Nonmuscle Myosin Type IIB
Nonmuscle Myosin Type IIA
Myosins
Myosin Type IV
Myosin Type II
Myosin Heavy Chains
Myosin Type III
Sodium-Phosphate Cotransporter Proteins, Type IIb
Heterocyclic Compounds with 4 or More Rings
Myosin Type I
Myosin Light Chains
Myosin Type V
Myosin Subfragments
Molecular Motor Proteins
Actins
Actomyosin
Myosin-Light-Chain Kinase
Protein Isoforms
Molecular Sequence Data
Myosin-Light-Chain Phosphatase
Muscle, Striated
Amino Acid Sequence
Sodium-Phosphate Cotransporter Proteins, Type II
Actin Cytoskeleton
Prolyl-Hydroxylase Inhibitors
Cytoskeleton
Activin Receptors, Type II
rho-Associated Kinases
von Willebrand Diseases
Sodium-Phosphate Cotransporter Proteins
Muscle Fibers, Fast-Twitch
BTEB2, a Kruppel-like transcription factor, regulates expression of the SMemb/Nonmuscle myosin heavy chain B (SMemb/NMHC-B) gene. (1/173)
We have recently characterized the promoter region of the rabbit embryonic smooth muscle myosin heavy chain (SMemb/NMHC-B) gene and identified the 15-bp sequence, designated SE1, located at -105 from the transcriptional start site as an important regulatory element for its transcriptional activity in a smooth muscle cell (SMC) line. In this study, we attempted to isolate cDNA clones encoding for the transcription factors that control the expression of the SMemb gene through binding to this cis-regulatory element. We screened a lambdagt11 cDNA library prepared from C2/2 cells, a rabbit-derived SMC line, by using a radiolabeled concatenated oligonucleotide containing SE1 as a probe. Sequence analysis revealed that one of the cDNA clones corresponds to the rabbit homologue of basic transcriptional element binding protein-2 (BTEB2), which has previously been identified as one of the Kruppel-like transcription factor. Gel mobility shift assays and antibody supershift analyses with nuclear extracts from C2/2 cells indicate that BTEB2 is a major component of nuclear factor:SE1 complexes. Furthermore, a glutathione S-transferase-BTEB2 fusion protein binds to the SE1 in a sequence-specific manner. In support of the functionality of BTEB2 binding, basal promoter activity and BTEB2-induced transcriptional activation were markedly attenuated by the disruption of the SE1. In adult rabbit tissues, BTEB2 mRNA was most highly expressed in intestine, urinary bladder, and uterus. BTEB2 mRNA levels were downregulated in rabbit aorta during normal development. Moreover, immunohistochemical analysis indicated a marked induction of BTEB2 protein in the neointimal SMC after balloon injury in rat aorta. These results suggest that BTEB2 mediates the transcriptional regulation of the SMemb/NMHC-B gene and possibly plays a role in regulating gene expression during phenotypic modulation of vascular SMC. (+info)A link between RNA interference and nonsense-mediated decay in Caenorhabditis elegans. (2/173)
Double-stranded RNA (dsRNA) inhibits expression of homologous genes by a process involving messenger RNA degradation. To gain insight into the mechanism of degradation, we examined how RNA interference is affected by mutations in the smg genes, which are required for nonsense-mediated decay. For three of six smg genes tested, mutations resulted in animals that were initially silenced by dsRNA but then recovered; wild-type animals remained silenced. The levels of target messenger RNAs were restored during recovery, and RNA editing and degradation of the dsRNA were identical to those of the wild type. We suggest that persistence of RNA interference relies on a subset of smg genes. (+info)Alterations in expression of myosin and myosin light chain kinases in response to vascular injury. (3/173)
Histochemical analysis of balloon-injured rat carotid arteries revealed a coordinated expression of nonmuscle myosin heavy chain-A and -B (NM-A and NM-B) in response to injury. Expression of these nonmuscle myosin forms shifts from the media to the adventitia and intima. In contrast, expression of smooth muscle myosin heavy chain-1 (SM-1) within the media is not altered, whereas smooth muscle myosin heavy chain-2 (SM-2) expression declines. Western blotting shows a statistically significant increase in expression of NM-A that occurs within 6 h in response to carotid injury, suggesting this myosin form may be an appropriate experimental marker for proliferating, migrating cells in injured vessels. No overall change in the relative expression level of NM-B was detected, suggesting that compensatory declines in media expression are balanced by increases in the intima and adventitia. Expression of SM-1 did not change in response to injury, whereas the expression of SM-2 significantly declined between 24 h and 7 days. Expression of myosin light chain kinase is also negatively regulated, and the decline in its expression parallels downregulation of SM-2. (+info)Mutations in sarcomere protein genes as a cause of dilated cardiomyopathy. (4/173)
BACKGROUND: The molecular basis of idiopathic dilated cardiomyopathy, a primary myocardial disorder that results in reduced contractile function, is largely unknown. Some cases of familial dilated cardiomyopathy are caused by mutations in cardiac cytoskeletal proteins; this finding implicates defects in contractile-force transmission as one mechanism underlying this disorder. To elucidate this important cause of heart failure, we investigated other genetic causes of dilated cardiomyopathy. METHODS: Clinical evaluations were performed in 21 kindreds with familial dilated cardiomyopathy. A genome-wide linkage study prompted a search of the genes encoding beta-myosin heavy chain, troponin T, troponin I, and alpha-tropomyosin for disease-causing mutations. RESULTS: A genetic locus for mutations associated with dilated cardiomyopathy was identified at chromosome 14q11.2-13 (maximal lod score, 5.11; theta=0), where the gene for cardiac beta-myosin heavy chain is encoded. Analyses of this and other genes for sarcomere proteins identified disease-causing dominant mutations in four kindreds. Cardiac beta-myosin heavy-chain missense mutations (Ser532Pro and Phe764Leu) and a deletion in cardiac troponin T (deltaLys210) caused early-onset ventricular dilatation (average age at diagnosis, 24 years) and diminished contractile function and frequently resulted in heart failure. Affected persons had neither antecedent cardiac hypertrophy (average maximal left-ventricular-wall thickness, 8.5 mm) nor histopathological findings characteristic of hypertrophy. CONCLUSION: Mutations in sarcomere protein genes account for approximately 10 percent of cases of familial dilated cardiomyopathy and are particularly prevalent in families with early-onset ventricular dilatation and dysfunction. Because distinct mutations in sarcomere proteins cause either dilated or hypertrophic cardiomyopathy, the effects of mutant sarcomere proteins on muscle mechanics must trigger two different series of events that remodel the heart. (+info)Homeobox protein Hex induces SMemb/nonmuscle myosin heavy chain-B gene expression through the cAMP-responsive element. (5/173)
Recent studies have shown that the homeobox gene Hex plays an important role in inducing differentiation of vascular endothelial cells. In this study, we examined the expression of Hex in vascular smooth muscle cells (VSMCs) in vitro and in vivo. Immunohistochemistry showed a marked induction of Hex protein in neointimal VSMCs after balloon injury in rat aorta. Western and reverse transcriptase-polymerase chain reaction analyses demonstrated that Hex was abundantly expressed in cultured VSMCs, whereas it was undetectable in other cell types or in normal aorta. The expression pattern of Hex was similar to that of SMemb/NMHC-B, a nonmuscle isoform of myosin heavy chain that we have previously reported to be a molecular marker of dedifferentiated VSMCs. We next examined the role of Hex in SMemb gene transcription. Promoter analysis demonstrated that the sequence identical to consensus cAMP-responsive element (CRE) located at -481 of the SMemb promoter was critical for Hex responsiveness. Mutant Hex expression vector, which lacks the homeodomain, failed to stimulate SMemb gene transcription, suggesting the requirement of the homeodomain for its transactivation. Elecrophoretic mobility shift assay showed that Hex binds to a consensus binding sequence for homeobox proteins, but not to CRE. Cotransfection of protein kinase A expression vector increased the ability of Hex to stimulate SMemb promoter activity in a CRE-dependent manner. Overexpression of CRE binding protein (CREB), but not Mut-CREB which contains mutation at Ser133, strongly activated Hex-induced SMemb promoter activity. These results suggest that Hex mediates transcriptional induction of the SMemb/NMHC-B gene via its homeodomain, and Hex can function as a transcriptional modulator of CRE-dependent transcription in VSMCs. (+info)Involvement of Flt-1 tyrosine kinase (vascular endothelial growth factor receptor-1) in pathological angiogenesis. (6/173)
Vascular endothelial growth factor (VEGF) and its two receptors, Fms-like tyrosine kinase 1 (Flt-1) (VEGFR-1) and KDR/Flk-1 (VEGFR-2), have been demonstrated to be an essential regulatory system for blood vessel formation in mammals. KDR is a major positive signal transducer for angiogenesis through its strong tyrosine kinase activity. Flt-1 has a unique biochemical activity, 10-fold higher affinity to VEGF, whereas much weaker tyrosine kinase activity compared with KDR. Recently, we and others have shown that Flt-1 has a negative regulatory function for physiological angiogenesis in the embryo, possibly with its strong VEGF-trapping activity. However, it is still open to question whether the tyrosine kinase of Flt-1 has any positive role in angiogenesis at adult stages. In this study, we examined whether Flt-1+ could be a positive signal transducer under certain pathological conditions, such as angiogenesis with tumors overexpressing a Flt-1-specific, VEGF-related ligand. Our results show clearly that murine Lewis lung carcinoma cells overexpressing placenta growth factor-2, an Flt-1-specific ligand, grew in wild-type mice much faster than in Flt-1 tyrosine kinase domain-deficient mice. Blood vessel formation in tumor tissue was higher in wild-type mice than in Flt-1 tyrosine kinase-deficient mice. On the other hand, the same carcinoma cells overexpressing VEGF showed no clear difference in the tumor growth rate between these two genotypes of mice. These results indicate that Flt-1 is a positive regulator using its tyrosine kinase under pathological conditions when the Flt-1-specific ligand is abnormally highly expressed. Thus, Flt-1 has a dual function in angiogenesis, acting in a positive or negative manner in different biological conditions. (+info)Suppression of the tumorigenicity of mutant p53-transformed rat embryo fibroblasts through expression of a newly cloned rat nonmuscle myosin heavy chain-B. (7/173)
In our previous study, a rat homolog of human nonmuscle myosin heavy chain-B (nmMHC-B) was identified by mRNA differential display comparing of transformed against nontransformed Rat 6 cells overexpressing mutant p53val135 gene. The nmMHC-B was found to be expressed in normal Rat 6 embryo fibroblast cell line, but markedly suppressed in the mutant p53val135-transformed Rat 6 cells. To examine the possible involvement of nmMHC-B in cell transformation, we first cloned and sequenced the full length cDNA of rat nmMHC-B, which was then cloned into an ecdysone-expression vector. The resulting construct was introduced into the T2 cell line, a mutant p53val135-transformed Rat 6 cells lacking the expression of the endogenous nmMHC-B. The clonal transfectants, expressing muristerone A-induced nmMHC-B, displayed a slightly flatter morphology and reached to a lower saturation density compared to the parental transformed cells. Reconstitution of actin filamental bundles was also clearly seen in cells overexpressing the nmMHC-B. In soft agar assays, nmMHC-B transfectants formed fewer and substantially smaller colonies than the parental cells in response to muristerone A induction. Moreover, it was strikingly effective in suppressing the tumorigenicity of the T2 cells when tested in nude mice. Thus, the nmMHC-B, known as a component of the cytoskeletal network, may act as a tumor suppressor gene. Our current finding may reveal a novel role of nmMHC-B in regulating cell growth and cell signaling in nonmuscle cells. Oncogene (2001) 20, 58 - 68. (+info)Impaired sarcoplasmic reticulum function leads to contractile dysfunction and cardiac hypertrophy. (8/173)
Sarcoplasmic reticulum (SR)-mediated Ca(2+) sequestration and release are important determinants of cardiac contractility. In end-stage heart failure SR dysfunction has been proposed to contribute to the impaired cardiac performance. In this study we tested the hypothesis that a targeted interference with SR function can be a primary cause of contractile impairment that in turn might alter cardiac gene expression and induce cardiac hypertrophy. To study this we developed a novel animal model in which ryanodine, a substance that alters SR Ca(2+) release, was added to the drinking water of mice. After 1 wk of treatment, in vivo hemodynamic measurements showed a 28% reduction in the maximum speed of contraction (+dP/dt(max)) and a 24% reduction in the maximum speed of relaxation (-dP/dt(max)). The slowing of cardiac relaxation was confirmed in isolated papillary muscles. The late phase of relaxation expressed as the time from 50% to 90% relaxation was prolonged by 22%. After 4 wk of ryanodine administration the animals had developed a significant cardiac hypertrophy that was most prominent in both atria (right atrium +115%, left atrium +100%, right ventricle +23%, and left ventricle +13%). This was accompanied by molecular changes including a threefold increase in atrial natriuretic factor mRNA and a sixfold increase in beta-myosin heavy chain mRNA. Sarcoplasmic endoplasmic reticulum Ca(2+) mRNA was reduced by 18%. These data suggest that selective impairment of SR function in vivo can induce changes in cardiac gene expression and promote cardiac growth. (+info)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.
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.
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 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.
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 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.
Sodium-phosphate cotransporter proteins, type IIb (NaPi-IIb), are membrane transport proteins found in the kidney's brush border membrane of proximal tubule cells. They play a crucial role in reabsorbing inorganic phosphate from the primary urine back into the bloodstream. These cotransporters facilitate the active transport of phosphate ions (PO4^3-) coupled with sodium ions (Na+) through the cell membrane, using the energy derived from the electrochemical gradient of sodium ions.
Type IIb sodium-phosphate cotransporters are specifically expressed in the kidney and contribute to maintaining phosphate homeostasis in the body. Disorders in NaPi-IIb function can lead to abnormal phosphate levels, which may be associated with various medical conditions such as hypophosphatemia or hyperphosphatemia.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Striated muscle, also known as skeletal or voluntary muscle, is a type of muscle tissue that is characterized by the presence of distinct light and dark bands, or striations, when viewed under a microscope. These striations correspond to the arrangement of sarcomeres, which are the functional units of muscle fibers.
Striated muscle is under voluntary control, meaning that it is consciously activated by signals from the nervous system. It is attached to bones via tendons and is responsible for producing movements of the body. Striated muscle fibers are multinucleated, meaning that they contain many nuclei, and are composed of numerous myofibrils, which are rope-like structures that run the length of the fiber.
The myofibrils are composed of thick and thin filaments that slide past each other to cause muscle contraction. The thick filaments are made up of the protein myosin, while the thin filaments are composed of actin, tropomyosin, and troponin. When a nerve impulse arrives at the muscle fiber, it triggers the release of calcium ions from the sarcoplasmic reticulum, which bind to troponin and cause a conformational change that exposes the binding sites on actin for myosin. The myosin heads then bind to the actin filaments and pull them towards the center of the sarcomere, causing the muscle fiber to shorten and contract.
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.
Sodium-phosphate cotransporter proteins, type II (NPTII), are a group of membrane transport proteins that facilitate the active transport of inorganic phosphate (Pi) and sodium ions (Na+) across the cell membrane. They play a crucial role in maintaining intracellular phosphate homeostasis and regulating various physiological processes, including energy metabolism, signal transduction, and bone mineralization.
The type II sodium-phosphate cotransporters are further divided into three subtypes: NPT2a, NPT2b, and NPT2c. These subtypes differ in their tissue distribution, substrate affinity, and regulatory mechanisms. NPT2a is primarily expressed in the kidney proximal tubules and plays a major role in reabsorbing phosphate from the glomerular filtrate. NPT2b is predominantly found in the small intestine and contributes to phosphate absorption from the diet. NPT2c is widely distributed, with significant expression in the kidney, brain, and testis, although its specific functions are not as well understood as those of NPT2a and NPT2b.
Dysregulation of sodium-phosphate cotransporter proteins, type II, has been implicated in several pathological conditions, such as renal phosphate wasting disorders, tumoral calcinosis, and certain forms of hyperparathyroidism.
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.
Prolyl-hydroxylase inhibitors (PHI) are a class of pharmaceutical compounds that function as inhibitors of prolyl-hydroxylase enzymes. These enzymes play a crucial role in the regulation of hypoxia-inducible factors (HIF), which are transcription factors that respond to changes in oxygen levels in the body.
Under normal conditions, prolyl-hydroxylase enzymes hydroxylate specific residues on HIF proteins, leading to their degradation by other proteins. However, when oxygen levels are low (hypoxia), these enzymes become less active, allowing HIF proteins to accumulate and activate genes that help the body adapt to low-oxygen conditions.
PHIs work by inhibiting prolyl-hydroxylase enzymes, which in turn leads to an increase in HIF protein levels and activation of HIF-dependent genes. This effect can be useful in treating certain medical conditions, such as anemia associated with chronic kidney disease (CKD). In CKD, the kidneys are unable to produce enough erythropoietin, a hormone that stimulates red blood cell production. By increasing HIF protein levels, PHIs can stimulate the production of erythropoietin and improve anemia symptoms in patients with CKD.
Examples of PHIs include roxadustat, vadadustat, and daprodustat, which are currently under investigation for the treatment of anemia associated with CKD.
The cytoskeleton is a complex network of various protein filaments that provides structural support, shape, and stability to the cell. It plays a crucial role in maintaining cellular integrity, intracellular organization, and enabling cell movement. The cytoskeleton is composed of three major types of protein fibers: microfilaments (actin filaments), intermediate filaments, and microtubules. These filaments work together to provide mechanical support, participate in cell division, intracellular transport, and help maintain the cell's architecture. The dynamic nature of the cytoskeleton allows cells to adapt to changing environmental conditions and respond to various stimuli.
Activin receptors, type II, are a subgroup of serine/threonine kinase receptors that play a crucial role in signal transduction pathways involved in various biological processes, including cell growth, differentiation, and apoptosis. There are two types of activin receptors, Type IIA (ACVR2A) and Type IIB (ACVR2B), which are single-pass transmembrane proteins with an extracellular domain that binds to activins and a cytoplasmic domain with kinase activity.
Activins are dimeric proteins that belong to the transforming growth factor-β (TGF-β) superfamily, and they play essential roles in regulating developmental processes, reproduction, and homeostasis. Activin receptors, type II, function as primary binding sites for activins, forming a complex with Type I activin receptors (ALK4, ALK5, or ALK7) to initiate downstream signaling cascades.
Once the activin-receptor complex is formed, the intracellular kinase domain of the Type II receptor phosphorylates and activates the Type I receptor, which in turn propagates the signal by recruiting and phosphorylating downstream effectors such as SMAD proteins. Activated SMADs then form a complex and translocate to the nucleus, where they regulate gene expression.
Dysregulation of activin receptors, type II, has been implicated in various pathological conditions, including cancer, fibrosis, and developmental disorders. Therefore, understanding their function and regulation is essential for developing novel therapeutic strategies to target these diseases.
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.
Von Willebrand disease (vWD) is a genetic bleeding disorder caused by deficiency or dysfunction of the von Willebrand factor (VWF), a protein involved in blood clotting. The VWF plays a crucial role in the formation of a stable platelet plug during the process of hemostasis, which helps to stop bleeding.
There are three main types of vWD:
1. Type 1: This is the most common form, characterized by a partial quantitative deficiency of functional VWF. Bleeding symptoms are usually mild.
2. Type 2: In this type, there is a qualitative defect in the VWF protein leading to various subtypes (2A, 2B, 2M, and 2N) with different bleeding patterns. Symptoms can range from mild to severe.
3. Type 3: This is the most severe form of vWD, characterized by a near or complete absence of functional VWF and Factor VIII. Affected individuals have a high risk of spontaneous and severe bleeding episodes.
The clinical manifestations of vWD include easy bruising, prolonged nosebleeds (epistaxis), heavy menstrual periods in women, and excessive bleeding after dental procedures, surgeries, or trauma. The diagnosis is made based on laboratory tests that assess VWF antigen levels, VWF activity, and Factor VIII coagulant activity. Treatment options include desmopressin (DDAVP) to stimulate the release of VWF from endothelial cells, recombinant VWF, or plasma-derived VWF concentrates, and antifibrinolytic agents like tranexamic acid to reduce bleeding.
Sodium-phosphate cotransporter proteins are membrane transport proteins that facilitate the active transport of sodium and inorganic phosphate ions across biological membranes. These proteins play a crucial role in maintaining phosphate homeostasis within the body by regulating the absorption and excretion of phosphate in the kidneys and intestines. They exist in two major types, type I (NaPi-I) and type II (NaPi-II), each having multiple subtypes with distinct tissue distributions and regulatory mechanisms.
Type I sodium-phosphate cotransporters are primarily expressed in the kidney's proximal tubules and play a significant role in reabsorbing phosphate from the primary urine back into the bloodstream. Type II sodium-phosphate cotransporters, on the other hand, are found in both the kidneys and intestines. In the kidneys, they contribute to phosphate reabsorption, while in the intestines, they facilitate phosphate absorption from food.
These proteins function by coupling the passive downhill movement of sodium ions (driven by the electrochemical gradient) with the active uphill transport of phosphate ions against their concentration gradient. This coupled transport process enables cells to maintain intracellular phosphate concentrations within a narrow range, despite fluctuations in dietary intake and renal function.
Dysregulation of sodium-phosphate cotransporter proteins has been implicated in various pathological conditions, such as chronic kidney disease (CKD), tumoral calcinosis, and certain genetic disorders affecting phosphate homeostasis.
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.
Fast-twitch muscle fibers, also known as type II fibers, are a type of skeletal muscle fiber that are characterized by their rapid contraction and relaxation rates. These fibers have a larger diameter and contain a higher concentration of glycogen, which serves as a quick source of energy for muscle contractions. Fast-twitch fibers are further divided into two subcategories: type IIa and type IIb (or type IIx). Type IIa fibers have a moderate amount of mitochondria and can utilize both aerobic and anaerobic metabolic pathways, making them fatigue-resistant. Type IIb fibers, on the other hand, have fewer mitochondria and primarily use anaerobic metabolism, leading to faster fatigue. Fast-twitch fibers are typically used in activities that require quick, powerful movements such as sprinting or weightlifting.
List of MeSH codes (D08)
List of MeSH codes (D12.776)
List of MeSH codes (D05)
MYH10
MYH1
Myosin-2
Blebbistatin
MYH4
Tropomyosin
Actin
MYH14
Skeletal muscle
MYH9
List of MeSH codes (D08) - Wikipedia
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Isoforms4
- We have addressed the function of one of the isoforms of myosin II, myosin IIB, by analyzing the movement and mechanical characteristics of fibroblasts where this protein has been ablated by gene disruption. (umassmed.edu)
- The technique described here can be used to identify specific myosin heavy chain (MHC) isoforms in segments of individual muscle fibers using dot blotting, hereafter referred to as Myosin heavy chain detection by Dot Blotting for IDentification of muscle fiber type (MyDoBID). (bvsalud.org)
- 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)
Phosphorylation3
- Work done using smooth muscle myosin and mammalian non-muscle myosin have demonstrated that phosphorylation of the RLC at conserved Serine and Threonine sites ( Figure 1B , Serine-19 and Threonine-18) activates myosin motor activity, enhances the affinity of myosin for actin, and promotes myosin filament assembly ( Heissler and Sellers, 2016 ). (elifesciences.org)
- However, it has not been biochemically demonstrated that Drosophila myosin motor activity and filament assembly is regulated by RLC phosphorylation or whether the extent of activation is similar to that of mammalian systems. (elifesciences.org)
- These effects were mediated via the down-regulation of caspase-3, ROCK1 (Rho-associated kinase1) activation and myosin light chain (MLC, Ser-19) phosphorylation. (ijbs.com)
Activates myosin1
- I report that semaphorin 3A activates myosin II in growth cones and axons. (biologists.com)
Cytoskeleton1
- Although, the non-muscle myosin II holoenzyme (myosin) is a molecular motor that powers contraction of actin cytoskeleton networks, recent studies have questioned the importance of myosin motor activity cell and tissue shape changes. (elifesciences.org)
Protein8
- The MYH9 gene provides instructions for making a protein called myosin-9. (medlineplus.gov)
- This protein is one part (subunit) of the myosin IIA protein. (medlineplus.gov)
- Each type of myosin II protein consists of two heavy chains and four light chains. (medlineplus.gov)
- Most of the mutations that cause this condition change single protein building blocks (amino acids) in the myosin-9 protein. (medlineplus.gov)
- Mutations that are located near the head of the myosin protein tend to lead to a more severe disorder than mutations that are located toward the tail of the protein. (medlineplus.gov)
- A nonfunctional myosin-9 protein cannot properly interact with other subunits to form myosin IIA. (medlineplus.gov)
- Nonmuscle myosin II (NM-II) is an important motor protein involved in cell migration. (nih.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)
Regulates3
- To study the molecular mechanism by which nonmuscle myosin II (MII) regulates protrusion and adhesion dynamics in migrating cells, Swiss3T3 cells were co-stained for βPIX (green) and myosin IIB (red). (ucsd.edu)
- To study the molecular mechanism by which nonmuscle myosin II (MII) regulates protrusion and adhesion dynamics in migrating cells, NIH3T3 cells were treated with scrambled siRNA (Scr) for 2 days, trea. (cellimagelibrary.org)
- To study the molecular mechanism by which nonmuscle myosin II (MII) regulates protrusion and adhesion dynamics in migrating cells, Swiss3T3 cells were transfected with a plasmid encoding myc-tagged β. (cellimagelibrary.org)
Stress fibers1
- Immunofluorescence staining indicated that myosin IIB was localized preferentially along stress fibers in the interior region of the cell. (umassmed.edu)
Superfamily1
- Specific members of the Myosin superfamily of motor proteins are known to transport cargo along actin filaments. (mechanobio.info)
Preferentially1
- The computer-aided homology modelling revealed that Rg1 preferentially positioned in the actin binding cleft of myosin IIA and might block the binding of myosin IIA to actin filaments. (ijbs.com)
Inhibits1
- Accordingly, the neuroprotective mechanism of Rg1 is related to the activity that inhibits myosin IIA-actin interaction and the caspase-3/ROCK1/MLC signaling pathway. (ijbs.com)
Inhibition1
- LIMCH1 interacted with NM-IIA, but not NM-IIB, independent of the inhibition of myosin ATPase activity with blebbistatin. (nih.gov)
Mechanism1
- Movement of myosin-X is driven by ATP hydrolysis, in a unique mechanism that resembles walking or stepping. (mechanobio.info)
Proteins3
- The long tail region interacts with other proteins, including the tail regions of other myosin proteins. (medlineplus.gov)
- Each fiber type-specific sample is then used to quantify the expression of various target proteins using western blotting techniques. (bvsalud.org)
- 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)
Chains5
- Myosin is a hexamer composed of two myosin heavy chains, two regulatory light chains (RLCs), and two essential light chains (ELCs) ( Figure 1A ). (elifesciences.org)
- The light chains bind to the central neck domain of the myosin heavy chain and have structural and regulatory functions ( Heissler and Sellers, 2014 ). (elifesciences.org)
- The C-terminal tail of the myosin heavy chain associates with the tails of other myosin heavy chains and promotes the assembly into bipolar filaments. (elifesciences.org)
- The top panel shows the myosin hexamer composed of two myosin heavy chains (green), two ELCs (light blue) and two RLCs (gray). (elifesciences.org)
- Here, we report a novel alternatively spliced isoform of nonmuscle myosin IIA (NM IIA), called NM IIA2, which is generated by the inclusion of 21 amino acids near the actin-binding region (loop 2) of the head domain of heavy chains. (bvsalud.org)
Filament1
- Myosin-X step size corresponds to a single twist of the actin filament helix. (mechanobio.info)
Functions2
- Although myosin II is known to play an important role in cell migration, little is known about its specific functions. (umassmed.edu)
- In cells, F-actin assumes specific types of organization depending on its functions. (biologists.com)
Fibers6
- Using MyDoBID, type I and II fibers are classified with MHCI- and IIa-specific antibodies, respectively. (bvsalud.org)
- Classified fibers are then combined into fiber type-specific samples for each biopsy. (bvsalud.org)
- The benefits of consolidating classified fibers into fiber type-specific samples compared to single-fiber western blots, include sample versatility, increased sample throughput, shorter time investment, and cost-saving measures, all while retaining valuable fiber type-specific information that is frequently overlooked using homogenized muscle samples. (bvsalud.org)
- The purpose of the protocol is to achieve accurate and efficient identification of type I and type II fibers isolated from freeze-dried human skeletal muscle samples. (bvsalud.org)
- These individual fibers are subsequently combined to create type I and type II fiber type-specific samples. (bvsalud.org)
- Furthermore, the protocol is extended to include the identification of type IIx fibers, using Actin as a marker for fibers that were negative for MHCI and MHCIIa, which are confirmed as IIx fibers by western blotting. (bvsalud.org)
Regulatory light1
- Depletion of LIMCH1 attenuated myosin regulatory light chain (MRLC) diphosphorylation in HeLa cells, which was restored by reexpression of small interfering RNA-resistant LIMCH1. (nih.gov)
Retraction6
- The Rg1 treatment also abolished H 2 O 2 -induced morphological changes, including cell rounding, membrane blebbing, neurite retraction and nuclei condensation, which were generated by myosin IIA-actin interaction. (ijbs.com)
- I investigated the roles of RhoA-kinase and myosin II in semaphorin-3A-induced growth cone collapse and axon retraction. (biologists.com)
- Myosin II activity is required for axon retraction but not growth cone collapse. (biologists.com)
- 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)
- Myosin II interacts with F-actin to generate contractile forces that result in axon retraction. (biologists.com)
- how can myosin II drive axon retraction if the major source of the required substratum for force generation, growth cone F-actin, has been depleted? (biologists.com)
Genes1
- 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)
Light chain1
- The myosin motor domain, the light chain binding neck and the tail domain of the heavy chain are indicated. (elifesciences.org)
Movement1
- Our results suggest that myosin IIB is involved not in propelling but in directing the cell movement, by coordinating protrusive activities and stabilizing the cell polarity. (umassmed.edu)
Rabbit1
- 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)
Functional1
- Platelets, which only express myosin IIA, are most affected by a lack of functional myosin-9, accounting for the thrombocytopenia seen in all individuals with MYH9 -related disorder. (medlineplus.gov)
Diseases1
- These findings put some insights into the unique neuroprotective properties of Rg1 associated with the regulation of myosin IIA-actin cytoskeletal structure under oxidative stress and provide experimental evidence for Rg1 in CNS diseases. (ijbs.com)
Cell1
- Overall, our data highlights that myosin activity is required for rapid cell contraction and tissue folding in developing Drosophila embryos. (elifesciences.org)
Organization1
- A ) Domain organization of the myosin heavy chain and myosin fragments used to study the biochemical properties of myosin. (elifesciences.org)
Cells1
- While some cells use more than one type of myosin II, certain blood cells such as platelets and white blood cells (leukocytes) use only myosin IIA. (medlineplus.gov)
HUMAN1
- In a resource-constrained world supporting a rapidly growing human population there is great interest in en-hancing the production efficiency of our major animal and plant food industries. (1library.net)
Motor3
- Here, combining the biochemical analysis of enzymatic and motile properties for purified myosin mutants with in vivo measurements of apical constriction for the same mutants, we show that in vivo constriction rate scales with myosin motor activity. (elifesciences.org)
- The defect in the myosin motor activity in these mutants is evident in developing Drosophila embryos where tissue recoil following laser ablation is decreased compared to wild-type tissue. (elifesciences.org)
- The motor domain at the N-terminus of the myosin heavy chain binds actin filaments in an ATP-dependent manner. (elifesciences.org)
Independent1
- Formation of axonal F-actin bundles was independent of myosin II, but partially required RhoA-kinase activity. (biologists.com)
Forms2
- There are three forms of myosin II, called myosin IIA, myosin IIB and myosin IIC. (medlineplus.gov)
- 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)