating: The consumption of edible substances.Clenbuterol: A substituted phenylaminoethanol that has beta-2 adrenomimetic properties at very low doses. It is used as a bronchodilator in asthma.Eukaryotic Initiation Factor-4G: A component of eukaryotic initiation factor-4F that is involved in multiple protein interactions at the site of translation initiation. Thus it may serve a role in bringing together various initiation factors at the site of translation initiation.Actinin: A protein factor that regulates the length of R-actin. It is chemically similar, but immunochemically distinguishable from actin.Hyperinsulinism: A syndrome with excessively high INSULIN levels in the BLOOD. It may cause HYPOGLYCEMIA. Etiology of hyperinsulinism varies, including hypersecretion of a beta cell tumor (INSULINOMA); autoantibodies against insulin (INSULIN ANTIBODIES); defective insulin receptor (INSULIN RESISTANCE); or overuse of exogenous insulin or HYPOGLYCEMIC AGENTS.Meat: The edible portions of any animal used for food including domestic mammals (the major ones being cattle, swine, and sheep) along with poultry, fish, shellfish, and game.Multienzyme Complexes: Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.Eukaryotic Initiation Factors: Peptide initiation factors from eukaryotic organisms. Over twelve factors are involved in PEPTIDE CHAIN INITIATION, TRANSLATIONAL in eukaryotic cells. Many of these factors play a role in controlling the rate of MRNA TRANSLATION.Insulin Resistance: Diminished effectiveness of INSULIN in lowering blood sugar levels: requiring the use of 200 units or more of insulin per day to prevent HYPERGLYCEMIA or KETOSIS.Femoral Vein: The vein accompanying the femoral artery in the same sheath; it is a continuation of the popliteal vein and becomes the external iliac vein.RNA: A polynucleotide consisting essentially of chains with a repeating backbone of phosphate and ribose units to which nitrogenous bases are attached. RNA is unique among biological macromolecules in that it can encode genetic information, serve as an abundant structural component of cells, and also possesses catalytic activity. (Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)Protein Isoforms: Different forms of a protein that may be produced from different GENES, or from the same gene by ALTERNATIVE SPLICING.Adipose Tissue: Specialized connective tissue composed of fat cells (ADIPOCYTES). It is the site of stored FATS, usually in the form of TRIGLYCERIDES. In mammals, there are two types of adipose tissue, the WHITE FAT and the BROWN FAT. Their relative distributions vary in different species with most adipose tissue being white.Oxygen Consumption: The rate at which oxygen is used by a tissue; microliters of oxygen STPD used per milligram of tissue per hour; the rate at which oxygen enters the blood from alveolar gas, equal in the steady state to the consumption of oxygen by tissue metabolism throughout the body. (Stedman, 25th ed, p346)Cattle: Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.Meals: A portion of the food eaten for the day, usually at regular occasions during the day.Dose-Response Relationship, Drug: The relationship between the dose of an administered drug and the response of the organism to the drug.Adaptation, Physiological: The non-genetic biological changes of an organism in response to challenges in its ENVIRONMENT.Proto-Oncogene Proteins c-akt: A protein-serine-threonine kinase that is activated by PHOSPHORYLATION in response to GROWTH FACTORS or INSULIN. It plays a major role in cell metabolism, growth, and survival as a core component of SIGNAL TRANSDUCTION. Three isoforms have been described in mammalian cells.Sarcoma, YoshidaFood: Any substances taken in by the body that provide nourishment.Proteolysis: Cleavage of proteins into smaller peptides or amino acids either by PROTEASES or non-enzymatically (e.g., Hydrolysis). It does not include Protein Processing, Post-Translational.Carbon Radioisotopes: Unstable isotopes of carbon that decay or disintegrate emitting radiation. C atoms with atomic weights 10, 11, and 14-16 are radioactive carbon isotopes.Cell Differentiation: Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs.Regeneration: The physiological renewal, repair, or replacement of tissue.Mice, Inbred mdx: A strain of mice arising from a spontaneous MUTATION (mdx) in inbred C57BL mice. This mutation is X chromosome-linked and produces viable homozygous animals that lack the muscle protein DYSTROPHIN, have high serum levels of muscle ENZYMES, and possess histological lesions similar to human MUSCULAR DYSTROPHY. The histological features, linkage, and map position of mdx make these mice a worthy animal model of DUCHENNE MUSCULAR DYSTROPHY.Ubiquitin: A highly conserved 76-amino acid peptide universally found in eukaryotic cells that functions as a marker for intracellular PROTEIN TRANSPORT and degradation. Ubiquitin becomes activated through a series of complicated steps and forms an isopeptide bond to lysine residues of specific proteins within the cell. These "ubiquitinated" proteins can be recognized and degraded by proteosomes or be transported to specific compartments within the cell.Growth Hormone: A polypeptide that is secreted by the adenohypophysis (PITUITARY GLAND, ANTERIOR). Growth hormone, also known as somatotropin, stimulates mitosis, cell differentiation and cell growth. Species-specific growth hormones have been synthesized.Postmortem Changes: Physiological changes that occur in bodies after death.Troponin: One of the minor protein components of skeletal muscle. Its function is to serve as the calcium-binding component in the troponin-tropomyosin B-actin-myosin complex by conferring calcium sensitivity to the cross-linked actin and myosin filaments.Gene Expression: The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Immunohistochemistry: Histochemical localization of immunoreactive substances using labeled antibodies as reagents.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Diet: Regular course of eating and drinking adopted by a person or animal.Dogs: The domestic dog, Canis familiaris, comprising about 400 breeds, of the carnivore family CANIDAE. They are worldwide in distribution and live in association with people. (Walker's Mammals of the World, 5th ed, p1065)Contractile Proteins: Proteins which participate in contractile processes. They include MUSCLE PROTEINS as well as those found in other cells and tissues. In the latter, these proteins participate in localized contractile events in the cytoplasm, in motile activity, and in cell aggregation phenomena.Muscle Stretching Exercises: Exercises that stretch the muscle fibers with the aim to increase muscle-tendon FLEXIBILITY, improve RANGE OF MOTION or musculoskeletal function, and prevent injuries. There are various types of stretching techniques including active, passive (relaxed), static, dynamic (gentle), ballistic (forced), isometric, and others.Ubiquitins: A family of proteins that are structurally-related to Ubiquitin. Ubiquitins and ubiquitin-like proteins participate in diverse cellular functions, such as protein degradation and HEAT-SHOCK RESPONSE, by conjugation to other proteins.PhosphoproteinsMuscle Rigidity: Continuous involuntary sustained muscle contraction which is often a manifestation of BASAL GANGLIA DISEASES. When an affected muscle is passively stretched, the degree of resistance remains constant regardless of the rate at which the muscle is stretched. This feature helps to distinguish rigidity from MUSCLE SPASTICITY. (From Adams et al., Principles of Neurology, 6th ed, p73)

Regulation of chamber-specific gene expression in the developing heart by Irx4. (1/8990)

The vertebrate heart consists of two types of chambers, the atria and the ventricles, which differ in their contractile and electrophysiological properties. Little is known of the molecular mechanisms by which these chambers are specified during embryogenesis. Here a chicken iroquois-related homeobox gene, Irx4, was identified that has a ventricle-restricted expression pattern at all stages of heart development. Irx4 protein was shown to regulate the chamber-specific expression of myosin isoforms by activating the expression of the ventricle myosin heavy chain-1 (VMHC1) and suppressing the expression of the atrial myosin heavy chain-1 (AMHC1) in the ventricles. Thus, Irx4 may play a critical role in establishing chamber-specific gene expression in the developing heart.  (+info)

Gamma-Actinin, a new regulatory protein from rabbit skeletal muscle. I. Purification and characterization. (2/8990)

A new regulatory protein which we have designated as gamma-actinin has been isolated from native thin filaments of rabbit skeletal muscle. Depolymerized native thin filaments were fractionated by salting out with ammonium sulfate, and the precipitates obtained at 40--60% ammonium sulfate saturation were further subjected to DEAE-Sephadex and Sephadex G-200 column chromatography. The purified gamma-actinin was shown to have a chain weight of 35,000 daltons and had a strong inhibitory action on the polymerization of G-actin. The results of amino acid analysis indicated a unique amino acid composition of gamma-actinin as compared with other structural proteins of muscle. Non-polar and neutral amino acid residues were abundant. One cysteine residue was contained per one molecule of gamma-actinin and played a critical role in the maintenance of the inhibitory activity. Pelleting of gamma-actinin with F-actin showed that gamma-actinin binds to F-action.  (+info)

Connectin, an elastic protein from myofibrils. (3/8990)

The elastic protein isolated from myofibrils of chicken skeletal muscle was compared with extracellular non-collagenous reticulin prepared from chicken liver and skeletal muscle. The amino acid compositions of these proteins were similar except that their contents of Phe, Leu, Cys/2, and Hyp were different. The impregnations of the elastic protein and reticulin with silver were also different. The reticulin was not at all elastic. It also differed from reticulin in solubility and antigenicity. It is proposed to call the intracellular elastic protein connectin.  (+info)

Model-independent analysis of the orientation of fluorescent probes with restricted mobility in muscle fibers. (4/8990)

The orientation of proteins in ordered biological samples can be investigated using steady-state polarized fluorescence from probes conjugated to the protein. A general limitation of this approach is that the probes typically exhibit rapid orientational motion ("wobble") with respect to the protein backbone. Here we present a method for characterizing the extent of this wobble and for removing its effects from the available information about the static orientational distribution of the probes. The analysis depends on four assumptions: 1) the probe wobble is fast compared with the nanosecond time scale of its excited-state decay; 2) the orientational distributions of the absorption and emission transition dipole moments are cylindrically symmetrical about a common axis c fixed in the protein; 3) protein motions are negligible during the excited-state decay; 4) the distribution of c is cylindrically symmetrical about the director of the experimental sample. In a muscle fiber, the director is the fiber axis, F. All of the information on the orientational order of the probe that is available from measurements of linearly polarized fluorescence is contained in five independent polarized fluorescence intensities measured with excitation and emission polarizers parallel or perpendicular to F and with the propagation axis of the detected fluorescence parallel or perpendicular to that of the excitation. The analysis then yields the average second-rank and fourth-rank order parameters ( and ) of the angular distribution of c relative to F, and and , the average second-rank order parameters of the angular distribution for wobble of the absorption and emission transition dipole moments relative to c. The method can also be applied to other cylindrically ordered systems such as oriented lipid bilayer membranes and to processes slower than fluorescence that may be observed using longer-lived optically excited states.  (+info)

Aging-specific expression of Drosophila hsp22. (5/8990)

hsp22 is among the least abundantly expressed Drosophila heat shock (hs) genes during both development and heat stress. In contrast, hsp22 was found to be the most abundantly expressed hs gene during Drosophila aging. During aging, hsp22 RNA was induced 60-fold in the head, with somewhat lower level induction in abdomen and thorax. Induction of the other hs gene RNAs was 150-fold, with particularly abundant expression in eye tissue. Aging-specific induction of hsp22 was reproduced by hsp22:lacZ fusion reporter constructs in transgenic flies. Analysis of specific promoter mutations in transgenic flies indicated that functional heat shock response elements are required for hsp22 induction during aging. Finally, comparison of hsp22 RNA and protein expression patterns suggests that aging-specific expression of hsp22 is regulated at both the transcriptional and the posttranscriptional levels. Aging-specific induction of hsp22 is discussed with regard to current evolutionary theories of aging.  (+info)

SNAP-23 participates in SNARE complex assembly in rat adipose cells. (6/8990)

SNARE proteins are required for vesicle docking and fusion in eukaryotic cells in processes as diverse as homotypic membrane fusion and synaptic vesicle exocytosis [SNARE stands for SNAP receptor, where SNAP is soluble NSF attachment protein]. The SNARE proteins syntaxin 4 and vesicle-associated membrane protein (VAMP) 2/3 also participate in the insulin-stimulated translocation of GLUT4 from intracellular vesicles to the plasma membrane in adipose cells. We now report the molecular cloning and characterization of rat SNAP-23, a ubiquitously expressed homologue of the essential neuronal SNARE protein SNAP-25 (synaptosomal-associated protein of 25 kDa). Rat SNAP-23 is 86% and 98% identical respectively to human and mouse SNAP-23. Southern blot analysis reveals that the rat, mouse and human SNAP-23 genes encode species-specific isoforms of the same protein. Co-immunoprecipitation of syntaxin 4 and SNAP-23 shows association of these two proteins in rat adipose cell plasma membranes, and insulin stimulation does not alter the SNAP-23/syntaxin 4 complex. In addition, we demonstrate for the first time the participation of SNAP-23, along with syntaxin 4 and VAMP2/3, in the formation of 20S SNARE complexes prepared using rat adipose cell membranes and recombinant alpha-SNAP and NSF proteins. The stoichiometry of the SNARE complexes formed is essentially identical using membranes from either unstimulated or insulin-stimulated adipose cells. These data demonstrate that rat SNAP-23 associates with syntaxin 4 before insulin stimulation and is present in the SNARE complexes known to mediate the translocation of GLUT4 from intracellular vesicles to the plasma membrane of rat adipose cells.  (+info)

Tumour necrosis factor-alpha regulates expression of the CCAAT-enhancer-binding proteins (C/EBPs) alpha and beta and determines the occupation of the C/EBP site in the promoter of the insulin-responsive glucose-transporter gene in 3T3-L1 adipocytes. (7/8990)

We have demonstrated previously that treatment of 3T3-L1 adipocytes with tumour necrosis factor-alpha (TNF) results in a rapid (4 h) and significant (75-80%) reduction in the rate of transcription of the GLUT4 gene. Control of GLUT4 gene transcription has been suggested at least in part to reside with the CCAAT-enhancer-binding protein (C/EBP) family (alpha, beta and delta isoforms) of transcription factors. Using electrophoretic mobility shift assays, we have examined the ability of TNF to alter the occupation of the C/EBP site in the GLUT4 promoter. The data suggest that in fully differentiated adipocytes the C/EBP site is a ligand for predominantly alpha/alpha homodimers; however, after exposure to TNF, a shift in occupancy of the site occurs and the ligands become alpha/beta heterodimers and beta/beta homodimers. Partner selection in dimer formation appears to be controlled by selective translocation of the beta-isoform from the cytosol to the nucleus after exposure of the cells to TNF.  (+info)

Intestinal trefoil factor binds to intestinal epithelial cells and induces nitric oxide production: priming and enhancing effects of mucin. (8/8990)

Intestinal trefoil factor (ITF or TFF3), NO and epithelium-associated mucin have important roles in sustaining mucosal integrity in the gastrointestinal tract. In the present study we examined ITF-binding molecules on IEC-18 cells (an intestinal epithelial cell line) with the use of flow cytometry and localized these molecules on the cell surface by confocal microscopy. Furthermore, we studied the interaction of mucin and ITF and their co-operative effect on NO production by the epithelium. Stimulation of cells with mucin (5 mg/ml) for 90 min resulted in a 5-fold increase in ITF binding. Treatment of IEC-18 cells with actinomycin D or cycloheximide attenuated mucin-enhanced ITF binding. Ligand blot analysis confirmed the induction of ITF-binding protein in IEC-18 cells by mucin. These results indicate that transcriptional and translational mechanisms are involved in the effect of mucin. Treatment with ITF overnight resulted in a low level of nitrite production by the cells, a 5-fold increase over control, in a concentration-dependent manner. ITF-induced NO production was attenuated by 1400W, a selective type II nitric oxide synthase (NOS2) inhibitor. By immunoblotting we found that NOS2 was up-regulated by ITF treatment. Priming IEC-18 cells with mucin for 90 min enhanced the effect of ITF on NO production, suggesting that the up-regulation of ITF-binding molecules by mucin might be physiologically relevant. Taken together, these observations indicate (1) that ITF-binding molecules that are up-regulated by mucin exist on the intestinal epithelial surface, and (2) that ITF modulates epithelial NO production via the NOS2 pathway, which is enhanced by mucin.  (+info)

Preservation of skeletal muscle mass is of great importance for maintaining both metabolic health and functional capacity. Muscle mass maintenance is regulated by the balance between muscle protein breakdown and synthesis rates. Both muscle protein breakdown and synthesis rates have been shown to be highly responsive to physical activity and food intake. Food intake, and protein ingestion in particular, directly stimulates muscle protein synthesis rates. The postprandial muscle protein synthetic response to feeding is regulated on a number of levels, including dietary protein digestion and amino acid absorption, splanchnic amino acid retention, postprandial insulin release, skeletal muscle tissue perfusion, amino acid uptake by muscle, and intramyocellular signaling. The postprandial muscle protein synthetic response to feeding is blunted in many conditions characterized by skeletal muscle loss, such as aging and muscle disuse. Therefore, it is important to define food characteristics that modulate
Purpose: Erythropoietin (EPO) is a renal cytokine that is primarily involved in hematopoiesis while also playing a role in non-hematopoietic tissues expressing the EPO-receptor (EPOR). The EPOR is present in human skeletal muscle. In mouse skeletal muscle, EPO stimulation can activate the AKT serine/threonine kinase 1 (AKT) signaling pathway, the main positive regulator of muscle protein synthesis. We hypothesized that a single intravenous EPO injection combined with acute resistance exercise would have a synergistic effect on skeletal muscle protein synthesis via activation of the AKT pathway.Methods: Ten young (24.2 ± 0.9 years) and 10 older (66.6 ± 1.1 years) healthy subjects received a primed, constant infusion of [ring-13C6] L-phenylalanine and a single injection of 10,000 IU epoetin-beta or placebo in a double-blind randomized, cross-over design. 2 h after the injection, the subjects completed an acute bout of leg extension resistance exercise to stimulate skeletal muscle protein synthesis
TY - JOUR. T1 - Rapamycin administration in humans blocks the contraction-induced increase in skeletal muscle protein synthesis. AU - Drummond, Micah J.. AU - Fry, Christopher. AU - Glynn, Erin L.. AU - Dreyer, Hans C.. AU - Dhanani, Shaheen. AU - Timmerman, Kyle L.. AU - Volpi, Elena. AU - Rasmussen, Blake. PY - 2009. Y1 - 2009. N2 - Muscle protein synthesis and mTORC1 signalling are concurrently stimulated following muscle contraction in humans. In an effort to determine whether mTORC1 signalling is essential for regulating muscle protein synthesis in humans, we treated subjects with a potent mTORC1 inhibitor (rapamycin) prior to performing a series of high-intensity muscle contractions. Here we show that rapamycin treatment blocks the early (1-2 h) acute contraction-induced increase (∼40%) in human muscle protein synthesis. In addition, several downstream components of the mTORC1 signalling pathway were also blunted or blocked by rapamycin. For instance, S6K1 phosphorylation (Thr421/Ser424) ...
Age-related muscle wasting (sarcopenia) is accompanied by a loss of strength which can compromise the functional abilities of the elderly. Muscle proteins are in a dynamic equilibrium between their respective rates of synthesis and breakdown. It has been suggested that age-related sarcopenia is due to: i) elevated basal-fasted rates of muscle protein breakdown, ii) a reduction in basal muscle protein synthesis (MPS), or iii) a combination of the two factors. However, basal rates of muscle protein synthesis and breakdown are unchanged with advancing healthy age. Instead, it appears that the muscles of the elderly are resistant to normally robust anabolic stimuli such as amino acids and resistance exercise. Ageing muscle is less sensitive to lower doses of amino acids than the young and may require higher quantities of protein to acutely stimulate equivalent muscle protein synthesis above rest and accrue muscle proteins. With regard to dietary protein recommendations, emerging evidence suggests ...
BACKGROUND. Systemic inflammation and muscle wasting are highly prevalent and coexist in patients on maintenance hemodialysis (MHD). We aimed to determine the effects of systemic inflammation on skeletal muscle protein metabolism in MHD patients. METHODS. Whole body and skeletal muscle protein turnover were assessed by stable isotope kinetic studies. We incorporated expressions of E1, E214K, E3αI, E3αII, MuRF-1, and atrogin-1 in skeletal muscle tissue from integrin β1 gene KO CKD mice models. RESULTS. Among 129 patients with mean (± SD) age 47 ± 12 years, 74% were African American, 73% were male, and 22% had diabetes mellitus. Median high-sensitivity C-reactive protein (hs-CRP) concentration was 13 (interquartile range 0.8, 33) mg/l. There were statistically significant associations between hs-CRP and forearm skeletal muscle protein synthesis, degradation, and net forearm skeletal muscle protein balance (P , 0.001 for all). The associations remained statistically significant after ...
BACKGROUND: The progressive loss of skeletal muscle mass with aging is attributed to a disruption in the regulation of skeletal muscle protein turnover. OBJECTIVE: We investigated the effects on whole-body protein balance and mixed-muscle protein synthesis rates of the ingestion of carbohydrate with or without protein and free leucine after simulated activities of daily living. DESIGN: Eight elderly (75 +/- 1 y) and 8 young (20 +/- 1 y) lean men were randomly assigned to 2 crossover experiments in which they consumed either carbohydrate (CHO) or carbohydrate plus protein and free leucine (CHO+Pro+Leu) after performing 30 min of standardized activities of daily living. Primed, continuous infusions with L-[ring-13C6]phenylalanine and L-[ring-2H2]tyrosine were applied, and blood and muscle samples were collected to assess whole-body protein turnover and the protein fractional synthetic rate in the vastus lateralis muscle over a 6-h period. RESULTS: Whole-body phenylalanine and tyrosine flux were ...
An abundant supply of amino acids enhances the metabolic effect of exercise on muscle protein. Am. J. Physiol. 273 (Endocrinol. Metab. 36): El22-E129, 1997. -Six normal untrained men were studied during the intravenous infusion of a balanced amino acid mixture (-0.15 g. kg-l. h-l for 3 h) at rest and after a leg resistance exercise routine to test the influence of exercise on the regulation of muscle protein kinetics by hyperaminoacidemia. Leg muscle protein kinetics and transport of selected amino acids (alanine, phenylalanine, leucine, and lysine) were isotopically determined using a model based on arteriovenous blood samples and muscle biopsy. The intravenous amino acid infusion resulted in comparable increases in arterial amino acid concentrations at rest and after exercise, whereas leg blood flow was 64 +/- 5% greater after exercise than at rest. During hyperaminoacidemia, the increases in amino acid transport above basal were 30-100% greater after exercise than at rest. Increases in muscle ...
We have previously shown that non-specific blockade of the cyclooxygenase (COX) enzymes in skeletal muscle eliminates the normal increase in muscle protein synthesis following resistance exercise. The current study tested the hypothesis that this COX-mediated increase in postexercise muscle protein synthesis is specifically regulated by the COX-2 isoform. Sixteen males (23 ± 1 yr, 177 ± 2 cm, 81.5 ± 3.4 kg) were randomly assigned to one of two groups that received three doses of either a specific COX-2 inhibitor (celecoxib; 200 mg per dose, 600 mg total) or a placebo during the 24 hours following a single bout of resistance exercise with the knee extensors. Skeletal muscle fractional synthesis rate (FSR) was measured at rest and 24 hours postexercise using a primed constant infusion of [2H5]phenylalanine coupled with muscle biopsies of the vastus lateralis. Mixed muscle FSR was increased following exercise to a greater extent (206%, P,0.05) in the COX-2 group (0.052 ± 0.014 %Ih) as compared ...
There were 2 primary goals of this work. The first was to develop a minimally invasive method for measuring integrated rates of skeletal muscle protein synthesis over a period of days to weeks based on a single blood measurement - i.e., without the need for a physical sample of the tissue. Muscle biopsies are not likely to be widely used in the clinical setting, so a blood test of muscle protein synthesis rates that could be monitored over time would be attractive for drug development, as well as clinical management of disorders of muscle, including sarcopenia and cachexia. Because changes in muscle protein synthesis rates have been shown to occur rapidly in response to anabolic therapies and to predict subsequent changes in muscle mass, strength, and performance (5, 8-10), the availability of a blood test for skeletal muscle protein synthesis rates would greatly simplify translational drug development and monitoring of treatment efficacy in this growing, unmet medical need.. We describe here an ...
It is thought that the production of muscle protein after a meal in response to consuming protein and/or amino acids is impaired in the elderly compared to the young. Also, consuming carbohydrates at the same time increases secretion of the hormone insulin and increases muscle protein production in the young. However, it is unclear how the elderly respond to the combined intake of protein and carbohydrates. Likewise, consuming the amino acid leucine may also increase muscle protein production. Adding carbohydrate or leucine to protein may represent effective strategies to overcome the impaired muscle protein production in the elderly. This study consists of three substudies. The aim of the first study is to determine if the response to combined protein and carbohydrate intake is different between young and elderly men. The aim of the second study is to investigate whether consuming carbohydrate as well increases muscle protein production in elderly men. The aim of the third study is to examine ...
Victor R. Preedy, James Keating, Timothy J. Peters; Ethanol-Induced Reductions in Skeletal Muscle Protein Synthesis in the Rat in Vivo. Clin Sci (Lond) 1 October 1990; 79 (s23): 7P. doi: https://doi.org/10.1042/cs079007P. Download citation file:. ...
The purpose of this investigation was to examine the effects of training either once or three times/day on the principal stages of skeletal muscle. The experiments were carried out on male albino rats fed either 3 or 5 times/day a diet containing 20% protein. Experimental animals swam either once or 3 times/day, 6 days/week for 10 weeks with weights attached. The total duration of daily activity was equal for both groups and at 10 weeks each animal was swimming for 60 min/day with 3% of his body weight attached. All the animals were examined at rest after the 10-week training programs. The adequacy of the weight-loading and training schedules was estimated by body weight dynamics and such energy metabolites as creatine phosphate and glycogen. Skeletal muscle RNA and protein synthesis were studied by means of 14C-orotic acid and 14C-leucine incorporation, respectively. Quadriceps and gastrocnemius muscles were used for analysis in all experiments. It was found that the increase in the number of daily
Optimal muscle protein synthesis requires a pulsatile increase in branch-chain amino acids (particularly leucine) with or without concomitant pulses in insulin levels. Pancreatic substrate clamp studies have demonstrated that insulin and branch-chain amino acids independently increase muscle synthesis with the effects of both being additive [45, 46]. Animal data demonstrates that muscle protein synthesis following a meal is rapid (within 30 min) and sustained for about 2 h but then declines toward baseline in parallel with the postprandial changes in circulating insulin and amino acids [34, 47]. Bohe and colleagues measured the latency and duration of the stimulation of human muscle protein synthesis during a continuous infusion of amino acids [48]. The rate of muscle protein synthesis increased after 30 min and reached a peak at 2 h rapidly returning to basal levels by 4 h despite continuous amino acid availability. In healthy individuals at rest, muscle protein synthesis displays a saturable ...
Insulin action on muscle protein kinetics and amino acid transport during recovery after resistance exercise. Biolo, Gianni; Williams, Bradley D.; Fleming, R.Y. Declan; Wolfe, Robert R. // Diabetes;May99, Vol. 48 Issue 5, p949 Determines the role of insulin on muscle protein kinetics and amino acid transport after heavy resistance exercise. Effect of insulin infusion on plasma insulin and glucose concentrations; Rate of muscle protein synthesis and degradation during hyperinsulinemia at rest and after exercise; Amino... ...
Abstracts of the Eighth European Conference on Muscle and Motility including the Erwin Riesch Symposium on Muscle Proteins - Polymorphism and Isoforms Heidelberg, 17-20 September ...
Sarcopenia is a well-known phenomenon in elderly individuals and resistance exercise together with sufficient amino acid (AA) availability has proved to be a counteractive implement. However, the source of AA and supplement timing require further investigation. The objective was to compare muscle protein synthesis (MPS) to intakes of whey and caseinate after heavy resistance exercise in healthy elderly individuals, and, furthermore, to compare the timing effect of caseinate intake. Twenty-four elderly men and women (mean ± SEM; 68 ± 1 years) were randomized to one of four groups: caseinate intake before exercise (CasPre), caseinate intake immediately after exercise (CasPost), whey intake immediately after exercise (Whey), or intake of a non-caloric control drink (Control). Muscle myofibrillar and collagen fractional synthesis rates (FSR) were measured by a primed continuous infusion of l-[1-13C]leucine using labeled proteins during a 6-h recovery period. No differences were observed in muscle ...
I think its fair to say that there are very few players who are not actively looking to increase their muscle mass or improve their body composition. Research suggests that additional muscle mass can improve the predicted success in some team sports such as rugby1. Building muscle is a multi-faceted approach and the following 3 tips will help you maximise those gains and improve performance.. Tip #1 - Engage in resistance training. Resistance Training (RT) is the single most important factor in building muscle. During RT muscle fibres are broken down and muscle protein synthesis (MPS) is increased. However, although MPS is increased, supporting nutrition in the form of protein is needed in order to ensure MPS is greater than muscle protein breakdown (MPB) and muscle grows. There is no change in muscle growth after one RT session but instead muscle hypertrophy is due to the accumulation of muscle protein in response to each individual bout of RT training plus protein that occurs ...
If patients could recognise themselves, or anyone else could recognise a patient from your description, please obtain the patients written consent to publication and send them to the editorial office before submitting your response [Patient consent forms] ...
Purpose: We have previously shown that the aminoacidemia caused by the consumption of a rapidly digested protein after resistance exercise enhances muscle protein synthesis (MPS) more than the amino acid (AA) profile associated with a slowly digested protein. Here, we investigated whether differential feeding patterns of a whey protein mixture commencing before exercise affect postexercise intracellular signaling and MPS. Methods: Twelve resistance-trained males performed leg resistance exercise 45 min after commencing each of three volume-matched nutrition protocols: placebo (PLAC, artificially sweetened water), BOLUS (25 g of whey protein + 5 g of leucine dissolved in artificially sweetened water; 1× 500 mL), or PULSE (15× 33-mL aliquots of BOLUS drink every 15 min). Results: The preexercise rise in plasma AA concentration with PULSE was attenuated compared with BOLUS (P less than 0.05); this effect was reversed after exercise, with two-fold greater leucine concentrations in PULSE compared ...
It turns out that only slight elevations of insulin above basal levels are all thats required to blunt muscle catabolic effects. Just consuming protein alone is enough to elicit a release of insulin that is sufficient to interact with the ingested amino acids in promoting muscle protein synthesis. Leucine alone is known to promote the release of insulin. This explains the recent studies showing that protein alone is enough to boost muscle protein synthesis following training. Indeed, one study showed that boosting insulin levels 30-times above fasting level did not further boost muscle protein synthesis if blood levels of amino acids were high. Just consuming protein alone, especially whey, which is rich in leucine, is enough to boost insulin levels 2-3-fold above resting levels. This level of insulin alone is enough to provide the anti-catabolic effects of insulin following exercise. Other studies show that adding 30 or 90 grams of carbs to 20 grams of protein does not boost muscle protein ...
Save 32% CytoSport - Muscle Milk Banana Creme 2.47 Pounds Muscle Milk Protein Powder Everyday Performance 310 Calories Per 2 Scoops 32g Protein Per 2 Scoops 20 Vitamins & Minerals Free of Banned Substances Gluten Free The Power of Protein Protein you eat breaks down into amino acids in the body, which support muscle growth, repair and maintenance Consuming both fast and slow release proteins, like those found in Muscle Milk Protein Powder, keeps your body in positive protein balance Protein after exercise aids in recovery and helps build lean muscle 32 Grams of Protein --Build lean muscles --Recover after exercise 20 Vitamins & Minerals --Antioxidant vitamins A, C and E --Vitamin D, Calcium, Magnesium and Phosphorus for strong bones BCAA (Branched Chain Amino Acids) --Leucine, Isoleucine, Valine help support muscle maintenance and growth --Leucine triggers muscle protein growth and helps prevent muscle protein breakdown. Protein Comparisons 2 Scoops of Muscle Milk = 4 Jumbo Eggs 2 Scoops of Muscle Milk
Save 32% CytoSport - Muscle Milk Cake Batter 2.47 Pounds Muscle Milk Protein Powder Everyday Performance 310 Calories Per 2 Scoops 32g Protein Per 2 Scoops 20 Vitamins & Minerals Free of Banned Substances Gluten Free The Power of Protein Protein you eat breaks down into amino acids in the body, which support muscle growth, repair and maintenance Consuming both fast and slow release proteins, like those found in Muscle Milk Protein Powder, keeps your body in positive protein balance Protein after exercise aids in recovery and helps build lean muscle 32 Grams of Protein --Build lean muscles --Recover after exercise 20 Vitamins & Minerals --Antioxidant vitamins A, C and E --Vitamin D, Calcium, Magnesium and Phosphorus for strong bones BCAA (Branched Chain Amino Acids --Leucine, Isoleucine, Valine help support muscle maintenance and growth --Leucine triggers muscle protein growth and helps prevent muscle protein breakdown. Protein Comparisons 2 Scoops of Muscle Milk = 4 Jumbo Eggs 2 Scoops of Muscle Milk =
Muscle protein synthesis is stimulated by resistance training and protein intake. Muscle growth is the outcome of effective MPS response in our body.
Autor: Schraders, M. et al.; Genre: Zeitschriftenartikel; Im Druck veröffentlicht: 2011; Keywords: Adolescent; Adult; Child; Child, Preschool; *Codon, Nonsense; DNA Mutational Analysis; Female; Frameshift Mutation; *Genes, X-Linked; Hearing Loss/*genetics/pathology; Humans; Insulin-Like Growth Factor I/genetics; Male; Middle Aged; Molecular Sequence Annotation; Muscle Proteins/*genetics; Pedigree; Polymorphism, Single Nucleotide; Sequence Analysis; Young Adult; Titel: Next-generation sequencing identifies mutations of SMPX, which encodes the small muscle protein, X-linked, as a cause of progressive hearing impairment
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Resistance coaching and subsequent intake of a protein-rich food encourages muscle mass hypertrophy and gains in muscle mass toughness by stimulating myofibrillar muscle protein synthesis (MPS) and inhibiting muscle protein breakdown (MPB).[108][109] The stimulation of muscle mass protein synthesis by resistance education happens by means of phosphorylation in the mechanistic target of rapamycin (mTOR) and subsequent activation of mTORC1, which ends up in protein biosynthesis while in the ribosome by means of phosphorylation of mTORC1s speedy targets (the p70S6 kinase and the translation repressor protein 4EBP1 ...
Resistance schooling and subsequent usage of the protein-loaded meal promotes muscle mass hypertrophy and gains in muscle mass power by stimulating myofibrillar muscle mass protein synthesis (MPS) and inhibiting muscle protein breakdown (MPB).[108][109] The stimulation of muscle protein synthesis by resistance schooling takes place through phosphorylation in the mechanistic concentrate on of rapamycin (mTOR) and subsequent activation of mTORC1, which results in protein biosynthesis within the ribosome by means of phosphorylation of mTORC1s quick targets (the p70S6 kinase and the translation repressor protein 4EBP1 ...
Bioactive peptides have been identified in a range of foods, including plant, milk and muscle, e.g., beef, chicken, pork and fish muscle proteins. Bioactive peptides from food proteins offer major potential for incorporation into functional foods and nutraceuticals. The aim of this paper is to present an outline of the bioactive peptides identified in the muscle protein of meat to date, with a focus on muscle protein from domestic animals and fish. The majority of research on bioactives from meat sources has focused on angiotensin-1-converting enzyme (ACE) inhibitory and antioxidant peptides.
Bioactive peptides have been identified in a range of foods, including plant, milk and muscle, e.g., beef, chicken, pork and fish muscle proteins. Bioactive peptides from food proteins offer major potential for incorporation into functional foods and nutraceuticals. The aim of this paper is to present an outline of the bioactive peptides identified in the muscle protein of meat to date, with a focus on muscle protein from domestic animals and fish. The majority of research on bioactives from meat sources has focused on angiotensin-1-converting enzyme (ACE) inhibitory and antioxidant peptides.
Sarcopenia seems to be attributed to a blunted muscle protein synthetic response to food intake and exercise. This blunted response could be the result of impaired protein digestion and absorption kinetics and lead to lower postprandial plasma amino acid availability.
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Its all about Amino Acids Skeletal muscle actively collaborates and participates in all amino acid exchanges with other tissues throughout the body, both at re
Muscle proteinsynthesis, as you already know, is required to construct muscle tissue. When ample leverageis created and sustained, these elements loosen their grip, permitting proteinsynthesis to consider off.* Subsequently, this promotes more substantial, far more immediate gains inmuscle mass, toughness, tone and definition.* BI will not be conscious of any othercompany that manufactures a protein powder with this type of substantial written content of MPI. MPIhas been often called the "leverage protein" for its capability to aid highanabolic leverage ...
Building muscle after 40 is definitely possible. In fact, you can still achieve the same level of muscle protein synthesis as someone in their 20s, however...
Since 1995, no-one has become in a position to duplicate MPs delectable flavor method or recognize its exact contents. Created by the labs R&D workforce around the course of not less than 5 time- and labor-intense rounds of audits, the flavor method is uncommon in many regards. By way of example, Whilst other protein nutritional supplements consist of added "filler" substances in order to handle flavor, texture and/or mixability difficulties, BI has preferred to conquer these challenges by introducing far more large-top quality proteins particularly combos ...
Produktbeschreibung: Milchmischgetränk aus Magermilch mit Zusatz von Milcheiweiß und Kohlenhydraten und einer Zuckerart Empfohlene Trainingsphasen: Muskelaufbauphase Kraftphase Definitionsphase (als Post-Workout Drink) Produkteigenschaften: liefert mehr Protein als Kohlenhydrate Proteine tragen zu einer Zunahme an Muskelmasse bei* ideal als Shake zwischendurch für alle aktiven Sportler Zufuhrempfehlung: 1 Flasche täglich Inhalt: 500 ml Dunkel lagern. Zutaten (Allergene…
Remember how we mentioned BCAA consists of three components of amino acids? Two of it, namely isoleucine and valine, are directly capable of producing energy and regulating blood sugar levels. Like we mentioned earlier, these amino acids do not metabolize in the liver but are instead broken down in your muscle itself, thus proving its significance in producing energy. This makes BCAA ideal for intense workouts because it will be used as an additional source of energy to keep your body fueled and going without tiring you out. These amino acids are also able to increase and preserve better your storage of glycogen, the component that keeps your body fueled and energized. All in all, BCAA helps fuel your body during intense workouts, prevents the breakdown of muscle protein while doing so, and preserves your bodys storage of glycogen. 2. Increases muscle growth. Consuming BCAA supplements will not only help speed up your muscle growth, but also protect and preserve your muscle mass. This links ...
Alcohol can hinder muscle growth by inhibiting muscle protein synthesis, and sports drinks - although beneficial in replacing lost micronutrients after hard training sessions that last an hour or longer - are often guilty of providing more calories, sodium, and sugar that the body needs. "Ive always enjoyed a big glass of water," he admits. "Every so often I have a sweet tea, but I know thats not great for me so I try not to drink a lot of it. I dont drink much alcohol. Nothing against it, but with my lifestyle, Im not around it. A big night for me is getting kids ready for bed and watching some TV ...
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The rest of the paper argues why this is the case on scaling grounds. They care about deriving this constant relationship, and estimating its magnitude (body-lengths-per-second), not exactly but to within a factor of ten.. They argue that that the moving speed is determined by three features shared universally among moving organisms. The first is that because all life forms are mostly water and more-or-less buoyant, they have roughly the density of water, 1 kg/L. The second is that all motility is caused by the contraction of muscle proteins that have a similar structure across all life-forms. Based on the non-covalent binding energy of these proteins and their diameter, the force-per-unit-area they can exert is roughly 20,000 N/m2. Could a square-meter cross section of muscle support two tons? Im picturing an elephant leg and I can believe it. The final feature is the metabolic rate per unit mass, which is related to an organisms ability to transfer heat across its surface. The paper states ...
1. Quadriceps muscle protein turnover was assessed in the post-absorptive state in six men immediately after the end of unilateral leg immobilization (37 ± 4 days) in a plaster cast after tibial fracture. A primed-constant intravenous infusion of l-[1-13C]leucine was administered over 7 h. Quadriceps needle biopsies, taken bilaterally at the end of the infusion, were analysed for muscle protein leucine enrichment with 13C.. 2. Quadriceps muscle protein synthetic rate, calculated from the fractional incorporation of [13C]leucine into protein compared with the average enrichment of blood α-ketoisocaproate, was 0.046 ±0.012%/h in the uninjured leg, but was only 0.034 ±0.007%/h in the quadriceps of the previously fractured leg (P , 0.05, means ± sd).. 3. Muscle RNA activity (i.e. protein synthetic rate per RNA) fell from 0.27 ±0.08 μg of protein synthesized h−1 μg−1 of RNA in the control leg to 0.14 ±0.03 μg of protein synthesized h−1 μg−1 of RNA in the immobilized leg (P , ...
Author: Mller, Rikke S. et al.; Genre: Journal Article; Published in Print: 2008-04-16; Title: Truncation of the Down syndrome candidate gene DYRK1A in two unrelated patients with microcephaly
Due to insufficient exercise training, skeletal mucle loss is beginning form 25 years old. Sarcopenia is the critical reason to effect activities of daily life in seniors. Strength training has been proven to be a great strategy to increase mucle mass and functions. Exercise training provokes skeletal muscle protein synthesis, in the meantime also causes muscle injury, induces muscle protien degradation and muscle cell inflammatory. Net muscle protein balace will become negative in nutrients or rest deficiency. Muscle biogenesis decreasing with aging may induce by signal transmit weakening in muscle protein synthesis pathway. Current studies showed that the phosphatidylinositol 3-kinase /AKT/mammalian target of rapamycin (PI3K/Akt/ mTOR) pathway is an important pathway to regulate skeletal muscle hypertrophy. Therefore, the first year, resveratrol is uesd as a nutriental ergogenic aid which may activate related protein expression of muscle synthesis pathway. In order to understand promotion or ...
Ingestion of sufficient dietary protein is a fundamental prerequisite for muscle protein synthesis and maintenance of muscle mass and function. Elderly people are often at increased risk for protein-energy malnutrition, sarcopenia, and a diminished quality of life. This study sought to compare chang …
Rationale: The giant protein titin plays key roles in myofilament assembly and determines the passive mechanical properties of the sarcomere. The cardiac titin molecule has 2 mayor elastic elements, the N2B and the PEVK region. Both have been suggested to determine the elastic properties of the heart with loss of function data only available for the N2B region.. Objective: The purpose of this study was to investigate the contribution of titins proline-glutamate-valine-lysine (PEVK) region to biomechanics and growth of the heart.. Methods and Results: We removed a portion of the PEVK segment (exons 219 to 225; 282 aa) that corresponds to the PEVK element of N2B titin, the main cardiac titin isoform. Adult homozygous PEVK knockout (KO) mice developed diastolic dysfunction, as determined by pressure-volume loops, echocardiography, isolated heart experiments, and muscle mechanics. Immunoelectron microscopy revealed increased strain of the N2B element, a spring region retained in the PEVK-KO. ...
1. We have used l-[1-13C,15N]leucine as the substrate tracer to study leucine and muscle protein metabolism across the forearm of eight normal fasting adults.. 2. The rates of protein synthesis and breakdown, de- and re-amination of leucine, and the oxidative de-carboxylation of its keto acid were calculated directly from the arteriovenous metabolite balances and isotope dilutions as described by the metabolic model.. 3. The results were compared with those obtained previously when subjects were fed. The effects of fasting on protein and leucine metabolism were a significant decrease in protein synthesis from 127 (sem 11; n = 6) to 70 (sem 6; n = 12) nmol of leucine min−-1 100 ml−-1 of forearm tissue (P , 0.001) and a marked decrease in leucine catabolism in the forearm muscle.. 4. This model has demonstrated that each subject was in negative protein balance across the forearm during fasting while positive during feeding, the mean values being −29(sem 5; n = 12) and + 39(sem 9; n = 6) nmol ...
The peroxisome proliferator-activated receptor γ (PPARγ) agonist rosiglitazone (Rosi) appears to provide protection against organ dysfunction during endotoxaemia. We examined the potential benefits of Rosi on skeletal muscle protein maintenance and carbohydrate metabolism during lipopolysaccharide (LPS)-induced endotoxaemia. Sprague-Dawley rats were fed either standard chow (control) or standard chow containing Rosi (8.5±0.1 mg.kg-1.day-1) for two weeks before and during 24 h continuous intravenous infusion of LPS (15 μg.kg-1.h-1) or saline. Rosi blunted LPS-induced increases in muscle tumor necrosis factor-α (TNF-α) and interleukin-6 (IL-6) mRNA by 70% (P,0.05) and 64% (P,0.01), respectively. Furthermore, Rosi suppressed the LPS-induced reduction in phosphorylated AKT and phosphorylated Forkhead box O (FOXO) 1 protein, as well as the upregulation of muscle RING finger 1 (MuRF1; P,0.01) mRNA, and the LPS-induced increase in 20S proteasome activity (P,0.05). Accordingly, LPS reduced the ...
The active and passive contractile performance of skeletal muscle fibers largely depends on the myosin heavy chain (MHC) isoform and the stiffness of the titin spring, respectively. Open questions concern the relationship between titin-based stiffness and active contractile parameters, and titins importance for total passive muscle stiffness. Here, a large set of adult rabbit muscles (n = 37) was studied for titin size diversity, passive mechanical properties, and possible correlations with the fiber/MHC composition. Titin isoform analyses showed sizes between ∼3300 and 3700 kD; 31 muscles contained a single isoform, six muscles coexpressed two isoforms, including the psoas, where individual fibers expressed similar isoform ratios of 30:70 (3.4:3.3 MD). Gel electrophoresis and Western blotting of two other giant muscle proteins, nebulin and obscurin, demonstrated muscle type-dependent size differences of ≤70 kD. Single fiber and single myofibril mechanics performed on a subset of muscles ...
It is a protein found in the M-band of muscle sarcomeres in association with M-protein. It is found in both slow and fast ... muscle fibers while M-protein is only found in fast fibers. These proteins are thought to be involved in anchoring the thick ... "Muscle Proteins". Ohio State University. Retrieved December 9, 2010. Roman Schoenauer; Patricia Bertoncini; Gia Machaidze; Ueli ... Tskhovrebova, Larissa; Trinick, John (2012). "Making muscle elastic: the structural basis of myomesin stretching". PLoS Biology ...
... meaning muscle and "statin" meaning stop).[5] Myostatin is a protein that inhibits muscle development. This mutation also ... "double-muscling". The double-muscling phenotype is a heritable condition resulting in an increased number of muscle fibers ( ... resulting in accelerated lean muscle growth. Muscle growth is due primarily to physiological changes in the animal's muscle ... Because of this breed's increased muscle yield, a diet containing higher protein is required to compensate for the altered mode ...
Increase protein-muscle catabolism. *Anemia due to erythropoietin deficiency and shortened red-cell survival ...
Troponin C, skeletal muscle is a protein that in humans is encoded by the TNNC2 gene. Troponin (Tn), a key protein complex in ... "Entrez Gene: TNNC2 troponin C type 2 (fast)". Romero-Herrera AE, Castillo O, Lehmann H (1977). "Human skeletal muscle proteins ... The protein encoded by this gene is the Tn-C subunit. GRCh38: Ensembl release 89: ENSG00000101470 - Ensembl, May 2017 GRCm38: ... Gahlmann R, Wade R, Gunning P, Kedes L (1988). "Differential expression of slow and fast skeletal muscle troponin C. Slow ...
There are specific proteins expressed in cardiac muscle cells.[25][26] These are mostly associated with muscle contraction, and ... "pectinate muscle". The Free Dictionary. Retrieved 31 July 2016.. *^ "The human proteome in heart - The Human Protein Atlas". ... Other proteins expressed are MYH7 and LDB3 that are also expressed in skeletal muscle.[27] ... As they are almost entirely muscle, they are high in protein. They are often included in dishes with other offal, for example ...
"Entrez Gene: TNNC1 troponin C type 1 (slow)". "Troponin C, slow skeletal and cardiac muscles". Cardiac Organellar Protein Atlas ... Kretsinger RH, Nockolds CE (May 1973). "Carp muscle calcium-binding protein. II. Structure determination and general ... is a protein that resides in the troponin complex on actin thin filaments of striated muscle (cardiac, fast-twitch skeletal, or ... In cardiac muscle, cTnC binds to cardiac troponin I (cTnI) and cardiac troponin T (cTnT), whereas cTnC binds to slow skeletal ...
... is a protein that in humans is encoded by the DES gene.[5][6] Desmin is a muscle-specific, type III[7] intermediate ... skeletal muscle and smooth muscle tissue.[13] In cardiac muscle, desmin is present in Z-discs and intercalated discs. Desmin ... Desmin is one of the earliest protein markers for muscle tissue in embryogenesis as it is detected in the somites.[12] Although ... identical protein binding. • structural molecule activity. • cytoskeletal protein binding. Cellular component. • intercalated ...
The sarcoplasm is the cytoplasm of a muscle fiber. Most of the sarcoplasm is filled with myofibrils, which are long protein ... and not cardiac muscle or smooth muscle. Myoblasts in skeletal muscle that do not form muscle fibers dedifferentiate back into ... The striated cells of cardiac and skeletal muscles are referred to as muscle fibers.[3] Cardiomyocytes are the muscle fibres ... Muscle fiber growth[edit]. Muscle fibers grow when exercised and shrink when not in use. This is due to the fact that exercise ...
Putney SD; Herlihy WC; Schimmel P (1983). "A new troponin T and cDNA clones for 13 different muscle proteins, found by shotgun ... who sequenced 178 clones from a rabbit muscle cDNA library.[7] In 1991 Adams and co-workers coined the term expressed sequence ...
Elevated levels of cortisol, if prolonged, can lead to proteolysis (breakdown of proteins) and muscle wasting.[6] Several ... Manchester, KL (1964). "Sites of Hormonal Regulation of Protein Metabolism". In Allison, NH & Munro JB. Mammalian Protein ... Cortisol also plays an important, but indirect, role in liver and muscle glycogenolysis, the breaking down of glycogen to ... It is vital for structural support and is found in muscles, tendons, and joints, as well as throughout the entire body. ...
"Characterising the muscle anabolic potential of dairy, meat and plant-based protein sources in older adults". Proceedings of ... meat and dairy provide only 18% of our calories and 37% of our protein, yet use up 83% of our farmland.. ... not for a richer supply of protein, but for essential nutrients such as Vitamin B12 that are absent from nectar. Similarly, ...
Morgan HE, Jefferson LS, Wolpert EB, Rannels DE (Apr 1971). "Regulation of protein synthesis in heart muscle. II. Effect of ... The Wrn protein is deficient in persons with Werner syndrome, a human premature aging disorder. PARP1 and Wrn proteins are part ... The messenger RNA level and protein level of PARP1 is controlled, in part, by the expression level of the ETS1 transcription ... Lebel M, Lavoie J, Gaudreault I, Bronsard M, Drouin R (May 2003). "Genetic cooperation between the Werner syndrome protein and ...
Salinthone S, Tyagi M, Gerthoffer WT (July 2008). "Small heat shock proteins in smooth muscle". Pharmacol. Ther. 119 (1): 44-54 ... uterine smooth muscle, cardiac muscle and skeletal muscle. HSPB6 has specific functions for vasodilation, platelet function, ... Heat shock protein beta-6 is a protein that in humans is encoded by the HSPB6 gene. HSPB6 also known as hsp20 is a 17-kDa ... "The small heat shock protein, HSPB6, in muscle function and disease". Cell Stress Chaperones. 15 (1): 1-11. doi:10.1007/s12192- ...
"Structural analysis of a tumor-produced sulfated glycoprotein capable of initiating muscle protein degradation". J. Biol. Chem ... Dermicidin, also known as proteolysis-inducing factor (PIF), is a protein that in humans is encoded by the DCD gene.[3][4] It ... "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/ ... protein binding. • hydrolase activity. • RNA binding. Cellular component. • extracellular exosome. • extracellular matrix. • ...
Muscle, for example, is mainly made of protein. The second is as enzymes, which are long-chain proteins which may include an ... Proteins[change , change source]. A ribbon diagram is one way biochemists describe the shape of proteins. This ribbon diagram ... Proteins are polymers of amino acids. There are twenty different common types of amino acid. Broadly speaking, they have two ... There are a few enzymes that are not proteins but instead made of RNA, which are called ribozymes, and are in fact nucleic ...
Dystrophin protein is found in muscle fibre membrane; its helical nature allows it to act like a spring or shock absorber. ... They are due to mutations in genes that are involved in making muscle proteins. This can occur due to either inheriting the ... Muscular dystrophy (MD) is a group of muscle diseases that results in increasing weakening and breakdown of skeletal muscles ... Medications used include steroids to slow muscle degeneration, anticonvulsants to control seizures and some muscle activity, ...
Press, 1997 Muscle elastic proteins, Japan Scientific Soc. Press, 1996 Endo, Makoto (31 August 2006). "Obituary: Setsuro Ebashi ... He is famous for the discovery of Troponin in 1965, which is integral to muscle contraction, as well as for the contribution of ... Ebashi, S; Kodama, A (1965). "A new protein factor promoting aggregation of tropomyosin". Journal of Biochemistry. 58 (1): 107- ... ISBN 978-0-387-12342-4 Protein array: an alternative biomolecular system Japan Scientific Soc. ...
G.; Umino, T.; Nakagawa, H. (1994). "The effect of Spirulina feeding on muscle protein deposition in red sea bream, Pagrus ... Like all protein-rich foods, spirulina contains the essential amino acid phenylalanine (2.6-4.1 g/100 g),[5] which should be ... Dried spirulina contains 5% water, 24% carbohydrates, 8% fat, and about 60% (51-71%) protein (table).[12][13] ... Toyomizu, M; Sato, K.; Taroda, H.; Kato, T.; Akiba, Y. (2001). "Effects of dietary Spirulina on meat colour in muscle of ...
The kidney removes the muscle protein from the blood. If the kidney takes up too much protein, it can be hurt. If it is bad ... This can cause weakness and muscle pain. The worse problem though is that when muscle cells die, they release cell proteins ... Rhabdomyolysis means a disease where muscle cells are damaged and die. Statins can cause damage to muscle cells. ... A heart attack is also called a myocardial infarction. Myocardial means relating to the heart muscle. Infarction means death of ...
... was to measure certain messenger RNA levels in various skeletal muscles and intestinal smooth muscle as an index of protein ... and to study the biochemistry of muscle protein breakdown. The institutions participating in this experiment were San Jose ... Effects of Muscle Atrophy on Motor End Plates: The objective of this experiment was to determine the effects of spaceflight on ... Skeletal Muscle Atrophy: The objective of this experiment was to determine the morphological and biochemical responses of ...
... is highly expressed in muscle, and is homologous to the ferlin family of proteins, which are thought to regulate ... Muscle is thought to be particularly prone to membrane wounds given that muscle cells transmit high force and undergo cycles of ... First, dysferlin-deficient muscle fibers show accumulation of vesicles (which are critical for membrane repair in non-muscle ... Further, dysferlin-deficient muscle fibers take up extracellular dyes to a greater extent than wild-type muscle fibers ...
McGrath MJ, Mitchell CA, Coghill ID, Robinson PA, Brown S (Dec 2003). "Skeletal muscle LIM protein 1 (SLIM1/FHL1) induces alpha ... Four and a half LIM domains protein 1 is a protein that in humans is encoded by the FHL1 gene. LIM proteins, named for 'LIN11, ... Morgan MJ, Madgwick AJ (Feb 1999). "The LIM proteins FHL1 and FHL3 are expressed differently in skeletal muscle". Biochemical ... "Characterization of two isoforms of the skeletal muscle LIM protein 1, SLIM1. Localization of SLIM1 at focal adhesions and the ...
"Costameric proteins in human skeletal muscle during muscular inactivity". Journal of Anatomy. 213 (3): 284-95. doi:10.1111/j. ... In cardiac muscle and skeletal muscle, the integrin beta-1D isoform is specifically expressed, and localizes to costameres, ... protein that complexes with integrins and other TM4SF proteins". The Journal of Biological Chemistry. 272 (46): 29181-9. doi: ... Integrin beta-1 also known as CD29 is a protein that in humans is encoded by the ITGB1 gene. CD29 is an integrin unit ...
This protein is expressed most abundantly in skeletal and cardiac muscle. The mutations in this gene have been associated with ... Delta-sarcoglycan is a protein that in humans is encoded by the SGCD gene. The protein encoded by this gene is one of the four ... A muscle-specific sarcoglycan interacting protein". J. Cell Biol. 148 (1): 115-26. doi:10.1083/jcb.148.1.115. PMC 3207142 . ... A muscle-specific sarcoglycan interacting protein". J. Cell Biol. 148 (1): 115-26. doi:10.1083/jcb.148.1.115. PMC 3207142 . ...
Grady RM, Starr DA, Ackerman GL, Sanes JR, Han M (March 2005). "Syne proteins anchor muscle nuclei at the neuromuscular ... The protein's in vivo half-life, the time it takes for half of the amount of protein in a cell to disappear after its synthesis ... This gene encodes a spectrin repeat containing protein expressed in skeletal and smooth muscle, and peripheral blood ... Enaptin also known as nesprin-1 or synaptic nuclear envelope protein 1 (syne-1) is an actin-binding protein that in humans that ...
Similar to statins, the risk of muscle damage exists.. *Niacin, like fibrates, is also well suited for lowering triglycerides ... Lomitapide is a microsomal triglyceride transfer protein inhibitor.. *Phytosterols may be found naturally in plants. Similar to ... A risk exists of muscle damage (myopathy and rhabdomyolysis) with statins. Hypercholesterolemia is not a risk factor for ... CETP inhibitors (cholesteryl ester transfer protein), 1 candidate is in trials. It is expected that these drugs will mainly ...
... Oldham, Jenny ... Myostatin inhibits myogenesis and there is reduced abundance of the mature protein in skeletal muscles of adult male compared ... Our final objective was to determine if the decrease in mature protein occurs in skeletal muscles of male Stat5b−/− mice ( ... The decrease in mature myostatin protein in male skeletal muscle is developmentally regulated by growth hormone. The Journal of ...
This presentation examines some of the important concepts of protein, amino acids, and betahydroxy-beta-methylbutyrate (HMB) on ... Supplementation with Strength Training and Muscle Development. ... The Influence of Protein, Amino Acids, and Beta-hydroxy-beta- ... This presentation examines some of the important concepts of protein, amino acids, and betahydroxy-beta-methylbutyrate (HMB) on ...
Longevity Protein Rejuvenates Muscle Healing in Old Mice. Current News Longevity Protein Rejuvenates Muscle Healing in Old ... Longevity Protein Rejuvenates Muscle Healing in Old Mice By: The McGowan Institute For Regenerative Medicine , Category: ... Clinically, these findings could translate to older adults who either sustained a muscle injury or underwent muscle-damaging ... "We found that we were able to rescue, at least in part, the regenerative defect of aged skeletal muscle," said lead author ...
The basic functional unit of a muscle, known as the sarcomere, consists of actin, myosin and tropomyosin proteins. If a muscle ... While theoretical models have in fact described exactly how these muscle proteins interact, this interaction has never ... The human heart is the bodys most important muscle and, if it is working at less than its best, the outcome can be fatal. ... Muscle contraction and many other movement processes are controlled by the interplay between myosin and actin filaments. Two ...
... protein or muscle gainer, natural diet pills to loss weight training, best ayurvedic remedies for weight loss ... Note: Muscle Proteins combination fast, medium and slow release protein blend is the ideal "anytime" formula, suitable for use ... SSNs Muscle Protein has been formulated in line with the latest research into muscle building nutritional technology, which ... Hence, the effect of all four of these proteins combined, as in SSNs Muscle Protein, appears to provide an extended release of ...
... protein diet to gain muscle, things to do when feeling sad, books on zen living, trans meditation mantra ... Maybe the protein group needed a little extra Protein in there diet which explains why the gained extra muscle compared to the ... And if building muscle isnt your primary objective, just shift a few of your carb-calories over to the protein side.. All of ... Proteins help you to build muscle, carbs gives you enough energy and fat helps you to put some weight. What are good carbs to ...
Invertebrate muscles: muscle specific genes and proteins.. Hooper SL1, Thuma JB. ... exist in muscle-like cells in Radiata, and almost all muscle proteins are present across Bilateria, implying that the first ... complement of present-day muscle proteins. The second is the extraordinary diversity of protein isoforms and genetic mechanisms ... The first is the evolutionary antiquity of muscle proteins. Actin, myosin, and tropomyosin (at least, the presence of other ...
... who have identified a protein in skeletal muscle that influences sleep-related behaviors. ... Researchers found that high levels of a protein called BMAL1 in the muscles of mice helped them to recover from the effects of ... Muscle protein helps to control sleep. Written by Honor Whiteman on August 4, 2017 ... Researchers have discovered that a muscle protein may influence sleep-related behaviors.. ...
If protein were really the key to building muscle you would see tons of 250 pound behemoths every where you went. ... Because, lets face it, everyone and their mother drinks protein shakes these days. And if thats all it took to build muscle ... Thats because they have been brainwashed to believe that without eating a billion grams of protein per day their muscles will ... The body can only assimilate so much protein on a daily basis and you can only build muscle so fast. ...
22 g protein. Gluten free. Muscle milk provides nutrients found in natural milk that are important for building muscles and ... High protein. Lactose free. Contains no milk. Naturally and artificially flavored. ... ProteinProtein BarsProtein BlendsProtein SnacksWhey Protein/IsolateProteinAmino AcidEnergyMeal ReplacementsMuscle GrowthMuscle ... 22 g protein. Gluten free. Muscle milk provides nutrients found in natural milk that are important for building muscles and ...
Specifically in skeletal muscle and to a lesser extent in cardiac muscle, the actin and myosin filaments are arranged in a ... Skeletal muscle cells drive movement and shape our physique.. *Cardiac muscle cells create the rhythmic and persistent ... A single muscle cell from a latissimus dorsi will have about 100,000 sarcomeres oriented in sequence (2). Skeletal muscle ... They range in length from 1,000 microns in the stapedius muscle to up to 500,000 microns in the sartorius muscle. ...
Several studies in sportsmen suggest that hydrolysed wheat proteins could help to reduce muscle injury after exercise. Wheat ... Meripro® is obtained by hydrolyzing wheat proteins, which makes it highly soluble in water, and which may also improve protein ... a soluble wheat protein. This webinar will cover both the application and the scientific aspects of this beverage concept. ... proteins display a high level of overall digestibility and contain high amounts of glutamine (36%), an amino acid which becomes ...
Protein from soy or from whey is equally effective for synthesis of muscle protein after endurance training, suggests an animal ... Important implications for protein formulations: Leucine-enrichment can boost low-protein beverages for muscle growth 21-Jan- ... Supplementing low-protein beverages with leucine can produce the same level of muscle synthesis in young men as a beverage with ... Daily supplements of omega-3 fatty acids may boost the production of muscle protein in older people, and reduce the risk of ...
As reported in The FASEB Journal, researchers discovered that by blocking the function of the protein Grb10 in mice in the womb ... This presents important implications for a range of conditions that are worsened by, or cause muscle wasting, such as injury, ... Scientists may soon help people grow strong muscles without needing to hit the weight room. ... Hulk protein, Grb10, controls muscle growth New research in The FASEB Journal suggests that a protein called Grb10 plays a ...
Injecting a blood protein called GDF11 reverses the damage caused by ageing in mice. And there are hopes a similar technique ... A protein in blood can repair age-related damage in the brains and muscles of old mice, returning them to a more youthful state ... Muscle fibres in old mice injected with GDF11 doubled in size to match that of 2-month old mice. Images from an electron ... Last year, the protein, called growth differentiation factor 11 (GDF11), was found to have a restorative effect on mouse hearts ...
Extra protein from food or supplements does lead to increases in strength and muscle, but not as much as some might hope, ... "Lots of people take protein supplements with the expectation that they are going to gain lots of muscle because of the protein ... The team found that protein supplementation led to an increase in muscle, but not much. In addition, protein supplements were ... Extra protein from food or supplements does lead to increases in strength and muscle, but not as much as some might hope, ...
If Joe and Megan Johnson have their way, the only pods people will be ingesting are their protein powders. ... "And afterwards, he always opens a fresh tub of protein powder.". As if he was in a bad infomercial, Joe lifted a jar of protein ... Shark Tank recap: A-Rod flexes some muscle to help protein-powder pod makers. Matthew Wilson ... patent-pending protein powder. Drop one in a bottle of water and shake until the pod dissolves to have a quick and easy protein ...
Moreover they will share some brand-new clinical data showing that NUTRALYS® pea protein consumption can increase muscle mass ... Plant proteins have beneficial properties in sports nutrition. However, with the variety of plant protein sources, its ... This webinar provides a key to sports nutrition development with the NUTRALYS® family of pea proteins.Roquettes global ... and its flexibility in being associated with other protein sources. ...
Protein does play an integral part in the muscle building process and body builders and athletics will use it in their diet to ... Types of protein. There are different types of protein to build muscle mass. Eggs contain a lot of protein however due to the ... Since the proteins job is the repair and recovery of muscle fibers and tissue, they are needed to repair the muscle at that ... Casein protein is slow to digest and therefore will continuously release protein to your blood system to feed your muscles for ...
But what if you dont want to-or cant-eat that much protein? ... Research suggests that higher protein meals can help you lose ... Eat a little protein, build a little muscle. Take in more protein, build more muscle...but only up to a point. ... How does your body make muscle?. Building and repairing muscle tissue requires protein-and thats a nutrient that our bodies ... Whenever we eat foods containing protein, we get a little burst of muscle-building activity. The amount of muscle you build is ...
Reverse engineering of the giant muscle protein titin.. Li H1, Linke WA, Oberhauser AF, Carrion-Vazquez M, Kerkvliet JG, Lu H, ... The protein titin provides muscle with its passive elasticity. Each titin molecule extends over half a sarcomere, and its ... Here we use protein engineering and single-molecule atomic force microscopy to examine the mechanical components that form the ... We show that when these mechanical elements are combined, they explain the macroscopic behaviour of titin in intact muscle. Our ...
Get free shipping at $35 and view promotions and reviews for CytoSport Muscle Milk Protein Shake Chocolate Milk ... CytoSport Muscle Milk Protein Shake Chocolate Milk at Walgreens. ... CytoSport Muscle Milk Protein Shake Chocolate Milk11.0 oz. x 4 ... Muscle milk helps grow faster than gainers, whey or even creatine. This increased muscle growth is possible because muscle milk ... Muscle Milk RTD is intended for anyone seeking a premium, protein-enhanced shake for their nutritional goals. Before (optional ...
... and thats where protein comes in. Here are seven snack ideas that will make your muscles grow. ... 7 High-Protein Snacks That Will Help You Build Muscle. By snacking smarter, your muscles will grow bigger, faster ... Whites protein shake recipe is about as easy as it gets. Drink it as is, or add in your favorite flavors with extra fruit, ... "Since our body can only use about 25 to 30 grams of protein at a time, dosing it throughout the day into several meals and ...
Muscle Milk, powder Nutrition - BellaOnline Nutrition Database - BellaOnline is committed to helping our visitors become ... Long Description: Protein supplement, milk based, Muscle Milk, powder. Short Description: PROTEIN SUPP,MILK BSD,MUSCLE MILK,PDR ... Protein supplement, milk based, Muscle Milk, powder Nutrition. This page is all about the nutrition of Protein supplement, milk ... Protein supplement, milk based, Muscle Milk, powder Nutrition Information - Full Details. All values shown in the detailed view ...
... shift after research from the University of Stirling has found individuals with more muscle mass do not need more protein after ... Scientists challenge recommendation that men with more muscle need more protein. Published Wednesday 24 August 2016 Published ... This difference suggests the amount of muscle worked in a single session has a bigger impact on the amount of protein needed ... "Scientists challenge recommendation that men with more muscle need more protein." Medical News Today. MediLexicon, Intl., 24 ...
  • Our first objective was to determine if the decrease in mature myostatin protein occurs before the linear growth phase to aid growth, or afterwards to maintain the mass of adult muscle. (waikato.ac.nz)
  • Since our body can only use about 25 to 30 grams of protein at a time , dosing it throughout the day into several meals and snacks paired with fiber-containing carbs and healthy fats is your best bet towards optimally utilizing nutrients," says certified exercise physiologist Jim White, R.D., owner of Jim White Fitness and Nutrition Studios in Virginia Beach. (menshealth.com)
  • Muscle Milk has several advantages over whey, namely that Muscle Milk is a mixture of several dairy proteins, including whey and calcium caseinate, it contains some carbs, and has a full spectrum of vitamins and minerals, Bodybuilding.com states. (reference.com)
  • The oatmeal gives you a great source of carbs which will provide you with energy to get you through your workout and the whey protein will get to your muscles quickly to provide nutrients to maintain lean muscle tissue. (shapefit.com)
  • Insulin is a transport hormone which will carry the carbs and refill your muscle glycogen levels and rush protein to your muscles. (shapefit.com)
  • Egg whites contain virtually zero fat and carbs which makes them a great low-calorie protein source to eat when your goal is to lose body fat and get lean. (shapefit.com)
  • In layman's terms, getting adequate carbs with your protein through these snacks will help keep you from breaking down muscle tissue during hard training, and instead send your body the message to add mass! (bodybuilding.com)
  • Sixteen young men were put to the test: They worked out at 8 pm for slightly less than an hour, then immediately ate a meal filled with protein and carbs. (greatist.com)
  • If anyone has any advice re:carbs/fat before bed to go with protein that would be appreciated too! (thinkmuscle.com)
  • Muscle contraction and many other movement processes are controlled by the interplay between myosin and actin filaments. (redorbit.com)
  • Two further proteins, tropomyosin and troponin, regulate how myosin binds to actin. (redorbit.com)
  • The basic functional unit of a muscle, known as the sarcomere, consists of actin, myosin and tropomyosin proteins. (redorbit.com)
  • If a muscle is to be able to contract, the myosin must slide along filamentous actin molecules. (redorbit.com)
  • Working together with troponin, tropomyosin regulates muscle contraction by controlling when myosin binds to actin. (redorbit.com)
  • Comparisons with myosin structures in other states have allowed the researchers to describe the interplay of myosin and actin during muscle contraction. (redorbit.com)
  • Actin, myosin, and tropomyosin (at least, the presence of other muscle proteins in these organisms has not been examined) exist in muscle-like cells in Radiata, and almost all muscle proteins are present across Bilateria, implying that the first Bilaterian had a complete, or near-complete, complement of present-day muscle proteins. (nih.gov)
  • At the heart of these micro-motors are two contractile proteins called actin and myosin. (crossfit.com)
  • Specifically in skeletal muscle and to a lesser extent in cardiac muscle, the actin and myosin filaments are arranged in a linear manner that gives the muscle a striated or striped appearance. (crossfit.com)
  • This results from the physical structures of myosin, a very large and thick protein with a globular end, and actin, a thinner more linear protein. (crossfit.com)
  • Myosin is a dimer, formed of two individual myosin proteins bound together. (crossfit.com)
  • Myosin is held in place by titin (another specialized protein). (crossfit.com)
  • Three myosin heavy chain isoforms with different actin-activated Mg 2+ -ATPase activities were found in the fast skeletal muscle from carp ( Cyprinus carpio ) acclimated to 10 and 30°C. The composition of three types of myosin heavy chain was dependent on acclimation temperature, demonstrating the presence of temperature-specific myosin isoforms in carp. (biologists.org)
  • This article shows that one of the myofibrillar proteins responsible for changes in muscle plasticity in association with temperature acclimation of carp is myosin, a major protein in the contractile apparatus. (biologists.org)
  • Myosin is the most abundant protein in the contractile apparatus, is essential for the contractile process and has been studied intensively. (biologists.org)
  • Protein solubility is related to myosin isoforms, muscle fiber types, meat quality traits, and postmortem protein changes in porcine longissimus dorsi muscle," Livestock Science , vol. 127, no. 2-3, pp. 183-191, 2010. (hindawi.com)
  • Maegen A. Ackermann and Aikaterini Kontrogianni-Konstantopoulos, "Myosin Binding Protein-C: A Regulator of Actomyosin Interaction in Striated Muscle," Journal of Biomedicine and Biotechnology , vol. 2011, Article ID 636403, 9 pages, 2011. (hindawi.com)
  • Chun, M. & Falkenthal, S. (1988) Ifm(2)2 is a myosin heavy chain allele that disrupts myofibrillar assembly only in the indirect flight muscle of Drosophila melanogaster . (springer.com)
  • George, E. L., Ober, M. B. & Emerson, C. P. , Jr. (1989) Functional domains of the Drosophila melanogaster muscle myosin heavy chain gene are encoded by alternatively spliced exons. (springer.com)
  • By raising Klotho levels in old animals, or by mitigating downstream effects of Klotho deficiency, the researchers could restore muscle regeneration after injury. (pitt.edu)
  • Researchers found that high levels of a protein called BMAL1 in the muscles of mice helped them to recover from the effects of sleep deprivation , while low levels of the protein interfered with sleep. (medicalnewstoday.com)
  • The researchers came to their findings by assessing how the BMAL1 protein affects sleep in mice. (medicalnewstoday.com)
  • The researchers found that eliminating BMAL1 from the brains of mice had no influence on sleep-related behaviors, and this did not change when the protein was restored. (medicalnewstoday.com)
  • When the researchers reintroduced BMAL1 to the muscles of the mice, their ability to recover from disrupted sleep was restored. (medicalnewstoday.com)
  • Australian researchers have found that by blocking the function of a protein called Grb10 while mice were in the womb, they were considerably stronger and more muscular than their normal counterparts. (eurekalert.org)
  • Researchers examined the properties of the muscles in both adult and newborn mice and discovered that the alterations caused by loss of Grb10 function had mainly occurred during prenatal development. (eurekalert.org)
  • I recently attended a meeting with some of the world's top protein researchers and in between sessions I hit them up for their insights on the questions you've raised. (scientificamerican.com)
  • Researchers examined data from 49 previously published studies with a total of 1,863 people who did muscle-building workouts like weightlifting. (reuters.com)
  • One limitation of the study is that researchers didn't have enough data on older adults to determine how much added protein might help these individuals build lean muscle mass, which typically declines with age. (reuters.com)
  • Researchers also didn't look at what happens when dieters get added protein. (reuters.com)
  • The researchers suggest that increasing PCG-1alpha activity in muscle could be a new and attractive therapeutic target for maintaining, improving and extending physical abilities in ALS patients. (ucsd.edu)
  • Researchers have long considered it to be essentially an affliction of primary motor neurons - the cells in the spinal cord and brainstem that control muscle movement. (medindia.net)
  • The trap some protein researchers fall into is to forget other important nutrients. (dairyreporter.com)
  • Researchers believe they have discovered what it takes to accomplish the most popular exercise goal in the fitness community: how to lose fat and gain muscle at the same time. (bodyecology.com)
  • The researchers were putting the subjects' feet to the fire to see how quickly they could get the men to lose fat, retain muscle, and improve fitness. (bodyecology.com)
  • Hamilton, Nov. 11, 2013 Researchers at McMaster University have discovered a protein that is only detectable after muscle damage, and it may serve as a way to measure injury. (bio-medicine.org)
  • The researchers found this to be true for healthy subjects who have damaged their muscles with intense exercise as well as numerous patients with various forms of muscle disease, including muscular dystrophy. (bio-medicine.org)
  • In the first study, researchers led by Stuart Phillips (McMaster University) investigated whether postexercise muscle protein synthesis is different when a large, single dose of whey protein (25 g) is consumed immediately after activity compared with when smaller doses (2.5 g) are consumed 10 times over an extended period. (anabolicminds.com)
  • According to the researchers' calculations, optimal protein consumption was 1.6 grams of protein per kilogram of body weight per day, or double the RDA of 0.8 gram of protein per kilogram of body weight. (uexpress.com)
  • This modern and advanced purification and homogenization process produces over 99% non-denatured amino acids which yields more intact whey protein fractions in addition to beta-lactoglobulins, alpha-lactoglobulins, serum albumin, lactoferrin and bioactive peptides with many biological health benefits. (scribd.com)
  • Proteins destined for degradation by the Ub-proteasome pathway are first covalently linked to a chain of Ub molecules, which marks them for rapid breakdown to short peptides by the 26S proteasome ( 12 ). (pnas.org)
  • Besides, the hydrolysed protein peptides quickly make their way into the small intestine, preventing any bloating to occur. (myprotein.com)
  • The other group, where the Grb10 gene was functional, had normal muscles. (eurekalert.org)
  • Finally, Don W. Cleveland, PhD, professor and chair of the Department of Cellular and Molecular Medicine and head of the Laboratory of Cell Biology at the Ludwig Institute for Cancer Research at UC San Diego and colleagues report the effects of elevated levels of a gene- regulating protein in mouse cells afflicted by a form of amyotrophic lateral sclerosis or ALS. (ucsd.edu)
  • Duchenne muscular dystrophy arises from mutations in the gene that produces dystrophin, a protein involved in the assembly and signaling of interrelated muscle-cell surface molecules known collectively as the dystrophin-associated protein complex. (medpagetoday.com)
  • The anabolic effects of both whey protein and the BCAAs combined with exercise stimulates skeletal muscle gene expression. (scribd.com)
  • To identify key factors in this process, we have used cDNA microarrays to compare normal and atrophying muscles and found a unique gene fragment that is induced more than ninefold in muscles of fasted mice. (pnas.org)
  • We cloned this gene, which is expressed specifically in striated muscles. (pnas.org)
  • We have also studied further the expression of this gene on food deprivation and in several other models of human diseases in which there is a marked acceleration of muscle proteolysis. (pnas.org)
  • p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence. (uniprot.org)
  • section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. (uniprot.org)
  • F-actin-capping protein subunit alpha-1 is a protein that in humans is encoded by the CAPZA1 gene. (wikipedia.org)
  • This gene encodes the alpha subunit of the barbed-end actin binding protein. (wikipedia.org)
  • The effect levels off at a certain point, after which extra protein provides no additional benefit. (reuters.com)
  • Also, the benefits of extra protein were more pronounced for newer exercisers than for people with lots of previous experience with resistance training. (reuters.com)
  • For each study, participants were randomly selected to stick to their usual diets or add extra protein. (reuters.com)
  • If you want to make outstanding muscle building progress, you must put together a solid weight training program , train with a high level of intensity , add poundage to your exercises as often as possible, eat six high protein meals every day, and make sure you are out of the gym often enough to recover from your workouts so that your muscles have time to grow. (bodybuilding.com)
  • This is a quick digesting and fast acting protein to use before and after your workouts since you want to get the protein into your system quickly to provide nutrients to your muscles. (shapefit.com)
  • Together, the combination will be powerful enough to provide energy for long workouts and recovery, but not as much recovery and bulk building power as animal-based protein. (healthtransformation.net)
  • In contrast, the small muscle-specific isoform of ankyrin 1 (ank1.5), a transmembrane protein of the longitudinal SR known to interact with the myofibrillar protein obscurin, is preferentially localized near the M band and, to a lesser extent, to the Z disk ( 11 - 16 ). (pnas.org)
  • Every cell and drop of our blood contains many thousands of different types of proteins, and each of these proteins is built from the protein we eat. (lesmills.com)
  • It's important to remember that there are many different types of proteins to choose from depending on your specific goals. (shapefit.com)
  • We found that we were able to rescue, at least in part, the regenerative defect of aged skeletal muscle," said lead author Fabrisia Ambrosio, PhD , director of rehabilitation for UPMC International, associate professor of physical medicine and rehabilitation at Pitt, and core faculty at the McGowan Institute of Regenerative Medicine. (pitt.edu)
  • Smooth muscle cells, the type found in vascular walls, intestine walls, and the uterus, act slowly create movement along tubular tracts. (crossfit.com)
  • Consumer Reports conducted a study on protein drinks and found some of them contain levels of heavy metals exceeding the recommended daily allowance. (livestrong.com)
  • Whey is one of the two proteins found in milk, the one other being casein. (newsmax.com)
  • Myoglobin is a protein found mostly in muscle cells comprised of eight alpha-helices. (reference.com)
  • One potential therapeutic approach to Duchenne muscular dystrophy would be to stabilize the muscle-cell membrane by upregulation of utrophin, a dystrophin homolog found primarily in developing, immature muscle cells. (medpagetoday.com)
  • But follistatin is a different protein that lies on the same pathway, and Lee recently found that follistatin makes muscles grow even larger than the absence of myostatin alone. (inventorspot.com)
  • Washington D.C. [USA], August 05 : Challenging the widely accepted notion that the brain controls sleep, a study has found a protein in the muscle can lessen the effect of sleep loss in mice. (newkerala.com)
  • Two proteins, α -actinin and Z(400/600), are found at the Z-band of every muscle examined. (springer.com)
  • It is found only in the asynchronous muscle and in the large cells of the jump muscle (tergal depressor of the trochanter). (springer.com)