Myosin Type I
Myosins
Myosin Type IV
Myosin Type III
Myosin Type II
Nonmuscle Myosin Type IIB
Myosin Type V
Nonmuscle Myosin Type IIA
Myosin Heavy Chains
Myosin Subfragments
Myosin Light Chains
Actins
Interferon Type I
Myosin-Light-Chain Kinase
Actomyosin
Collagen Type I
Gizzard
Heterocyclic Compounds with 4 or More Rings
Rabbits
Myosin-Light-Chain Phosphatase
Adenosine Triphosphatases
Ventricular Myosins
Molecular Motor Proteins
Chickens
Muscle, Smooth
Actin Cytoskeleton
Molecular Sequence Data
Phosphorylation
Amino Acid Sequence
Muscle Contraction
Dictyostelium
Myofibrils
Turkeys
Tropomyosin
Muscle, Skeletal
Protein Binding
Adenosine Triphosphate
Protein Isoforms
Muscle Fibers, Skeletal
Electrophoresis, Polyacrylamide Gel
rho-Associated Kinases
Transient kinetic analysis of the 130-kDa myosin I (MYR-1 gene product) from rat liver. A myosin I designed for maintenance of tension? (1/185)
The 130-kDa myosin I (MI(130)), product of the myr-1 gene, is one member of the mammalian class I myosins, a group of small, calmodulin-binding mechanochemical molecules of the myosin superfamily that translocate actin filaments. Roles for MI(130) are unknown. Our hypothesis is that, as with all myosins, MI(130) is designed for a particular function and hence possesses specific biochemical attributes. To test this hypothesis we have characterized the enzymatic properties of MI(130) using steady-state and stopped-flow kinetic analyses. Our results indicate that: (i) the Mg(2+)-ATPase activity is activated in proportion to actin concentration in the absence of Ca(2+); (ii) the ATP-induced dissociation of actin-MI(130) is much slower for MI(130) than has been observed for other myosins (-Ca(2+), second order rate constant of ATP binding, 1.7 x 10(4) M(-1) s(-1); maximal rate constant, 32 s(-1)); (iii) ADP binds to actin-MI(130) with an affinity of approximately 10 microM and competes with ATP-induced dissociation of actin-MI(130); the rate constant of ADP release from actin-MI(130) is 2 s(-1); (iv) the rates of the ATP-induced dissociation of actin-MI and ADP release are 2-3 times greater in the presence of CaCl(2), indicating a sensitivity of motor activity to Ca(2+); and (v) the affinity of MI(130) for actin (15 nM) is typical of that observed for other myosins. Together, these results indicate that although MI(130) shares some characteristics with other myosins, it is well adapted for maintenance of cortical tension. (+info)A role for myosin-I in actin assembly through interactions with Vrp1p, Bee1p, and the Arp2/3 complex. (2/185)
Type I myosins are highly conserved actin-based molecular motors that localize to the actin-rich cortex and participate in motility functions such as endocytosis, polarized morphogenesis, and cell migration. The COOH-terminal tail of yeast myosin-I proteins, Myo3p and Myo5p, contains an Src homology domain 3 (SH3) followed by an acidic domain. The myosin-I SH3 domain interacted with both Bee1p and Vrp1p, yeast homologues of human WASP and WIP, adapter proteins that link actin assembly and signaling molecules. The myosin-I acidic domain interacted with Arp2/3 complex subunits, Arc40p and Arc19p, and showed both sequence similarity and genetic redundancy with the COOH-terminal acidic domain of Bee1p (Las17p), which controls Arp2/3-mediated actin nucleation. These findings suggest that myosin-I proteins may participate in a diverse set of motility functions through a role in actin assembly. (+info)Dictyostelium myosin IK is involved in the maintenance of cortical tension and affects motility and phagocytosis. (3/185)
Dictyostelium discoideum myosin Ik (MyoK) is a novel type of myosin distinguished by a remarkable architecture. MyoK is related to class I myosins but lacks a cargo-binding tail domain and carries an insertion in a surface loop suggested to modulate motor velocity. This insertion shows similarity to a secondary actin-binding site present in the tail of some class I myosins, and indeed a GST-loop construct binds actin. Probably as a consequence, binding of MyoK to actin was not only ATP- but also salt-dependent. Moreover, as both binding sites reside within its motor domain and carry potential sites of regulation, MyoK might represent a new form of actin crosslinker. MyoK was distributed in the cytoplasm with a significant enrichment in dynamic regions of the cortex. Absence of MyoK resulted in a drop of cortical tension whereas overexpression led to significantly increased tension. Absence and overexpression of MyoK dramatically affected the cortical actin cytoskeleton and resulted in reduced initial rates of phagocytosis. Cells lacking MyoK showed excessive ruffling, mostly in the form of large lamellipodia, accompanied by a thicker basal actin cortex. At early stages of development, aggregation of myoK null cells was slowed due to reduced motility. Altogether, the data indicate a distinctive role for MyoK in the maintenance and dynamics of the cell cortex. (+info)The mouse neurological mutant flailer expresses a novel hybrid gene derived by exon shuffling between Gnb5 and Myo5a. (4/185)
Exon shuffling is thought to be an important mechanism for evolution of new genes. Here we show that the mouse neurological mutation flailer (flr) expresses a novel gene that combines the promoter and first two exons of guanine nucleotide binding protein beta 5 (Gnb5) with the C-terminal exons of the closely linked Myosin 5A (MyoVA) gene (Myo5a). The flailer protein, which is expressed predominantly in brain, contains the N-terminal 83 amino acids of Gnb5 fused in-frame with the C-terminal 711 amino acids of MyoVA, including the globular tail domain that binds organelles for intracellular transport. Biochemical and genetic studies indicate that the flailer protein competes with wild-type MyoVA in vivo, preventing the localization of smooth endoplasmic reticulum vesicles in the dendritic spines of cerebellar Purkinje cells. The flailer protein thus has a dominant-negative mechanism of action with a recessive mode of inheritance due to the dependence of competitive binding on the ratio between mutant and wild-type proteins. The chromosomal arrangement of Myo5a upstream of Gnb5 is consistent with non-homologous recombination as the mutational mechanism. To our knowledge, flailer is the first example of a mammalian mutation caused by germ line exon shuffling between unrelated genes. (+info)Truncation of a mammalian myosin I results in loss of Ca2+-sensitive motility. (5/185)
MYR-1, a mammalian class I myosin, consisting of a heavy chain and 4-6 associated calmodulins, is represented by the 130-kDa myosin I (or MI(130)) from rat liver. MI(130) translocates actin filaments in vitro in a Ca(2+)-regulated manner. A decrease in motility observed at higher Ca(2+) concentrations has been attributed to calmodulin dissociation. To investigate mammalian myosin I regulation, we have coexpressed in baculovirus calmodulin and an epitope-tagged 85-kDa fragment representing the amino-terminal catalytic "motor" domain and the first calmodulin-binding IQ domain of rat myr-1; we refer to this truncated molecule here as MI(1IQ). Association of calmodulin to MI(1IQ) is Ca(2+)-insensitive. MI(1IQ) translocates actin filaments in vitro at a rate resembling MI(130), but unlike MI(130), does not exhibit sensitivity to 0.1-100 micrometer Ca(2+). In addition to demonstrating successful expression of a functional truncated mammalian myosin I in vitro, these results indicate that: 1) Ca(2+)-induced calmodulin dissociation from MI(130) in the presence of actin is not from the first IQ domain, 2) velocity is not affected by the length of the IQ region, and 3) the Ca(2+) sensitivity of actin translocation exhibited by MI(130) involves 1 or more of the other 5 IQ domains and/or the carboxyl tail. (+info)Kinetic analyses of a truncated mammalian myosin I suggest a novel isomerization event preceding nucleotide binding. (6/185)
MI(1IQ) is a complex of calmodulin and an epitope-tagged 85-kDa fragment representing the amino-terminal catalytic motor domain and the first of 6 calmodulin-binding IQ domains of the mammalian myosin I gene, rat myr-1 (130-kDa myosin I or MI(130)). We have determined the transient kinetic parameters that dictate the ATP hydrolysis cycle of mammalian myosin I by examining the properties of MI(1IQ). Transient kinetics reveal that the affinity of MI(1IQ) for actin is 12 nm. The ATP-induced dissociation of actin-MI(1IQ) is biphasic. The fast phase is dependent upon [ATP], whereas the slow phase is not; both phases show a Ca(2+) sensitivity. The fast phase is eliminated by the addition of ADP, 10 micrometer being required for half-saturation of the effect in the presence of Ca(2+) and 3 micrometer ADP in the absence of Ca(2+). The slow phase shares the same rate constant as ADP release (8 and 3 s(-)(1) in the presence and absence of Ca(2+), respectively), but cannot be eliminated by decreasing [ADP]. We interpret these results to suggest that actin-myosin I exists in two forms in equilibrium, one of which is unable to bind nucleotide. These results also indicate that the absence of the COOH-terminal 5 calmodulin binding domains of myr-1 do not influence the kinetic properties of MI(130) and that the Ca(2+) sensitivity of the kinetics are in all likelihood due to Ca(2+) binding to the first IQ domain. (+info)An intact SH3 domain is required for myosin I-induced actin polymerization. (7/185)
The yeast type I myosins (MYO3 and MYO5) are involved in endocytosis and in the polarization of the actin cytoskeleton. The tail of these proteins contains a Tail Homology 2 (TH2) domain that constitutes a putative actin-binding site. Because of the important mechanistic implications of a second ATP-independent actin-binding site, we analyzed its functional relevance in vivo. Even though the myosin tail interacts with actin, and this interaction seems functionally important, deletion of a major portion of the TH2 domain did not abolish interaction. In contrast, we found that the SH3 domain of Myo5p significantly contributes to this interaction, implicating other proteins. We found that Vrp1p, the yeast homolog of WIP [Wiskott-Aldrich syndrome protein (WASP)-interacting protein], seems necessary to sustain the Myo5p tail-F-actin interaction. Consistent with recent results implicating the yeast type I myosins in regulating actin polymerization in vivo, we demonstrate that the C-terminal domain of Myo5p is able to induce cytosol-dependent actin polymerization in vitro, and that this activity requires both an intact Myo5p SH3 domain and Vrp1p. (+info)Fission yeast myosin-I, Myo1p, stimulates actin assembly by Arp2/3 complex and shares functions with WASp. (8/185)
Fission yeast myo1(+) encodes a myosin-I with all three tail homology domains (TH1, 2, 3) found in typical long-tailed myosin-Is. Myo1p tail also contains a COOH-terminal acidic region similar to the A-domain of WASp/Scar proteins and other fungal myosin-Is. Our analysis shows that Myo1p and Wsp1p, the fission yeast WASp-like protein, share functions and cooperate in controlling actin assembly. First, Myo1p localizes to cortical patches enriched at tips of growing cells and at sites of cell division. Myo1p patches partially colocalize with actin patches and are dependent on an intact actin cytoskeleton. Second, although deletion of myo1(+) is not lethal, Deltamyo1 cells have actin cytoskeletal defects, including loss of polarized cell growth, delocalized actin patches, and mating defects. Third, additional disruption of wsp1(+) is synthetically lethal, suggesting that these genes may share functions. In mapping the domains of Myo1p tail that share function with Wsp1p, we discovered that a Myo1p construct with just the head and TH1 domains is sufficient for cortical localization and to rescue all Deltamyo1 defects. However, it fails to rescue the Deltamyo1 Deltawsp1 lethality. Additional tail domains, TH2 and TH3, are required to complement the double mutant. Fourth, we show that a recombinant Myo1p tail binds to Arp2/3 complex and activates its actin nucleation activity. (+info)Myosin Type I, also known as myosin-IA, is a type of motor protein found in non-muscle cells. It is involved in various cellular processes such as organelle transport, cell division, and maintenance of cell shape. Myosin-IA consists of a heavy chain, light chains, and a cargo-binding tail domain. The heavy chain contains the motor domain that binds to actin filaments and hydrolyzes ATP to generate force and movement along the actin filament.
Myosin-I is unique among myosins because it can move in both directions along the actin filament, whereas most other myosins can only move in one direction. Additionally, myosin-I has a high duty ratio, meaning that it spends a larger proportion of its ATP hydrolysis cycle bound to the actin filament, making it well-suited for processes requiring sustained force generation or precise positioning.
Myosins are a large family of motor proteins that play a crucial role in various cellular processes, including muscle contraction and intracellular transport. They consist of heavy chains, which contain the motor domain responsible for generating force and motion, and light chains, which regulate the activity of the myosin. Based on their structural and functional differences, myosins are classified into over 35 classes, with classes II, V, and VI being the most well-studied.
Class II myosins, also known as conventional myosins, are responsible for muscle contraction in skeletal, cardiac, and smooth muscles. They form filaments called thick filaments, which interact with actin filaments to generate force and movement during muscle contraction.
Class V myosins, also known as unconventional myosins, are involved in intracellular transport and organelle positioning. They have a long tail that can bind to various cargoes, such as vesicles, mitochondria, and nuclei, and a motor domain that moves along actin filaments to transport the cargoes to their destinations.
Class VI myosins are also unconventional myosins involved in intracellular transport and organelle positioning. They have two heads connected by a coiled-coil tail, which can bind to various cargoes. Class VI myosins move along actin filaments in a unique hand-over-hand motion, allowing them to transport their cargoes efficiently.
Overall, myosins are essential for many cellular functions and have been implicated in various diseases, including cardiovascular diseases, neurological disorders, and cancer.
Myosin type IV, also known as myosin-1c, is a member of the unconventional myosin family. It is an actin-based molecular motor protein that plays a role in intracellular transport, organelle positioning, and cell signaling. Myosin-1c has a single head domain, which can bind to actin filaments and hydrolyze ATP to generate force and motion. It is widely expressed in various tissues, including the heart, skeletal muscle, and brain. Mutations in the gene that encodes myosin-1c have been associated with several human diseases, such as deafness, cardiomyopathy, and neurological disorders.
Myosin III is a type of molecular motor protein found in cells, responsible for providing cellular movement and organization. More specifically, Myosin III is involved in the regulation of actin filament dynamics and contributes to various cellular functions such as vesicle transport, maintenance of cell shape, and signal transduction.
Myosin III has a unique motor domain that allows it to move along actin filaments while generating force. It also contains a protein kinase domain, which enables it to phosphorylate target proteins and regulate their activity. Mutations in the MYO3 gene have been associated with certain inherited diseases, such as Usher syndrome type 1F, a condition characterized by hearing loss and retinitis pigmentosa, leading to vision loss.
Myosin Type II, also known as myosin II or heavy meromyosin, is a type of motor protein involved in muscle contraction and other cellular movements. It is a hexameric protein composed of two heavy chains and four light chains. The heavy chains have a head domain that binds to actin filaments and an tail domain that forms a coiled-coil structure, allowing the formation of filaments. Myosin II uses the energy from ATP hydrolysis to move along actin filaments, generating force and causing muscle contraction or other cell movements. It plays a crucial role in various cellular processes such as cytokinesis, cell motility, and maintenance of cell shape.
Nonmuscle Myosin Type IIB (NMMIIB) is a type of motor protein that belongs to the myosin superfamily. It is involved in various cellular processes, including cell division, adhesion, migration, and maintenance of cell shape. NMMIIB is composed of two heavy chains, two regulatory light chains, and two essential light chains. The heavy chains have a motor domain that enables the protein to move along actin filaments, generating force and movement.
NMMIIB is widely expressed in non-muscle tissues, and its activity is regulated by phosphorylation and dephosphorylation of the regulatory light chains. Phosphorylation activates NMMIIB, leading to contractile forces that can alter cell shape and promote cell motility. In contrast, dephosphorylation inactivates NMMIIB, allowing for relaxation of the contractile forces.
Abnormal regulation of NMMIIB has been implicated in various pathological conditions, including cancer metastasis, cardiovascular diseases, and neurological disorders. Therefore, understanding the molecular mechanisms that regulate NMMIIB function is an important area of research with potential therapeutic implications.
Myosin Type V is an molecular motor protein involved in the intracellular transport of various cargoes, including vesicles and organelles. It belongs to the family of myosins, which are actin-based motors that convert chemical energy into mechanical work through the hydrolysis of ATP.
Myosin V is characterized by its long tail domain, which allows it to form dimers or higher-order oligomers, and its head domain, which binds to actin filaments and hydrolyzes ATP to generate force and movement. The protein moves in a hand-over-hand manner along the actin filament, allowing it to transport cargoes over long distances within the cell.
Myosin V has been implicated in various cellular processes, including exocytosis, endocytosis, and organelle positioning. Mutations in the MYO5A gene, which encodes Myosin Type V, have been associated with several human genetic disorders, such as Griscelli syndrome type 1 and familial progressive arthro-ophthalmopathy.
Nonmuscle Myosin Type IIA (NMIIA) is a type of non-muscle myosin protein that belongs to the myosin II family. These motor proteins are responsible for generating contractile forces in non-muscle cells, which allows them to change shape and move. NMIIA is widely expressed in various tissues and plays crucial roles in numerous cellular processes, including cytokinesis (cell division), maintenance of cell shape, and intracellular transport.
NMIIA consists of two heavy chains, two regulatory light chains, and two essential light chains. The heavy chains have a motor domain that binds to actin filaments and hydrolyzes ATP to generate force for movement along the actin filament. The regulatory and essential light chains regulate the activity and assembly of NMIIA.
Mutations in the gene encoding NMIIA (MYH9) have been associated with several human genetic disorders, such as May-Hegglin anomaly, Fechtner syndrome, and Delletten-Patterson syndrome, which are characterized by thrombocytopenia, bleeding disorders, and hearing loss.
Myosin Heavy Chains are the large, essential components of myosin molecules, which are responsible for the molecular motility in muscle cells. These heavy chains have a molecular weight of approximately 200 kDa and form the motor domain of myosin, which binds to actin filaments and hydrolyzes ATP to generate force and movement during muscle contraction. There are several different types of myosin heavy chains, each with specific roles in various tissues and cellular functions. In skeletal and cardiac muscles, for example, myosin heavy chains have distinct isoforms that contribute to the contractile properties of these tissues.
Myosin subfragments refer to the smaller components that result from the dissociation or proteolytic digestion of myosin, a motor protein involved in muscle contraction. The two main subfragments are called S1 and S2.
S1 is the "head" of the myosin molecule, which contains the actin-binding site, ATPase activity, and the ability to generate force and motion during muscle contraction. It has a molecular weight of approximately 120 kDa.
S2 is the "tail" of the myosin molecule, which has a molecular weight of about 350 kDa and is responsible for forming the backbone of the thick filament in muscle sarcomeres. S2 can be further divided into light meromyosin (LMM) and heavy meromyosin (HMM). HMM consists of S1 and part of S2, while LMM comprises the remaining portion of S2.
These subfragments are essential for understanding myosin's structure, function, and interactions with other muscle components at a molecular level.
Myosin light chains are regulatory proteins that bind to the myosin head region of myosin molecules, which are involved in muscle contraction. There are two types of myosin light chains, essential and regulatory, that have different functions. The essential light chains are necessary for the assembly and stability of the myosin filaments, while the regulatory light chains control the calcium-sensitive activation of the myosin ATPase activity during muscle contraction. Phosphorylation of the regulatory light chains plays a critical role in regulating muscle contraction and relaxation.
Cardiac myosins are a type of myosin protein that are specifically expressed in the cardiac muscle cells (or cardiomyocytes) of the heart. These proteins play a crucial role in the contraction and relaxation of heart muscles, which is essential for proper heart function and blood circulation.
Myosins are molecular motors that use chemical energy from ATP to generate force and movement. In the context of cardiac muscle cells, cardiac myosins interact with another protein called actin to form sarcomeres, which are the basic contractile units of muscle fibers. During contraction, the heads of cardiac myosin molecules bind to actin filaments and pull them together, causing the muscle fiber to shorten and generate force.
There are different isoforms of cardiac myosins that can vary in their structure and function. Mutations in the genes encoding these proteins have been linked to various forms of cardiomyopathy, which are diseases of the heart muscle that can lead to heart failure and other complications. Therefore, understanding the structure and function of cardiac myosins is an important area of research for developing therapies and treatments for heart disease.
Actin is a type of protein that forms part of the contractile apparatus in muscle cells, and is also found in various other cell types. It is a globular protein that polymerizes to form long filaments, which are important for many cellular processes such as cell division, cell motility, and the maintenance of cell shape. In muscle cells, actin filaments interact with another type of protein called myosin to enable muscle contraction. Actins can be further divided into different subtypes, including alpha-actin, beta-actin, and gamma-actin, which have distinct functions and expression patterns in the body.
Interferon type I is a class of signaling proteins, also known as cytokines, that are produced and released by cells in response to the presence of pathogens such as viruses, bacteria, and parasites. These interferons play a crucial role in the body's innate immune system and help to establish an antiviral state in surrounding cells to prevent the spread of infection.
Interferon type I includes several subtypes, such as interferon-alpha (IFN-α), interferon-beta (IFN-β), and interferon-omega (IFN-ω). When produced, these interferons bind to specific receptors on the surface of nearby cells, triggering a cascade of intracellular signaling events that lead to the activation of genes involved in the antiviral response.
The activation of these genes results in the production of enzymes that inhibit viral replication and promote the destruction of infected cells. Interferon type I also enhances the adaptive immune response by promoting the activation and proliferation of immune cells such as T-cells and natural killer (NK) cells, which can directly target and eliminate infected cells.
Overall, interferon type I plays a critical role in the body's defense against viral infections and is an important component of the immune response to many different types of pathogens.
Myosin-Light-Chain Kinase (MLCK) is an enzyme that plays a crucial role in muscle contraction. It phosphorylates the regulatory light chains of myosin, a protein involved in muscle contraction, leading to the activation of myosin and the initiation of the contractile process. MLCK is activated by calcium ions and calmodulin, and its activity is essential for various cellular processes, including cytokinesis, cell motility, and maintenance of cell shape. In addition to its role in muscle contraction, MLCK has been implicated in several pathological conditions, such as hypertension, atherosclerosis, and cancer.
Actomyosin is a contractile protein complex that consists of actin and myosin filaments. It plays an essential role in muscle contraction, cell motility, and cytokinesis (the process of cell division where the cytoplasm is divided into two daughter cells). The interaction between actin and myosin generates force and movement through a mechanism called sliding filament theory. In this process, myosin heads bind to actin filaments and then undergo a power stroke, which results in the sliding of one filament relative to the other and ultimately leads to muscle contraction or cellular movements. Actomyosin complexes are also involved in various non-muscle cellular processes such as cytoplasmic streaming, intracellular transport, and maintenance of cell shape.
Collagen Type I is the most abundant form of collagen in the human body, found in various connective tissues such as tendons, ligaments, skin, and bones. It is a structural protein that provides strength and integrity to these tissues. Collagen Type I is composed of three alpha chains, two alpha-1(I) chains, and one alpha-2(I) chain, arranged in a triple helix structure. This type of collagen is often used in medical research and clinical applications, such as tissue engineering and regenerative medicine, due to its excellent mechanical properties and biocompatibility.
Smooth muscle myosin is a type of motor protein that is responsible for the contraction and relaxation of smooth muscles, which are found in various organs such as the bladder, blood vessels, and digestive tract. Smooth muscle myosin is composed of two heavy chains and four light chains, forming a hexameric structure. The heavy chains have an N-terminal head domain that contains the ATPase activity and a C-terminal tail domain that mediates filament assembly.
The smooth muscle myosin molecule has several unique features compared to other types of myosins, such as skeletal or cardiac myosin. For example, smooth muscle myosin has a longer lever arm, which allows for greater force generation during contraction. Additionally, the regulatory mechanism of smooth muscle myosin is different from that of skeletal or cardiac myosin. In smooth muscles, the contractile activity is regulated by phosphorylation of the light chains, which is mediated by a specific kinase called myosin light chain kinase (MLCK).
Overall, the proper regulation and function of smooth muscle myosin are critical for maintaining normal physiological functions in various organs. Dysregulation or mutations in smooth muscle myosin can lead to several diseases, such as hypertension, atherosclerosis, and gastrointestinal motility disorders.
A muscle is a soft tissue in our body that contracts to produce force and motion. It is composed mainly of specialized cells called muscle fibers, which are bound together by connective tissue. There are three types of muscles: skeletal (voluntary), smooth (involuntary), and cardiac. Skeletal muscles attach to bones and help in movement, while smooth muscles are found within the walls of organs and blood vessels, helping with functions like digestion and circulation. Cardiac muscle is the specific type that makes up the heart, allowing it to pump blood throughout the body.
In human anatomy, a "gizzard" does not exist as it is not part of the human digestive system. However, in veterinary medicine, the gizzard refers to a part of the stomach in birds and some other animals, such as crocodiles and alligators. It is a muscular, thick-walled portion where food is stored and mechanically broken down by grinding and mixing it with grit that the animal has swallowed. This action helps in the digestion process, especially for birds that do not have teeth to chew their food.
Skeletal muscle myosin, also known as myosin II, is a type of motor protein that plays a crucial role in muscle contraction. It is a hexameric protein composed of two heavy chains and four light chains. The heavy chains have a head region, which contains the ATPase activity and binds to actin filaments, and a tail region, which forms a coiled-coil structure that allows myosin molecules to self-associate into thick filaments.
During muscle contraction, the myosin heads bind to actin filaments in the sarcomere and undergo a power stroke, which results in the sliding of the actin filaments relative to the myosin filaments and thus shortening of the sarcomere. The ATP hydrolysis provides the energy for this power stroke.
Skeletal muscle myosin is essential for generating force and movement in skeletal muscles, and its dysfunction can lead to various muscle diseases and disorders.
Heterocyclic compounds with 4 or more rings refer to a class of organic compounds that contain at least four aromatic or non-aromatic rings in their structure, where one or more of the rings contains atoms other than carbon (heteroatoms) such as nitrogen, oxygen, sulfur, or selenium. These compounds are widely found in nature and have significant importance in medicinal chemistry due to their diverse biological activities. Many natural and synthetic drugs, pigments, vitamins, and antibiotics contain heterocyclic structures with four or more rings. The properties of these compounds depend on the size, shape, and nature of the rings, as well as the presence and position of functional groups.
I believe there may be some confusion in your question. "Rabbits" is a common name used to refer to the Lagomorpha species, particularly members of the family Leporidae. They are small mammals known for their long ears, strong legs, and quick reproduction.
However, if you're referring to "rabbits" in a medical context, there is a term called "rabbit syndrome," which is a rare movement disorder characterized by repetitive, involuntary movements of the fingers, resembling those of a rabbit chewing. It is also known as "finger-chewing chorea." This condition is usually associated with certain medications, particularly antipsychotics, and typically resolves when the medication is stopped or adjusted.
Myosin-Light-Chain Phosphatase (MLCP) is an enzyme complex that plays a crucial role in the regulation of muscle contraction and relaxation. It is responsible for dephosphorylating the myosin light chains, which are key regulatory components of the contractile apparatus in muscles.
The phosphorylation state of the myosin light chains regulates the interaction between actin and myosin filaments, which is necessary for muscle contraction. When the myosin light chains are phosphorylated, they bind more strongly to actin, leading to increased contractile force. Conversely, when the myosin light chains are dephosphorylated by MLCP, the interaction between actin and myosin is weakened, allowing for muscle relaxation.
MLCP is composed of three subunits: a catalytic subunit (PP1cδ), a regulatory subunit (MYPT1), and a small subunit (M20). The regulatory subunit contains binding sites for various signaling molecules that can modulate the activity of MLCP, such as calcium/calmodulin, protein kinase C, and Rho-associated protein kinase (ROCK). Dysregulation of MLCP has been implicated in various muscle disorders, including hypertrophic cardiomyopathy, dilated cardiomyopathy, and muscle atrophy.
Adenosine triphosphatases (ATPases) are a group of enzymes that catalyze the conversion of adenosine triphosphate (ATP) into adenosine diphosphate (ADP) and inorganic phosphate. This reaction releases energy, which is used to drive various cellular processes such as muscle contraction, transport of ions across membranes, and synthesis of proteins and nucleic acids.
ATPases are classified into several types based on their structure, function, and mechanism of action. Some examples include:
1. P-type ATPases: These ATPases form a phosphorylated intermediate during the reaction cycle and are involved in the transport of ions across membranes, such as the sodium-potassium pump and calcium pumps.
2. F-type ATPases: These ATPases are found in mitochondria, chloroplasts, and bacteria, and are responsible for generating a proton gradient across the membrane, which is used to synthesize ATP.
3. V-type ATPases: These ATPases are found in vacuolar membranes and endomembranes, and are involved in acidification of intracellular compartments.
4. A-type ATPases: These ATPases are found in the plasma membrane and are involved in various functions such as cell signaling and ion transport.
Overall, ATPases play a crucial role in maintaining the energy balance of cells and regulating various physiological processes.
Ventricular myosins are the type of myosin proteins that are primarily found in the cardiac muscle cells (cardiomyocytes) of the heart ventricles. These myosin filaments are responsible for generating the mechanical force needed for cardiac muscle contraction and relaxation, which is essential for pumping blood throughout the body.
More specifically, ventricular myosins are part of the sarcomere structure in cardiomyocytes, where they interact with actin filaments to form cross-bridges during muscle contraction. The formation and breaking of these cross-bridges result in the sliding of actin and myosin filaments relative to each other, leading to muscle shortening and force generation.
Mutations or dysfunction in ventricular myosins can lead to various cardiac diseases, including hypertrophic cardiomyopathy (HCM), dilated cardiomyopathy (DCM), and heart failure. Therefore, understanding the structure and function of ventricular myosins is crucial for developing new therapeutic strategies to treat these conditions.
Molecular motor proteins are a type of protein that convert chemical energy into mechanical work at the molecular level. They play a crucial role in various cellular processes, such as cell division, muscle contraction, and intracellular transport. There are several types of molecular motor proteins, including myosin, kinesin, and dynein.
Myosin is responsible for muscle contraction and movement along actin filaments in the cytoplasm. Kinesin and dynein are involved in intracellular transport along microtubules, moving cargo such as vesicles, organelles, and mRNA to various destinations within the cell.
These motor proteins move in a stepwise fashion, with each step driven by the hydrolysis of adenosine triphosphate (ATP) into adenosine diphosphate (ADP) and inorganic phosphate (Pi). The directionality and speed of movement are determined by the structure and regulation of the motor proteins, as well as the properties of the tracks along which they move.
"Chickens" is a common term used to refer to the domesticated bird, Gallus gallus domesticus, which is widely raised for its eggs and meat. However, in medical terms, "chickens" is not a standard term with a specific definition. If you have any specific medical concern or question related to chickens, such as food safety or allergies, please provide more details so I can give a more accurate answer.
Smooth muscle, also known as involuntary muscle, is a type of muscle that is controlled by the autonomic nervous system and functions without conscious effort. These muscles are found in the walls of hollow organs such as the stomach, intestines, bladder, and blood vessels, as well as in the eyes, skin, and other areas of the body.
Smooth muscle fibers are shorter and narrower than skeletal muscle fibers and do not have striations or sarcomeres, which give skeletal muscle its striped appearance. Smooth muscle is controlled by the autonomic nervous system through the release of neurotransmitters such as acetylcholine and norepinephrine, which bind to receptors on the smooth muscle cells and cause them to contract or relax.
Smooth muscle plays an important role in many physiological processes, including digestion, circulation, respiration, and elimination. It can also contribute to various medical conditions, such as hypertension, gastrointestinal disorders, and genitourinary dysfunction, when it becomes overactive or underactive.
The actin cytoskeleton is a complex, dynamic network of filamentous (threadlike) proteins that provides structural support and shape to cells, allows for cell movement and division, and plays a role in intracellular transport. Actin filaments are composed of actin monomers that polymerize to form long, thin fibers. These filaments can be organized into different structures, such as stress fibers, which provide tension and support, or lamellipodia and filopodia, which are involved in cell motility. The actin cytoskeleton is constantly remodeling in response to various intracellular and extracellular signals, allowing for changes in cell shape and behavior.
Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.
Phosphorylation is the process of adding a phosphate group (a molecule consisting of one phosphorus atom and four oxygen atoms) to a protein or other organic molecule, which is usually done by enzymes called kinases. This post-translational modification can change the function, localization, or activity of the target molecule, playing a crucial role in various cellular processes such as signal transduction, metabolism, and regulation of gene expression. Phosphorylation is reversible, and the removal of the phosphate group is facilitated by enzymes called phosphatases.
An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.
Muscle contraction is the physiological process in which muscle fibers shorten and generate force, leading to movement or stability of a body part. This process involves the sliding filament theory where thick and thin filaments within the sarcomeres (the functional units of muscles) slide past each other, facilitated by the interaction between myosin heads and actin filaments. The energy required for this action is provided by the hydrolysis of adenosine triphosphate (ATP). Muscle contractions can be voluntary or involuntary, and they play a crucial role in various bodily functions such as locomotion, circulation, respiration, and posture maintenance.
'Dictyostelium' is a genus of social amoebae that are commonly found in soil and decaying organic matter. These microscopic organisms have a unique life cycle, starting as individual cells that feed on bacteria. When food becomes scarce, the cells undergo a developmental process where they aggregate together to form a multicellular slug-like structure called a pseudoplasmodium or grex. This grex then moves and differentiates into a fruiting body that can release spores for further reproduction.
Dictyostelium discoideum is the most well-studied species in this genus, serving as a valuable model organism for research in various fields such as cell biology, developmental biology, and evolutionary biology. The study of Dictyostelium has contributed significantly to our understanding of fundamental biological processes like chemotaxis, signal transduction, and cell differentiation.
Myofibrils are the basic contractile units of muscle fibers, composed of highly organized arrays of thick and thin filaments. They are responsible for generating the force necessary for muscle contraction. The thick filaments are primarily made up of the protein myosin, while the thin filaments are mainly composed of actin. Myofibrils are surrounded by a membrane called the sarcolemma and are organized into repeating sections called sarcomeres, which are the functional units of muscle contraction.
In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."
1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.
2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.
3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.
4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).
Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.
I'm not aware of any recognized medical term or condition specifically referred to as "turkeys." The term "turkey" is most commonly used in a non-medical context to refer to the large, bird-like domesticated fowl native to North America, scientifically known as Meleagris gallopavo.
However, if you are referring to a medical condition called "turkey neck," it is a colloquial term used to describe sagging or loose skin around the neck area, which can resemble a turkey's wattle. This condition is not a formal medical diagnosis but rather a descriptive term for an aesthetic concern some people may have about their appearance.
If you meant something else by "turkeys," please provide more context so I can give you a more accurate answer.
Tropomyosin is a protein that plays a crucial role in muscle contraction. It is a long, thin filamentous protein that runs along the length of actin filaments in muscle cells, forming part of the troponin-tropomyosin complex. This complex regulates the interaction between actin and myosin, which are the other two key proteins involved in muscle contraction.
In a relaxed muscle, tropomyosin blocks the myosin-binding sites on actin, preventing muscle contraction from occurring. When a signal is received to contract, calcium ions are released into the muscle cell, which binds to troponin and causes a conformational change that moves tropomyosin out of the way, exposing the myosin-binding sites on actin. This allows myosin to bind to actin and generate force, leading to muscle contraction.
Tropomyosin is composed of two alpha-helical chains that wind around each other in a coiled-coil structure. There are several isoforms of tropomyosin found in different types of muscle cells, including skeletal, cardiac, and smooth muscle. Mutations in the genes encoding tropomyosin have been associated with various inherited muscle disorders, such as hypertrophic cardiomyopathy and distal arthrogryposis.
Skeletal muscle, also known as striated or voluntary muscle, is a type of muscle that is attached to bones by tendons or aponeuroses and functions to produce movements and support the posture of the body. It is composed of long, multinucleated fibers that are arranged in parallel bundles and are characterized by alternating light and dark bands, giving them a striped appearance under a microscope. Skeletal muscle is under voluntary control, meaning that it is consciously activated through signals from the nervous system. It is responsible for activities such as walking, running, jumping, and lifting objects.
Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.
In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.
Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.
Adenosine Triphosphate (ATP) is a high-energy molecule that stores and transports energy within cells. It is the main source of energy for most cellular processes, including muscle contraction, nerve impulse transmission, and protein synthesis. ATP is composed of a base (adenine), a sugar (ribose), and three phosphate groups. The bonds between these phosphate groups contain a significant amount of energy, which can be released when the bond between the second and third phosphate group is broken, resulting in the formation of adenosine diphosphate (ADP) and inorganic phosphate. This process is known as hydrolysis and can be catalyzed by various enzymes to drive a wide range of cellular functions. ATP can also be regenerated from ADP through various metabolic pathways, such as oxidative phosphorylation or substrate-level phosphorylation, allowing for the continuous supply of energy to cells.
Protein isoforms are different forms or variants of a protein that are produced from a single gene through the process of alternative splicing, where different exons (or parts of exons) are included in the mature mRNA molecule. This results in the production of multiple, slightly different proteins that share a common core structure but have distinct sequences and functions. Protein isoforms can also arise from genetic variations such as single nucleotide polymorphisms or mutations that alter the protein-coding sequence of a gene. These differences in protein sequence can affect the stability, localization, activity, or interaction partners of the protein isoform, leading to functional diversity and specialization within cells and organisms.
Skeletal muscle fibers, also known as striated muscle fibers, are the type of muscle cells that make up skeletal muscles, which are responsible for voluntary movements of the body. These muscle fibers are long, cylindrical, and multinucleated, meaning they contain multiple nuclei. They are surrounded by a connective tissue layer called the endomysium, and many fibers are bundled together into fascicles, which are then surrounded by another layer of connective tissue called the perimysium.
Skeletal muscle fibers are composed of myofibrils, which are long, thread-like structures that run the length of the fiber. Myofibrils contain repeating units called sarcomeres, which are responsible for the striated appearance of skeletal muscle fibers. Sarcomeres are composed of thick and thin filaments, which slide past each other during muscle contraction to shorten the sarcomere and generate force.
Skeletal muscle fibers can be further classified into two main types based on their contractile properties: slow-twitch (type I) and fast-twitch (type II). Slow-twitch fibers have a high endurance capacity and are used for sustained, low-intensity activities such as maintaining posture. Fast-twitch fibers, on the other hand, have a higher contractile speed and force generation capacity but fatigue more quickly and are used for powerful, explosive movements.
Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.
In this process:
1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.
EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.
Rho-associated kinases (ROCKs) are serine/threonine kinases that are involved in the regulation of various cellular processes, including actin cytoskeleton organization, cell migration, and gene expression. They are named after their association with the small GTPase RhoA, which activates them upon binding.
ROCKs exist as two isoforms, ROCK1 and ROCK2, which share a high degree of sequence homology and have similar functions. They contain several functional domains, including a kinase domain, a coiled-coil region that mediates protein-protein interactions, and a Rho-binding domain (RBD) that binds to active RhoA.
Once activated by RhoA, ROCKs phosphorylate a variety of downstream targets, including myosin light chain (MLC), LIM kinase (LIMK), and moesin, leading to the regulation of actomyosin contractility, stress fiber formation, and focal adhesion turnover. Dysregulation of ROCK signaling has been implicated in various pathological conditions, such as cancer, cardiovascular diseases, neurological disorders, and fibrosis. Therefore, ROCKs have emerged as promising therapeutic targets for the treatment of these diseases.
Myosin binding protein C, cardiac
Unconventional myosin-Va
Myosin-2
Unconventional myosin-VI
Myosin-11
Unconventional myosin-Ia
Myosin
Myosin light-chain kinase
MYH13
TPM2
MYH14
Pseudoathletic appearance
Skeletal muscle
MYBPC2
Troponin C type 1
Muscular system
Left-right asymmetry
Cytokinesis
MYH3
Protein filament
Meromyosin
Freeman-Sheldon syndrome
MYO7A
AMPA receptor
Martin Antonio
Meat emulsion
Second-harmonic imaging microscopy
Restructured steak
Blebbistatin
Myofilament
Mutations in the gene for cardiac myosin-binding protein C and late-onset familial hypertrophic cardiomyopathy
MYO1B myosin IB [Homo sapiens (human)] - Gene - NCBI
Category:Myosins - Wikimedia Commons
RCSB PDB - 1D1B: DICTYOSTELIUM MYOSIN S1DC (MOTOR DOMAIN FRAGMENT) COMPLEXED WITH O,P-DINITROPHENYL AMINOPROPYLDIPHOSPHATE...
Myosin binding protein C, cardiac - Wikipedia
Identification of lipid binding sites in myosin VI and XXI and regulation by the cargo-binding domain
Nonmuscle myosin-dependent synthesis of type I collagen. | DigiNole
The real story of myosin, jaw muscles, and ancient brains
Figures and data in Drosophila non-muscle myosin II motor activity determines the rate of tissue folding | eLife
Myosin storage myopathy: MedlinePlus Genetics
Effect of different drying methods on the myosin structure, amino acid composition, protein digestibility and volatile profile...
Alpha and beta myosin isoforms and human atrial and ventricular contraction.
Congenital Myopathies: Background, Pathophysiology, Epidemiology
The mechanobiome: a goldmine for cancer therapeutics
MYO2 | SGD
Blebs produced by actin-myosin contraction during apoptosis release damage-associated molecular pattern proteins before...
MYO7A gene: MedlinePlus Genetics
SCIENTIFIC ABSTRACT VARGA, E. - VARGA, F. | CIA FOIA (foia.cia.gov)
MMRRC:043237-MU
RhoA-kinase coordinates F-actin organization and myosin II activity during semaphorin-3A-induced axon retraction | Journal of...
MMRRC:039366-MU
PDF) SVMRFE based approach for prediction of most discriminatory gene target for type II diabetes
Frontiers | An altered transcriptome underlies cln5-deficiency phenotypes in Dictyostelium discoideum
Myosin
Browsing by Subject "Cellular biology"
Light microscopy | LMCB - Laboratory for Molecular Cell Biology - UCL - London's Global University
Myo10 gene cDNA ORF clone, Rattus norvegicus(Norway rat) - GenScript
Volume 99 Issue 1 | Canadian Journal of Animal Science
Filaments12
- Here we show that intact nonmuscle myosin filaments are required for the synthesis of heterotrimeric type I collagen. (fsu.edu)
- LARP6 interacts with nonmuscle myosin through its C-terminal domain and associates collagen mRNAs with the filaments. (fsu.edu)
- Dissociation of nonmuscle myosin filaments results in secretion of collagen alpha1(I) homotrimer, diminished intracellular colocalization of collagen alpha1(I) and alpha2(I) polypeptides (required for folding of the heterotrimer), and their increased intracellular degradation. (fsu.edu)
- Inhibition of the motor function of myosin has similar collagen-specific effects, while disruption of actin filaments has a general effect on protein secretion. (fsu.edu)
- These results indicate that association of collagen mRNAs with nonmuscle myosin filaments is necessary to coordinately synthesize collagen alpha1(I) and alpha2(I) polypeptides. (fsu.edu)
- The rational for the different myosin fragments lies in the different biochemical properties: Full-length myosin forms filaments, sediments at high speed and can be used in the in vitro motility assay. (elifesciences.org)
- Soluble HMM fragments were used in this assay since myosin filaments sediment under the assay conditions. (elifesciences.org)
- Mutations in the MYH7 gene lead to the production of an altered cardiac β-myosin heavy chain protein, which is thought to be less able to form thick filaments. (medlineplus.gov)
- Researchers believe that myosins use long filaments of actin as tracks along which to transport other molecules. (medlineplus.gov)
- Myosin is a major component of thick filaments and exists as a hexamer of 2 heavy chains [ ( PUBMED:1939027 ) ], 2 alkali light chains, and 2 regulatory light chains. (embl.de)
- BACKGROUND: Myosins are motors that use energy supplied by ATP to travel along actin filaments. (embl.de)
- The sarcomeres contain a number of proteins, including alpha actinin, which is the major constituent of the Z band, and actin and myosin, which are the major components of the thin and thick filaments, respectively. (medscape.com)
Protein35
- Mutations in the gene for cardiac myosin-binding protein C account for approximately 15 percent of cases of familial hypertrophic cardiomyopathy. (nih.gov)
- DNA sequences encoding cardiac myosin-binding protein C were determined in unrelated patients with familial hypertrophic cardiomyopathy. (nih.gov)
- The genotypes of these family members were determined, and the clinical status of 212 family members with mutations in the gene for cardiac myosin-binding protein C was assessed. (nih.gov)
- eight defects (insertions, deletions, and splice mutations) were predicted to truncate cardiac myosin-binding protein C. The clinical expression of either missense or truncation mutations was similar to that observed for other genetic causes of hypertrophic cardiomyopathy, but the age at onset of the disease differed markedly. (nih.gov)
- The clinical expression of mutations in the gene for cardiac myosin-binding protein C is often delayed until middle age or old age. (nih.gov)
- Delayed expression of cardiac hypertrophy and a favorable clinical course may hinder recognition of the heritable nature of mutations in the cardiac myosin-binding protein C gene. (nih.gov)
- The myosin-binding protein C, cardiac-type is a protein that in humans is encoded by the MYBPC3 gene. (wikipedia.org)
- cMyBP-C is a myosin-associated protein that binds at 43 nm intervals along the myosin thick filament backbone, stretching for 200 nm on either side of the M-line within the crossbridge-bearing zone (C-region) of the A band in striated muscle. (wikipedia.org)
- In its dephosphorylated state, cMyBP-C binds predominantly to myosin S2 and brakes crossbridge formation, however, when phosphorylated in response to β-adrenergic stimulation through activating cAMP-dependent protein kinase (PKA), it favours binding to actin, then accelerating crossbridge formation, enhancing force development and promoting relaxation. (wikipedia.org)
- Type I collagen, synthesized in all tissues as the heterotrimer of two alpha1(I) polypeptides and one alpha2(I) polypeptide, is the most abundant protein in the human body. (fsu.edu)
- The protein product of MYH16 is one of the heavy chain myosins, a kind of protein that works with actin to enable muscle fibers to contract. (johnhawks.net)
- The protein is denoted as MyHC-M, for myosin heavy chain-masticatory. (johnhawks.net)
- This condition is characterized by the formation of protein clumps, which contain a protein called myosin, within certain muscle fibers. (medlineplus.gov)
- The MYH7 gene provides instructions for making a protein known as the cardiac beta (β)-myosin heavy chain. (medlineplus.gov)
- This protein is found in heart (cardiac) muscle and in type I skeletal muscle fibers, one of two types of fibers that make up the muscles that the body uses for movement. (medlineplus.gov)
- The altered proteins accumulate in type I skeletal muscle fibers, forming the protein clumps characteristic of the disorder. (medlineplus.gov)
- Effect of different drying methods on the myosin structure, amino acid composition, protein digestibility and volatile profile of squid fillets. (oregonstate.edu)
- The impacts of freeze drying (FD), hot-air drying (AD), and heat pump drying (HPD) on myosin structure, amino acid composition, protein digestibility and volatile compounds of squid (Todarodes pacificus) fillets were evaluated. (oregonstate.edu)
- We also examined a wide range of data sets to assess how gene and protein expression levels of these proteins are altered across many different cancer types. (nih.gov)
- Blebbing, apoptotic body formation and protein release during early apoptosis are dependent on ROCK and myosin ATPase activity to drive actomyosin contraction. (nature.com)
- The MYO7A gene provides instructions for making a protein called myosin VIIA, which is part of a group of proteins called unconventional myosins. (medlineplus.gov)
- Myosins interact with actin, a protein that is important for cell movement and shape. (medlineplus.gov)
- Most of the mutations that cause DFNA11 alter a single protein building block (amino acid) in myosin VIIA, resulting in an abnormal protein that does not work properly. (medlineplus.gov)
- Many of these genetic changes alter a single protein building block (amino acid) in critical regions of the myosin VIIA protein. (medlineplus.gov)
- In several instances, such as rheumatoid arthritis, multiple sclerosis, and myocarditis, the autoimmune disease can be induced experimentally by administering self-antigen in the presence of adjuvant (col- lagen, myelin basic protein, and cardiac myosin, respec- tively) (3). (cdc.gov)
- Thus, although myosin was originally thought to be restricted to muscle cells (hence myo- (s) + -in ), there is no single "myosin" but rather a huge superfamily of genes whose protein products share the basic properties of actin binding, ATP hydrolysis (ATPase enzyme activity), and force transduction. (wn.com)
- Because the described cDNAs encode less than half of the protein predicted from immunoblots, we have cloned cDNAs encoding the rest of human myosin-VIIa. (embl-heidelberg.de)
- Nonmuscle myosin II (NMM2) is an actin-based motor protein that plays a crucial role in a variety of cellular processes, including smooth muscle contraction, cell migration, polarity formation, and cytokinesis. (reactome.org)
- NMM2 consists of two myosin heavy chains encoded by MYH9, MYH10, MYH14 (NMHC-IIA, B and C) or MYH11, two copies of MYL6 essential light chain protein, and two regulatory light chains (MRLCs), MYL9 and MYL12B. (reactome.org)
- 1988). Kinases responsible for the phosphorylation include myosin light chain kinase (MLCK), ROCK kinase, citron kinase, myotonic dystrophy kinase-related CDC42-binding protein kinase, and Zipper-interacting protein (ZIP) kinase. (reactome.org)
- In fact, myosin is the most highly acetylated protein found to date with 49 acetylated lysine residues 10 . (cytoskeleton.com)
- Cytoskeleton: Definition, Functions and Types Contents Definition Functions Types Microtubule Intermediate filament Microfilament Cytoskeleton Definition Cytoskeleton is Intracellular network of protein filament present in cytoplasm. (microbiologynotes.org)
- The myosin protein is well known for walking, but now it seems it also sleeps. (cosmosmagazine.com)
- Myosin is a motor protein that helps muscles contract. (cosmosmagazine.com)
- The myosin protein looks like a two-headed tadpole with a very long tail. (cosmosmagazine.com)
Function of myosin3
- Research suggests that one function of myosin VIIA is to carry small sacs of pigment (called melanosomes) within the RPE. (medlineplus.gov)
- The mutations that cause DFNB2 alter the structure and function of myosin VIIA, but they probably do not eliminate the protein's function completely. (medlineplus.gov)
- The structure and function of myosin is strongly conserved across species, to the extent that rabbit muscle myosin II will bind to actin from an amoeba . (wn.com)
ATPase1
- Note that the myosin activity in these assays are even lower than shown since direct actin-mediated hydrolysis of ATP likely accounts for a substantial portion of the ATPase of the unphosphorylated and mutant samples. (elifesciences.org)
Mutations7
- Mutations in the MYH7 gene cause myosin storage myopathy. (medlineplus.gov)
- Armel TZ, Leinwand LA. Mutations in the beta-myosin rod cause myosin storage myopathy via multiple mechanisms. (medlineplus.gov)
- More than 200 mutations in the MYO7A gene have been identified in people with Usher syndrome type I, which is characterized by a combination of hearing loss, vision loss, and problems with balance and coordination. (medlineplus.gov)
- Specifically, MYO7A gene mutations cause a form of the disorder known as Usher syndrome type IB (USH1B), which accounts for more than half of all cases of Usher syndrome type I. (medlineplus.gov)
- Other mutations introduce a premature stop signal in the instructions for making myosin VIIA. (medlineplus.gov)
- Mutations in myosin VIIa (MyoVIIa), an unconventional myosin, have been shown to cause Usher Syndrome Type 1B in humans. (duke.edu)
- Thankfully, the incredible detail they described provides a good model for researching these types of mutations in other myosin-related diseases. (cosmosmagazine.com)
Beta myosin heavy2
- 2002). Divergence in species and regulatory role of beta -myosin heavy chain proximal promoter muscle-CAT elements. (missouri.edu)
- 2001). Multiprotein complex formation at the beta myosin heavy chain distal muscle CAT element correlates with slow muscle expression but not mechanical overload responsiveness. (missouri.edu)
Isoforms6
- Alpha and beta myosin isoforms and human atrial and ventricular contraction. (cam.ac.uk)
- In recent years exploration of the properties of pure α- & β-myosin isoforms have been possible in solution, in isolated myocytes and myofibrils. (cam.ac.uk)
- This allowed us consider what features of contraction can and cannot be ascribed to the myosin isoforms present in the atria and ventricles. (cam.ac.uk)
- Virtually all eukaryotic cells contain myosin isoforms . (wn.com)
- Some isoforms have specialized functions in certain cell types (such as muscle), while other isoforms are ubiquitous . (wn.com)
- We have previously demonstrated that a layer of skeletal muscle cells in the EOMs demonstrate a longitudinal variation in their myosin heavy chain (MyHC) isoforms. (upenn.edu)
Proteins9
- This type of adaptation is dependent on mechanoresponsive proteins that sense and respond to mechanical stress, as well as their regulators. (nih.gov)
- Despite the altered expression patterns of key mechanobiome proteins across many different cancer types, pharmaceutical targeting of these proteins has been overlooked. (nih.gov)
- Here, we review the biochemistry of key mechanoresponsive proteins, specifically nonmuscle myosin II, α-actinins, and filamins, as well as the partnering proteins 14-3-3 and CLP36. (nih.gov)
- Myosin VIIA is also found in other parts of the retina, where it likely carries additional proteins and molecules that are important for vision. (medlineplus.gov)
- Myosins ( / ˈ m aɪ ə s ᵻ n , - oʊ - / ) comprise a family of ATP -dependent motor proteins and are best known for their role in muscle contraction and their involvement in a wide range of other motility processes in eukaryotes . (wn.com)
- The giant spectrin ?V couples the molecular motors to phototransduction and Usher syndrome type I proteins along their trafficking route. (genscript.com)
- During the initial infection, alpha-helical M proteins (M8 and M13) on the surface of the streptococcus bind type IV collagen in the host, and this interaction can trigger auto-antibody formation. (medscape.com)
- Using a broad spectrum anti-acetyl antibody, the researchers determined that one of the acetylated proteins is myosin. (cytoskeleton.com)
- Recently, Foster et al 10 reported that in an initial acetylome of porcine heart proteins, 240 proteins were modified on 994 lysine residues with myosin acetylated on many different lysine amino acids. (cytoskeleton.com)
Chains2
- The top panel shows the myosin hexamer composed of two myosin heavy chains (green), two ELCs (light blue) and two RLCs (gray). (elifesciences.org)
- May be a homodimer, which associates with multiple calmodulin or myosin light chains. (lu.se)
Gene5
- MYBPC3 was thus the fourth gene for hypertrophic cardiomyopathy, following MYH7, encoding β-myosin heavy chain, TNNT2 and TPM1, encoding cardiac troponin T and α-tropomyosin, respectively, earmarking hypertrophic cardiomyopathy as a disease of the sarcomere. (wikipedia.org)
- Phenotype annotations for a gene are curated single mutant phenotypes that require an observable (e.g., "cell shape"), a qualifier (e.g., "abnormal"), a mutant type (e.g., null), strain background, and a reference. (yeastgenome.org)
- Molecular cloning and domain structure of human myosin-VIIa, the gene product defective in Usher syndrome 1B. (embl-heidelberg.de)
- TEA domain-1 (TEAD1) transcription factor participates in both slow oxidative fiber type gene expression and plays a role in satellite cell biology. (missouri.edu)
- 2009). IGF-I activates the mouse type IIb myosin heavy chain gene. (missouri.edu)
Activation of myosin1
- Collectively, these observations suggest that guidance cues cause axon retraction through the coordinated activation of myosin II and the formation of intra-axonal F-actin bundles for myosin-II-based force generation. (biologists.com)
Storage myopathy5
- Myosin storage myopathy is a condition that causes muscle weakness (myopathy) that does not worsen or worsens very slowly over time. (medlineplus.gov)
- The signs and symptoms of myosin storage myopathy usually become noticeable in childhood, although they can occur later. (medlineplus.gov)
- Myosin storage myopathy is a rare condition. (medlineplus.gov)
- It is unclear how these changes lead to muscle weakness in people with myosin storage myopathy. (medlineplus.gov)
- Tajsharghi H, Thornell LE, Lindberg C, Lindvall B, Henriksson KG, Oldfors A. Myosin storage myopathy associated with a heterozygous missense mutation in MYH7. (medlineplus.gov)
Unconventional myosin1
- Myosin-VIIa is an unconventional myosin with relatively restricted expression. (embl-heidelberg.de)
Nonmuscle2
Interacts1
- Myosin II interacts with F-actin to generate contractile forces that result in axon retraction. (biologists.com)
Isoform2
- Notably, the ventricle expresses predominantly β-cardiac myosin while the atrium expresses mostly the α-isoform. (cam.ac.uk)
- This allows us to consider the extent to which the atrial vs ventricular mechanical characteristics are defined by the myosin isoform expressed, and how the isoform properties are matched to their physiological roles. (cam.ac.uk)
Inhibition1
- In this study, we analyzed bile canaliculi dynamics, Rho kinase (ROCK)/myosin light chain kinase (MLCK) pathway implication, efflux inhibition of taurocholate [a predominant bile salt export pump (BSEP) substrate], and expression of the major canalicular and basolateral bile acid transporters. (aspetjournals.org)
Heavy5
- A ) Domain organization of the myosin heavy chain and myosin fragments used to study the biochemical properties of myosin. (elifesciences.org)
- The myosin motor domain, the light chain binding neck and the tail domain of the heavy chain are indicated. (elifesciences.org)
- RLC and mutant RLC (19 kDa) and the ELC (16 kDa) bind in a 1:1 stoichiometry to the myosin heavy chain, indicating that mutant RLCs bind with a similar affinity as RLC-TS. (elifesciences.org)
- Cardiac β-myosin heavy chain is the major component of the thick filament in muscle cell structures called sarcomeres . (medlineplus.gov)
- Both young and old rats displayed an increase in developmental myosin heavy chain (MHCdev+) labeling in the exposed muscle, indicating muscle regeneration. (cdc.gov)
Binds1
- In addition to myosin, cMyBP-C also binds titin and actin. (wikipedia.org)
Activates2
- I report that semaphorin 3A activates myosin II in growth cones and axons. (biologists.com)
- The structure of myosin is known, but the actin-binding site is not well defined, and the mechanisms by which actin activates ATP hydrolysis by myosin, and myosin moves relative to the actin filament, developing force, are not fully understood. (embl.de)
VIIA6
- Myosin VIIA is made in the inner ear and in the retina, which is the light-sensitive tissue at the back of the eye. (medlineplus.gov)
- In the inner ear, myosin VIIA plays a role in the development and maintenance of hairlike projections called stereocilia. (medlineplus.gov)
- In the retina, myosin VIIA is found primarily in a thin layer of cells called the retinal pigment epithelium (RPE). (medlineplus.gov)
- Myosin VIIA probably plays a role in the development and maintenance of this tissue, which supports and nourishes the retina. (medlineplus.gov)
- Domain present twice in myosin-VIIa, and also present in 3 other myosins. (embl-heidelberg.de)
- Defects in myosin-VIIa cause the shaker-1 phenotype in mice and Usher syndrome 1B in human, which are characterized by deafness, lack of vestibular function, and (in human) progressive retinal degeneration. (embl-heidelberg.de)
Genes2
- To further validate the results pathway study was performed to identify the involvement of the coding genes in type II diabetes. (researchgate.net)
- Following the discovery by Pollard and Korn (1973) of enzymes with myosin-like function in Acanthamoeba castellanii , a large number of divergent myosin genes have been discovered throughout eukaryotes. (wn.com)
Muscle4
- MYH2 (Myosin-2) is associated with muscle contraction and is required for cytoskeleton organization. (thermofisher.com)
- The microtubule-based kinesin motors and actin-based myosin motors generate movements required for intracellular trafficking, cell division, and muscle contraction. (embl-heidelberg.de)
- Muscle contraction consists of a cyclical interaction between myosin and actin. (embl.de)
- A major interest of my lab is to better understand the mechanism(s) by which skeletal muscle fiber type composition is regulated. (missouri.edu)
Ventricular1
- According to Kaski, there have several innovations in HCM since the previous guidelines, such as when to consider cardiac myosin inhibitors for symptomatic left ventricular outflow tract obstruction. (medscape.com)
Myo101
- Rattus norvegicus myosin X (Myo10), mRNA. (genscript.com)
Residues2
- We set out to analyse the positions of conserved residues within this domain in detail, and relate the conserved residues to the myosin structure. (embl.de)
- Modified lysine residues occurred in the actin binding region as well as the coiled-coil tail and the hinge regions of myosin (see Fig. 1). (cytoskeleton.com)
Amino acid1
- Therefore, the effects of interactions between polyphenols and myosin after freezing on myosin gel and digestive properties were investigated using low field NMR, a texture analyzer, a dynamic rheometer, ultraviolet-visible spectra, scanning electron microscopy , LC-MS/MS, an automatic amino acid analyzer, etc. (bvsalud.org)
Molecules2
- The approximate stoichiometry of cMyBP-C along the thick filament is 1 per 9-10 myosin molecules, or 37 cMyBP-C molecules per thick filament. (wikipedia.org)
- This helps other molecules move the myosin around the cell for use later. (cosmosmagazine.com)
Inhibitors2
- The importance of acetylation has recently been elevated by the utilization of histone deacetylase (HDAC) inhibitors in pre-clinical research and the treatment of hypertrophic heart disease 6,7 , as well as the discovery of several critical acetylated forms of myosin amino acids that need to be modified in order for the sarcomere to function correctly 8,9 . (cytoskeleton.com)
- These results indicate that HBVP, in an in vitro model of microvasculature, respond morphologically to vasoconstrictors, dilators, and myosin inhibitors. (lu.se)
Retina1
- In the past few years, this premise has been supported by genetic evidence that has shown that unconventional myosins are essential for the proper functioning of neurons, retina and the sensory cells of the inner ear. (embl.de)
Actomyosin1
- The presence of ATP disassembles the actomyosin complex and myosin mostly remains in the supernatant. (elifesciences.org)
Drosophila1
- Purification and characterization of wild-type and mutant Drosophila myosin ( A ) PageBlue-stained 4-12% Bis-Tris gel showing recombinant HMM (160 kDa) and full-length (228 kDa) RLC-TS or RLC mutants. (elifesciences.org)
Biochemical2
- Biochemical and physiological evidence has suggested that myosins, both conventional and unconventional, are critical for neurosensory activities. (embl.de)
- Given the prominence of myosin as a target for acetylation in cardiomyocytes, further biochemical and functional studies were undertaken. (cytoskeleton.com)
Kinesin2
- The MyTH4 domain is found in one or two copies associated with other domains, such as myosin head, kinesin motor, FERM, PH, SH3 and IQ. (embl-heidelberg.de)
- The core of the myosin structure is similar in fold to that of kinesin. (embl.de)
Digestibility1
- Meanwhile, the four types of polyphenols under study significantly improved the gastric and gastrointestinal digestibility of myosin . (bvsalud.org)
Regulates2
- cMyBP-C regulates the positioning of myosin and actin for interaction and acts as a tether to the myosin S1 heads, limiting their mobility. (wikipedia.org)
- We postulate that LARP6/myosin-dependent mechanism regulates the synthesis of heterotrimeric type I collagen by coordinating the translation of collagen mRNAs. (fsu.edu)
Molecular1
- Myosin-X is a molecular motor that functions in filopodia formation. (genscript.com)
Muscles2
- The three types of muscles are striated (or skeletal), cardiac, and smooth (or nonstriated). (britannica.com)
- Notably, a given muscles fiber-type composition is not static, but instead, fiber-type composition is remarkably adaptable (fastàslow-twitch fibers or slowàfast-twitch fibers) to a broad spectrum of stimuli that include altered weight-bearing (increase load bearing, zero gravity), endocrine factors, altitude, endurance & resistance training, and diet (high fat vs high carbohydrate). (missouri.edu)
Diabetes mellitus4
- Despite the fact that sexual differences increase diabetic risk and contribute to the need for gender-specific care, there remain contradictory results as to whether or not sexual dimorphism increases susceptibility to the development of type 1 diabetes mellitus. (karger.com)
- Type 1 diabetes mellitus (T1DM) results from autoimmune destruction of pancreatic β-cells, leading to absolute insulin deficiency in patients as well as a requirement for exogenous insulin supplementation for survival [ 6 ]. (karger.com)
- Autoantibodies may be present many years before the diagnosis of diseases such as rheumatoid arthritis (RA), systemic lupus erythematosus (SLE), Type 1 diabetes mellitus (DM) and antiphospholipid syndrome. (ppdg.net)
- However, IAPP aggregates, related to type 2 diabetes mellitus (T2DM), are toxic not only for the pancreas, but also for the brain. (lu.se)
Cytokinesis1
- Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. (joplink.net)