A subtype of bone morphogenetic protein receptors with low affinity for BONE MORPHOGENETIC PROTEINS. They are constitutively active PROTEIN-SERINE-THREONINE KINASES that can interact with and phosphorylate TYPE I BONE MORPHOGENETIC PROTEIN RECEPTORS.
A subtype of bone morphogenetic protein receptors with high affinity for BONE MORPHOGENETIC PROTEINS. They can interact with and undergo PHOSPHORYLATION by BONE MORPHOGENETIC PROTEIN RECEPTORS, TYPE II. They signal primarily through RECEPTOR-REGULATED SMAD PROTEINS.
Increased VASCULAR RESISTANCE in the PULMONARY CIRCULATION, usually secondary to HEART DISEASES or LUNG DISEASES.
A family of CELL SURFACE RECEPTORS that bind BONE MORPHOGENETIC PROTEINS. They are PROTEIN-SERINE-THREONINE KINASES that mediate SIGNAL TRANSDUCTION PATHWAYS through SMAD PROTEINS.
Bone-growth regulatory factors that are members of the transforming growth factor-beta superfamily of proteins. They are synthesized as large precursor molecules which are cleaved by proteolytic enzymes. The active form can consist of a dimer of two identical proteins or a heterodimer of two related bone morphogenetic proteins.
A potent osteoinductive protein that plays a critical role in the differentiation of osteoprogenitor cells into OSTEOBLASTS.
A receptor-regulated smad protein that undergoes PHOSPHORYLATION by BONE MORPHOGENETIC PROTEIN RECEPTORS. It regulates BONE MORPHOGENETIC PROTEIN signaling and plays an essential role in EMBRYONIC DEVELOPMENT.
A bone morphogenetic protein that is a potent inducer of bone formation. It also functions as a regulator of MESODERM formation during EMBRYONIC DEVELOPMENT.
Cell surface receptors that bind growth or trophic factors with high affinity, triggering intracellular responses which influence the growth, differentiation, or survival of cells.
A family of smad proteins that undergo PHOSPHORYLATION by CELL SURFACE RECEPTORS in response to TRANSFORMING GROWTH FACTOR BETA; ACTIVIN; or BONE MORPHOGENETIC PROTEIN signaling.
A bone morphogenetic protein that is widely expressed during EMBRYONIC DEVELOPMENT. It is both a potent osteogenic factor and a specific regulator of nephrogenesis.
One of the two types of ACTIVIN RECEPTORS or activin receptor-like kinases (ALK'S). There are several type I activin receptors. The major active ones are ALK-2 (ActR-IA) and ALK-4 (ActR-IB).
A family of proteins that are involved in the translocation of signals from TGF-BETA RECEPTORS; BONE MORPHOGENETIC PROTEIN RECEPTORS; and other surface receptors to the CELL NUCLEUS. They were originally identified as a class of proteins that are related to the mothers against decapentaplegic protein, Drosophila and sma proteins from CAENORHABDITIS ELEGANS.
Cell-surface proteins that bind transforming growth factor beta and trigger changes influencing the behavior of cells. Two types of transforming growth factor receptors have been recognized. They differ in affinity for different members of the transforming growth factor beta family and in cellular mechanisms of action.
One of the two types of ACTIVIN RECEPTORS. They are membrane protein kinases belonging to the family of PROTEIN-SERINE-THREONINE KINASES. The major type II activin receptors are ActR-IIA and ActR-IIB.
A factor synthesized in a wide variety of tissues. It acts synergistically with TGF-alpha in inducing phenotypic transformation and can also act as a negative autocrine growth factor. TGF-beta has a potential role in embryonal development, cellular differentiation, hormone secretion, and immune function. TGF-beta is found mostly as homodimer forms of separate gene products TGF-beta1, TGF-beta2 or TGF-beta3. Heterodimers composed of TGF-beta1 and 2 (TGF-beta1.2) or of TGF-beta2 and 3 (TGF-beta2.3) have been isolated. The TGF-beta proteins are synthesized as precursor proteins.
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
A bone morphogenetic protein that is a potent inducer of BONE formation. It plays additional roles in regulating CELL DIFFERENTIATION of non-osteoblastic cell types and epithelial-mesenchymal interactions.
The short wide vessel arising from the conus arteriosus of the right ventricle and conveying unaerated blood to the lungs.
A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.
A pyrrolizidine alkaloid and a toxic plant constituent that poisons livestock and humans through the ingestion of contaminated grains and other foods. The alkaloid causes pulmonary artery hypertension, right ventricular hypertrophy, and pathological changes in the pulmonary vasculature. Significant attenuation of the cardiopulmonary changes are noted after oral magnesium treatment.
An interleukin-1 receptor subtype that is involved in signaling cellular responses to INTERLEUKIN-1ALPHA and INTERLEUKIN-1BETA. The binding of this receptor to its ligand causes its favorable interaction with INTERLEUKIN-1 RECEPTOR ACCESSORY PROTEIN and the formation of an activated receptor complex.
A specialized CONNECTIVE TISSUE that is the main constituent of the SKELETON. The principle cellular component of bone is comprised of OSTEOBLASTS; OSTEOCYTES; and OSTEOCLASTS, while FIBRILLAR COLLAGENS and hydroxyapatite crystals form the BONE MATRIX.
A bone morphogenetic protein that may play a role in CARTILAGE formation. It is a potent regulator of the growth of CHONDROCYTES and the synthesis of cartilage matrix proteins. Evidence for its role in cartilage formation can be seen in MICE, where genetic mutations that cause loss of bone morphogenetic protein 5 function result in the formation of small malformed ears.
Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behavior of the target cell (From Alberts, Molecular Biology of the Cell, 2nd ed, pp693-5). Cell surface receptors, unlike enzymes, do not chemically alter their ligands.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
A bone morphogenetic protein that is found at high concentrations in a purified osteoinductive protein fraction from BONE. Bone morphogenetic protein 3 is referred to as osteogenin, however it may play a role in variety of developmental processes.
Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs.

Transducing the Dpp morphogen gradient in the wing of Drosophila: regulation of Dpp targets by brinker. (1/372)

Dpp, a TGFbeta, organizes pattern in the Drosophila wing by acting as a graded morphogen, activating different targets above distinct threshold concentrations. Like other TGFbetas, Dpp appears to induce transcription directly via activation of a SMAD, Mad. However, here we demonstrate that Dpp can also control gene expression indirectly by downregulating the expression of the brinker gene, which encodes a putative transcription factor that functions to repress Dpp targets. The medial-to-lateral Dpp gradient along the anterior-posterior axis is complemented by a lateral-to-medial gradient of Brinker, and the presence of these two opposing gradients may function to allow cells to detect small differences in Dpp concentration and respond by activating different target genes.  (+info)

The Drosophila gene brinker reveals a novel mechanism of Dpp target gene regulation. (2/372)

decapentaplegic (dpp), a Drosophila member of the TGFbeta family of secreted molecules, functions as a long-range morphogen in patterning of the embryo and the adult appendages. Dpp signals via the SMAD proteins Mad and Medea. Here we show that in the absence of brinker (brk), Mad is not required for the activation of Dpp target genes that depend on low levels of Dpp. brk encodes a novel protein with features of a transcriptional repressor. brk itself is negatively regulated by Dpp. Dpp signaling might relieve brk's repression of low-level target genes either by transcriptional repression of brk or by antagonizing a repressor function of brk at the target gene promoters.  (+info)

Restricted expression of the receptor serine/threonine kinase BMPR-IB in zebrafish. (3/372)

Bone morphogenetic proteins (BMPs) comprise a rapidly expanding subclass of the transforming growth factor-beta superfamily. They are known to regulate a diverse range of developmental phenomena including cell differentiation, morphogenesis and apoptosis. In this study, we have isolated a zebrafish homolog of BMP type IB receptor (BMPR-IB) and examined the localization of the transcripts during embryogenesis. Whole-mount in situ hybridization analysis revealed that unlike other type I and type II receptors that mediate BMP signal, it is expressed in developing somite and in mid-hind brain region in a restricted manner.  (+info)

Bmp signaling regulates proximal-distal differentiation of endoderm in mouse lung development. (4/372)

In the mature mouse lung, the proximal-distal (P-D) axis is delineated by two distinct epithelial subpopulations: the proximal bronchiolar epithelium and the distal respiratory epithelium. Little is known about the signaling molecules that pattern the lung along the P-D axis. One candidate is Bone Morphogenetic Protein 4 (Bmp4), which is expressed in a dynamic pattern in the epithelial cells in the tips of growing lung buds. Previous studies in which Bmp4 was overexpressed in the lung endoderm (Bellusci, S., Henderson, R., Winnier, G., Oikawa, T. and Hogan, B. L. M. (1996) Development 122, 1693-1702) suggested that this factor plays an important role in lung morphogenesis. To further investigate this question, two complementary approaches were utilized to inhibit Bmp signaling in vivo. The Bmp antagonist Xnoggin and, independently, a dominant negative Bmp receptor (dnAlk6), were overexpressed using the surfactant protein C (Sp-C) promoter/enhancer. Inhibiting Bmp signaling results in a severe reduction in distal epithelial cell types and a concurrent increase in proximal cell types, as indicated by morphology and expression of marker genes, including the proximally expressed hepatocyte nuclear factor/forkhead homologue 4 (Hfh4) and Clara cell marker CC10, and the distal marker Sp-C. In addition, electron microscopy demonstrates the presence of ciliated cells, a proximal cell type, in the most peripheral regions of the transgenic lungs. We propose a model in which Bmp4 is a component of an apical signaling center controlling P-D patterning. Endodermal cells at the periphery of the lung, which are exposed to high levels of Bmp4, maintain or adopt a distal character, while cells receiving little or no Bmp4 signal initiate a proximal differentiation program.  (+info)

Characterization of bone morphogenetic protein-6 signaling pathways in osteoblast differentiation. (5/372)

Bone morphogenetic protein (BMP)-6 is a member of the transforming growth factor (TGF)-(&bgr;) superfamily, and is most similar to BMP-5, osteogenic protein (OP)-1/BMP-7, and OP-2/BMP-8. In the present study, we characterized the endogenous BMP-6 signaling pathway during osteoblast differentiation. BMP-6 strongly induced alkaline phosphatase (ALP) activity in cells of osteoblast lineage, including C2C12 cells, MC3T3-E1 cells, and ROB-C26 cells. The profile of binding of BMP-6 to type I and type II receptors was similar to that of OP-1/BMP-7 in C2C12 cells and MC3T3-E1 cells; BMP-6 strongly bound to activin receptor-like kinase (ALK)-2 (also termed ActR-I), together with type II receptors, i.e. BMP type II receptor (BMPR-II) and activin type II receptor (ActR-II). In addition, BMP-6 weakly bound to BMPR-IA (ALK-3), to which BMP-2 also bound. In contrast, binding of BMP-6 to BMPR-IB (ALK-6), and less efficiently to ALK-2 and BMPR-IA, together with BMPR-II was detected in ROB-C26 cells. Intracellular signalling was further studied using C2C12 and MC3T3-E1 cells. Among the receptor-regulated Smads activated by BMP receptors, BMP-6 strongly induced phosphorylation and nuclear accumulation of Smad5, and less efficiently those of Smad1. However, Smad8 was constitutively phosphorylated, and no further phosphorylation or nuclear accumulation of Smad8 by BMP-6 was observed. These findings indicate that in the process of differentiation to osteoblasts, BMP-6 binds to ALK-2 as well as other type I receptors, and transduces signals mainly through Smad5 and possibly through Smad1.  (+info)

Roles of bone morphogenetic protein type I receptors and Smad proteins in osteoblast and chondroblast differentiation. (6/372)

The biological effects of type I serine/threonine kinase receptors and Smad proteins were examined using an adenovirus-based vector system. Constitutively active forms of bone morphogenetic protein (BMP) type I receptors (BMPR-IA and BMPR-IB; BMPR-I group) and those of activin receptor-like kinase (ALK)-1 and ALK-2 (ALK-1 group) induced alkaline phosphatase activity in C2C12 cells. Receptor-regulated Smads (R-Smads) that act in the BMP pathways, such as Smad1 and Smad5, also induced the alkaline phosphatase activity in C2C12 cells. BMP-6 dramatically enhanced alkaline phosphatase activity induced by Smad1 or Smad5, probably because of the nuclear translocation of R-Smads triggered by the ligand. Inhibitory Smads, i.e., Smad6 and Smad7, repressed the alkaline phosphatase activity induced by BMP-6 or the type I receptors. Chondrogenic differentiation of ATDC5 cells was induced by the receptors of the BMPR-I group but not by those of the ALK-1 group. However, kinase-inactive forms of the receptors of the ALK-1 and BMPR-I groups blocked chondrogenic differentiation. Although R-Smads failed to induce cartilage nodule formation, inhibitory Smads blocked it. Osteoblast differentiation induced by BMPs is thus mediated mainly via the Smad-signaling pathway, whereas chondrogenic differentiation may be transmitted by Smad-dependent and independent pathways.  (+info)

Combinatorial signaling through BMP receptor IB and GDF5: shaping of the distal mouse limb and the genetics of distal limb diversity. (7/372)

In this study, we use a mouse insertional mutant to delineate gene activities that shape the distal limb skeleton. A recessive mutation that results in brachydactyly was found in a lineage of transgenic mice. Sequences flanking the transgene insertion site were cloned, mapped to chromosome 3, and used to identify the brachydactyly gene as the type IB bone morphogenetic protein receptor, BmprIB (ALK6). Expression analyses in wild-type mice revealed two major classes of BmprIB transcripts. Rather than representing unique coding RNAs generated by alternative splicing of a single pro-mRNA transcribed from one promoter, the distinct isoforms reflect evolution of two BmprIB promoters: one located distally, driving expression in the developing limb skeleton, and one situated proximally, initiating transcription in neural epithelium. The distal promoter is deleted in the insertional mutant, resulting in a regulatory allele (BmprIB(Tg)) lacking cis-sequences necessary for limb BmprIB expression. Mutants fail to generate digit cartilage, indicating that BMPRIB is the physiologic transducer for the formation of digit cartilage from the skeletal blastema. Expansion of BmprIB expression into the limb through acquisition of these distal cis-regulatory sequences appears, therefore, to be an important genetic component driving morphological diversity in distal extremities. GDF5 is a BMP-related signal, which is also required for proper digit formation. Analyses incorporating both Gdf5 and BmprIB(Tg) alleles revealed that BMPRIB regulates chondrogenesis and segmentation through both GDF5-dependent and -independent processes, and that, reciprocally, GDF5 acts through both IB and other type I receptors. Together, these findings provide in vivo support for the concept of combinatorial BMP signaling, in which distinct outcomes result both from a single receptor being triggered by different ligands and from a single ligand binding to different receptors.  (+info)

The type I BMP receptor BMPRIB is required for chondrogenesis in the mouse limb. (8/372)

Mice carrying a targeted disruption of BmprIB were generated by homologous recombination in embryonic stem cells. BmprIB(-/-) mice are viable and, in spite of the widespread expression of BMPRIB throughout the developing skeleton, exhibit defects that are largely restricted to the appendicular skeleton. Using molecular markers, we show that the initial formation of the digital rays occurs normally in null mutants, but proliferation of prechondrogenic cells and chondrocyte differentiation in the phalangeal region are markedly reduced. Our results suggest that BMPRIB-mediated signaling is required for cell proliferation after commitment to the chondrogenic lineage. Analyses of BmprIB and Gdf5 single mutants, as well as BmprIB; Gdf5 double mutants suggests that GDF5 is a ligand for BMPRIB in vivo. BmprIB; Bmp7 double mutants were constructed in order to examine whether BMPRIB has overlapping functions with other type I BMP receptors. BmprIB; Bmp7 double mutants exhibit severe appendicular skeletal defects, suggesting that BMPRIB and BMP7 act in distinct, but overlapping pathways. These results also demonstrate that in the absence of BMPRIB, BMP7 plays an essential role in appendicular skeletal development. Therefore, rather than having a unique role, BMPRIB has broadly overlapping functions with other BMP receptors during skeletal development.  (+info)

Bone morphogenetic protein receptors, type II (BMPR2) are a type of cell surface receptor that bind to bone morphogenetic proteins (BMPs), which are growth factors involved in the regulation of various cellular processes such as cell proliferation, differentiation, and apoptosis. BMPR2 is a serine/threonine kinase receptor and forms a complex with type I BMP receptors upon BMP binding. This complex activation leads to the phosphorylation and activation of downstream signaling molecules, including SMAD proteins, which ultimately regulate gene transcription.

Mutations in the BMPR2 gene have been associated with several genetic disorders, most notably pulmonary arterial hypertension (PAH), a rare but life-threatening condition characterized by increased pressure in the pulmonary arteries that supply blood to the lungs. In addition, BMPR2 mutations have also been linked to Marfan syndrome, a genetic disorder that affects connective tissue and can cause skeletal, cardiovascular, and ocular abnormalities.

Bone morphogenetic protein receptors (BMPRs) are a group of transmembrane serine/threonine kinase receptors that play a crucial role in the signaling pathway of bone morphogenetic proteins (BMPs), which are growth factors involved in various biological processes including cell proliferation, differentiation, and apoptosis.

Type I BMPRs include three subtypes: activin receptor-like kinase 2 (ALK2), ALK3 (also known as BMPR-IA), and ALK6 (also known as BMPR-IB). These receptors form a complex with type II BMPRs upon binding of BMP ligands to their extracellular domains. The activation of the receptor complex leads to the phosphorylation of intracellular signaling molecules, such as SMAD proteins, which then translocate to the nucleus and regulate gene expression.

Mutations in type I BMPRs have been associated with several genetic disorders, including hereditary hemorrhagic telangiectasia (HHT), a vascular dysplasia disorder characterized by the formation of abnormal blood vessels. Additionally, alterations in BMP signaling pathways have been implicated in various human diseases, such as cancer, fibrosis, and bone disorders.

Pulmonary hypertension is a medical condition characterized by increased blood pressure in the pulmonary arteries, which are the blood vessels that carry blood from the right side of the heart to the lungs. This results in higher than normal pressures in the pulmonary circulation and can lead to various symptoms and complications.

Pulmonary hypertension is typically defined as a mean pulmonary artery pressure (mPAP) greater than or equal to 25 mmHg at rest, as measured by right heart catheterization. The World Health Organization (WHO) classifies pulmonary hypertension into five groups based on the underlying cause:

1. Pulmonary arterial hypertension (PAH): This group includes idiopathic PAH, heritable PAH, drug-induced PAH, and associated PAH due to conditions such as connective tissue diseases, HIV infection, portal hypertension, congenital heart disease, and schistosomiasis.
2. Pulmonary hypertension due to left heart disease: This group includes conditions that cause elevated left atrial pressure, such as left ventricular systolic or diastolic dysfunction, valvular heart disease, and congenital cardiovascular shunts.
3. Pulmonary hypertension due to lung diseases and/or hypoxia: This group includes chronic obstructive pulmonary disease (COPD), interstitial lung disease, sleep-disordered breathing, alveolar hypoventilation disorders, and high altitude exposure.
4. Chronic thromboembolic pulmonary hypertension (CTEPH): This group includes persistent obstruction of the pulmonary arteries due to organized thrombi or emboli.
5. Pulmonary hypertension with unclear and/or multifactorial mechanisms: This group includes hematologic disorders, systemic disorders, metabolic disorders, and other conditions that can cause pulmonary hypertension but do not fit into the previous groups.

Symptoms of pulmonary hypertension may include shortness of breath, fatigue, chest pain, lightheadedness, and syncope (fainting). Diagnosis typically involves a combination of medical history, physical examination, imaging studies, and invasive testing such as right heart catheterization. Treatment depends on the underlying cause but may include medications, oxygen therapy, pulmonary rehabilitation, and, in some cases, surgical intervention.

Bone morphogenetic protein (BMP) receptors are a type of cell surface receptor that play a crucial role in bone and cartilage development, as well as in other biological processes such as wound healing and embryonic development. These receptors are part of the TGF-β (transforming growth factor-beta) superfamily and are composed of two types of subunits: type I and type II.

Type I BMP receptors include BMPR1A, BMPR1B, and ACTRIIA/B. Type II BMP receptors include BMPR2, ACVR2A, and ACVR2B. When BMPs bind to these receptors, they initiate a signaling cascade that leads to the activation of downstream targets involved in bone formation, cartilage development, and other processes.

Mutations in BMP receptor genes have been associated with various genetic disorders, including fibrodysplasia ossificans progressiva (FOP), a rare condition characterized by the abnormal formation of bone in muscles, tendons, and ligaments. Additionally, dysregulation of BMP signaling has been implicated in diseases such as cancer, where it can contribute to tumor growth and metastasis.

Bone Morphogenetic Proteins (BMPs) are a group of growth factors that play crucial roles in the development, growth, and repair of bones and other tissues. They belong to the Transforming Growth Factor-β (TGF-β) superfamily and were first discovered when researchers found that certain proteins extracted from demineralized bone matrix had the ability to induce new bone formation.

BMPs stimulate the differentiation of mesenchymal stem cells into osteoblasts, which are the cells responsible for bone formation. They also promote the recruitment and proliferation of these cells, enhancing the overall process of bone regeneration. In addition to their role in bone biology, BMPs have been implicated in various other biological processes, including embryonic development, wound healing, and the regulation of fat metabolism.

There are several types of BMPs (BMP-2, BMP-4, BMP-7, etc.) that exhibit distinct functions and expression patterns. Due to their ability to stimulate bone formation, recombinant human BMPs have been used in clinical applications, such as spinal fusion surgery and non-healing fracture treatment. However, the use of BMPs in medicine has been associated with certain risks and complications, including uncontrolled bone growth, inflammation, and cancer development, which necessitates further research to optimize their therapeutic potential.

Bone Morphogenetic Protein 2 (BMP-2) is a growth factor that belongs to the transforming growth factor-beta (TGF-β) superfamily. It plays a crucial role in bone and cartilage formation, as well as in the regulation of wound healing and embryonic development. BMP-2 stimulates the differentiation of mesenchymal stem cells into osteoblasts, which are cells responsible for bone formation.

BMP-2 has been approved by the US Food and Drug Administration (FDA) as a medical device to promote bone growth in certain spinal fusion surgeries and in the treatment of open fractures that have not healed properly. It is usually administered in the form of a collagen sponge soaked with recombinant human BMP-2 protein, which is a laboratory-produced version of the natural protein.

While BMP-2 has shown promising results in some clinical applications, its use is not without risks and controversies. Some studies have reported adverse effects such as inflammation, ectopic bone formation, and increased rates of cancer, which have raised concerns about its safety and efficacy. Therefore, it is essential to weigh the benefits and risks of BMP-2 therapy on a case-by-case basis and under the guidance of a qualified healthcare professional.

Smad1 is a protein that belongs to the Smad family, which are intracellular signaling proteins that play a critical role in the transforming growth factor-beta (TGF-β) signaling pathway. Smad1 is primarily involved in the bone morphogenetic protein (BMP) branch of the TGF-β superfamily.

When BMPs bind to their receptors on the cell surface, they initiate a signaling cascade that leads to the phosphorylation and activation of Smad1. Once activated, Smad1 forms a complex with other Smad proteins, known as a Smad complex, which then translocates into the nucleus. In the nucleus, the Smad complex interacts with various DNA-binding proteins and transcription factors to regulate gene expression.

Smad1 plays crucial roles in several biological processes, including embryonic development, cell differentiation, and tissue homeostasis. Dysregulation of Smad1 signaling has been implicated in a variety of human diseases, such as cancer, fibrosis, and skeletal disorders.

Bone Morphogenetic Protein 4 (BMP-4) is a growth factor that belongs to the transforming growth factor-beta (TGF-β) superfamily. It plays crucial roles in various biological processes, including embryonic development, cell growth, and differentiation. In the skeletal system, BMP-4 stimulates the formation of bone and cartilage by inducing the differentiation of mesenchymal stem cells into chondrocytes and osteoblasts. It also regulates the maintenance and repair of bones throughout life. An imbalance in BMP-4 signaling has been associated with several skeletal disorders, such as heterotopic ossification and osteoarthritis.

Growth factor receptors are a type of cell surface receptor that bind to specific growth factors, which are signaling molecules that play crucial roles in regulating various cellular processes such as growth, differentiation, and survival. These receptors have an extracellular domain that can recognize and bind to the growth factor and an intracellular domain that can transduce the signal into the cell through a series of biochemical reactions.

There are several types of growth factors, including fibroblast growth factors (FGFs), epidermal growth factors (EGFs), vascular endothelial growth factors (VEGFs), and transforming growth factors (TGFs). Each type of growth factor has its own specific receptor or family of receptors.

Once a growth factor binds to its receptor, it triggers a cascade of intracellular signaling events that ultimately lead to changes in gene expression, protein synthesis, and other cellular responses. These responses can include the activation of enzymes, the regulation of ion channels, and the modulation of cytoskeletal dynamics.

Abnormalities in growth factor receptor signaling have been implicated in various diseases, including cancer, developmental disorders, and autoimmune diseases. For example, mutations in growth factor receptors can lead to uncontrolled cell growth and division, which is a hallmark of cancer. Therefore, understanding the structure and function of growth factor receptors has important implications for the development of new therapies for these diseases.

Receptor-regulated Smad proteins (R-Smads) are a subgroup of the Smad family of intracellular signaling proteins that play a critical role in mediating signals from the transforming growth factor-β (TGF-β) superfamily of cytokines and hormones. In humans, there are three types of R-Smads: Smad1, Smad2, Smad3, Smad5, and Smad8/9.

R-Smads are directly phosphorylated by the type I TGF-β receptor kinases upon ligand binding, which leads to their activation and subsequent translocation into the nucleus. Once in the nucleus, R-Smads form complexes with other transcription factors and co-regulators to regulate the expression of target genes involved in various cellular processes such as proliferation, differentiation, apoptosis, migration, and extracellular matrix production.

R-Smad signaling is tightly regulated by several mechanisms, including inhibitory Smads (I-Smads), ubiquitination, and phosphatases, to ensure proper signal transduction and prevent aberrant activation of the pathway. Dysregulation of R-Smad signaling has been implicated in various human diseases, including fibrosis, cancer, and developmental disorders.

Bone Morphogenetic Protein 7 (BMP-7) is a growth factor belonging to the transforming growth factor-beta (TGF-β) superfamily. It plays crucial roles in the development and maintenance of various tissues, including bones, cartilages, and kidneys. In bones, BMP-7 stimulates the differentiation of mesenchymal stem cells into osteoblasts, which are bone-forming cells, thereby promoting bone formation and regeneration. It also has potential therapeutic applications in the treatment of various musculoskeletal disorders, such as fracture healing, spinal fusion, and osteoporosis.

Activin receptors, type I are serine/threonine kinase receptors that play a crucial role in the activin signaling pathway. There are two types of activin receptors, Type I (ALK2, ALK4, and ALK7) and Type II (ActRII and ActRIIB). Activin receptors, type I are transmembrane proteins that bind to activins, which are cytokines belonging to the TGF-β superfamily.

Once activated by binding to activins, activin receptors, type I recruit and phosphorylate type II receptors, leading to the activation of downstream signaling pathways, including SMAD proteins. Activated SMAD proteins then translocate to the nucleus and regulate gene expression, thereby mediating various cellular responses such as proliferation, differentiation, apoptosis, and migration.

Mutations in activin receptors, type I have been implicated in several human diseases, including cancer, fibrosis, and developmental disorders. Therefore, understanding the structure and function of activin receptors, type I is essential for developing novel therapeutic strategies to treat these diseases.

Smad proteins are a family of intracellular signaling molecules that play a crucial role in the transmission of signals from the cell surface to the nucleus in response to transforming growth factor β (TGF-β) superfamily ligands. These ligands include TGF-βs, bone morphogenetic proteins (BMPs), activins, and inhibins.

There are eight mammalian Smad proteins, which are categorized into three classes based on their function: receptor-regulated Smads (R-Smads), common mediator Smads (Co-Smads), and inhibitory Smads (I-Smads). R-Smads include Smad1, Smad2, Smad3, Smad5, and Smad8/9, while Smad4 is the only Co-Smad. The I-Smads consist of Smad6 and Smad7.

Upon TGF-β superfamily ligand binding to their transmembrane serine/threonine kinase receptors, R-Smads are phosphorylated and form complexes with Co-Smad4. These complexes then translocate into the nucleus, where they regulate the transcription of target genes involved in various cellular processes, such as proliferation, differentiation, apoptosis, migration, and extracellular matrix production. I-Smads act as negative regulators of TGF-β signaling by competing with R-Smads for receptor binding or promoting the degradation of receptors and R-Smads.

Dysregulation of Smad protein function has been implicated in various human diseases, including fibrosis, cancer, and developmental disorders.

Transforming Growth Factor beta (TGF-β) receptors are a group of cell surface receptors that bind to TGF-β ligands and transduce signals into the cell. These receptors play crucial roles in regulating various cellular processes, including cell growth, differentiation, apoptosis, and extracellular matrix production.

There are two types of TGF-β receptors: type I and type II. Type I receptors, also known as activin receptor-like kinases (ALKs), have serine/threonine kinase activity and include ALK1, ALK2, ALK3, ALK4, ALK5, and ALK6. Type II receptors are constitutively active serine/threonine kinases and include TGF-β RII, ActRII, and ActRIIB.

When a TGF-β ligand binds to a type II receptor, it recruits and phosphorylates a type I receptor, which in turn phosphorylates downstream signaling molecules called Smads. Phosphorylated Smads form complexes with co-Smad proteins and translocate to the nucleus, where they regulate gene expression.

Abnormalities in TGF-β signaling have been implicated in various human diseases, including fibrosis, cancer, and autoimmune disorders. Therefore, understanding the mechanisms of TGF-β receptor function is essential for developing therapeutic strategies to target these conditions.

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.

Transforming Growth Factor-beta (TGF-β) is a type of cytokine, which is a cell signaling protein involved in the regulation of various cellular processes, including cell growth, differentiation, and apoptosis (programmed cell death). TGF-β plays a critical role in embryonic development, tissue homeostasis, and wound healing. It also has been implicated in several pathological conditions such as fibrosis, cancer, and autoimmune diseases.

TGF-β exists in multiple isoforms (TGF-β1, TGF-β2, and TGF-β3) that are produced by many different cell types, including immune cells, epithelial cells, and fibroblasts. The protein is synthesized as a precursor molecule, which is cleaved to release the active TGF-β peptide. Once activated, TGF-β binds to its receptors on the cell surface, leading to the activation of intracellular signaling pathways that regulate gene expression and cell behavior.

In summary, Transforming Growth Factor-beta (TGF-β) is a multifunctional cytokine involved in various cellular processes, including cell growth, differentiation, apoptosis, embryonic development, tissue homeostasis, and wound healing. It has been implicated in several pathological conditions such as fibrosis, cancer, and autoimmune diseases.

Signal transduction is the process by which a cell converts an extracellular signal, such as a hormone or neurotransmitter, into an intracellular response. This involves a series of molecular events that transmit the signal from the cell surface to the interior of the cell, ultimately resulting in changes in gene expression, protein activity, or metabolism.

The process typically begins with the binding of the extracellular signal to a receptor located on the cell membrane. This binding event activates the receptor, which then triggers a cascade of intracellular signaling molecules, such as second messengers, protein kinases, and ion channels. These molecules amplify and propagate the signal, ultimately leading to the activation or inhibition of specific cellular responses.

Signal transduction pathways are highly regulated and can be modulated by various factors, including other signaling molecules, post-translational modifications, and feedback mechanisms. Dysregulation of these pathways has been implicated in a variety of diseases, including cancer, diabetes, and neurological disorders.

Bone Morphogenetic Protein 6 (BMP-6) is a member of the transforming growth factor-beta (TGF-β) superfamily of proteins. It plays crucial roles in bone and cartilage formation, as well as in the regulation of iron metabolism. BMP-6 stimulates the differentiation of mesenchymal stem cells into osteoblasts, which are bone-forming cells, and contributes to the maintenance of bone homeostasis. Additionally, BMP-6 is involved in the process of hepcidin regulation, a hormone that controls iron absorption and recycling in the body. Dysregulation of BMP-6 has been implicated in various diseases, including skeletal disorders and iron metabolism-related conditions.

The pulmonary artery is a large blood vessel that carries deoxygenated blood from the right ventricle of the heart to the lungs for oxygenation. It divides into two main branches, the right and left pulmonary arteries, which further divide into smaller vessels called arterioles, and then into a vast network of capillaries in the lungs where gas exchange occurs. The thin walls of these capillaries allow oxygen to diffuse into the blood and carbon dioxide to diffuse out, making the blood oxygen-rich before it is pumped back to the left side of the heart through the pulmonary veins. This process is crucial for maintaining proper oxygenation of the body's tissues and organs.

Protein-Serine-Threonine Kinases (PSTKs) are a type of protein kinase that catalyzes the transfer of a phosphate group from ATP to the hydroxyl side chains of serine or threonine residues on target proteins. This phosphorylation process plays a crucial role in various cellular signaling pathways, including regulation of metabolism, gene expression, cell cycle progression, and apoptosis. PSTKs are involved in many physiological and pathological processes, and their dysregulation has been implicated in several diseases, such as cancer, diabetes, and neurodegenerative disorders.

Monocrotaline is not a medical condition but a toxic compound that is found in certain plants, including the Crotalaria species (also known as "rattlebox" or "crowtoe"). It has been used in research to create laboratory models of pulmonary hypertension. Ingestion or inhalation of monocrotaline can lead to serious health effects, including lung damage and death.

Therefore, there is no medical definition for 'Monocrotaline' as it is not a disease or condition.

Interleukin-1 Type I receptors (IL-1R1) are cell surface receptors that bind to and mediate the effects of interleukin-1 (IL-1), which is a cytokine involved in the inflammatory response. IL-1R1 is a transmembrane protein with an extracellular domain that binds to IL-1, and an intracellular domain that activates signaling pathways leading to the expression of genes involved in immune and inflammatory responses.

IL-1R1 is widely expressed on various cell types including hematopoietic cells (e.g., monocytes, macrophages, dendritic cells) and non-hematopoietic cells (e.g., endothelial cells, fibroblasts, epithelial cells). The binding of IL-1 to IL-1R1 triggers the recruitment of the accessory protein, IL-1 receptor accessory protein (IL-1RAcP), which is necessary for signal transduction.

The activation of IL-1R1 leads to the activation of several signaling pathways including NF-κB, MAPKs, and PI3K/Akt, resulting in the production of proinflammatory cytokines, chemokines, adhesion molecules, and other mediators involved in inflammation. Dysregulation of IL-1 signaling has been implicated in various pathological conditions such as autoimmune diseases, chronic inflammation, and cancer.

"Bone" is the hard, dense connective tissue that makes up the skeleton of vertebrate animals. It provides support and protection for the body's internal organs, and serves as a attachment site for muscles, tendons, and ligaments. Bone is composed of cells called osteoblasts and osteoclasts, which are responsible for bone formation and resorption, respectively, and an extracellular matrix made up of collagen fibers and mineral crystals.

Bones can be classified into two main types: compact bone and spongy bone. Compact bone is dense and hard, and makes up the outer layer of all bones and the shafts of long bones. Spongy bone is less dense and contains large spaces, and makes up the ends of long bones and the interior of flat and irregular bones.

The human body has 206 bones in total. They can be further classified into five categories based on their shape: long bones, short bones, flat bones, irregular bones, and sesamoid bones.

Bone Morphogenetic Protein 5 (BMP-5) is a growth factor belonging to the Transforming Growth Factor-β (TGF-β) superfamily. It plays crucial roles in bone and cartilage formation during embryonic development, as well as in fracture healing and tissue repair in adults. BMP-5 stimulates the differentiation of mesenchymal stem cells into chondrocytes and osteoblasts, which are essential for the production of cartilage and bone tissues, respectively. Additionally, BMP-5 has been implicated in regulating cell proliferation, apoptosis, and migration during various developmental and repair processes.

Cell surface receptors, also known as membrane receptors, are proteins located on the cell membrane that bind to specific molecules outside the cell, known as ligands. These receptors play a crucial role in signal transduction, which is the process of converting an extracellular signal into an intracellular response.

Cell surface receptors can be classified into several categories based on their structure and mechanism of action, including:

1. Ion channel receptors: These receptors contain a pore that opens to allow ions to flow across the cell membrane when they bind to their ligands. This ion flux can directly activate or inhibit various cellular processes.
2. G protein-coupled receptors (GPCRs): These receptors consist of seven transmembrane domains and are associated with heterotrimeric G proteins that modulate intracellular signaling pathways upon ligand binding.
3. Enzyme-linked receptors: These receptors possess an intrinsic enzymatic activity or are linked to an enzyme, which becomes activated when the receptor binds to its ligand. This activation can lead to the initiation of various signaling cascades within the cell.
4. Receptor tyrosine kinases (RTKs): These receptors contain intracellular tyrosine kinase domains that become activated upon ligand binding, leading to the phosphorylation and activation of downstream signaling molecules.
5. Integrins: These receptors are transmembrane proteins that mediate cell-cell or cell-matrix interactions by binding to extracellular matrix proteins or counter-receptors on adjacent cells. They play essential roles in cell adhesion, migration, and survival.

Cell surface receptors are involved in various physiological processes, including neurotransmission, hormone signaling, immune response, and cell growth and differentiation. Dysregulation of these receptors can contribute to the development of numerous diseases, such as cancer, diabetes, and neurological disorders.

"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.

Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.

It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.

Bone Morphogenetic Protein 3 (BMP-3) is a member of the transforming growth factor-beta (TGF-β) superfamily of proteins. It plays crucial roles in regulating bone and cartilage development, as well as homeostasis. BMP-3 inhibits the differentiation and mineralization of osteoblasts (cells responsible for bone formation), while promoting the differentiation of chondrocytes (cells responsible for cartilage formation). Additionally, BMP-3 has been implicated in wound healing, tissue regeneration, and cancer progression. Genetic variations in the BMP-3 gene have been associated with several skeletal disorders, including osteoporosis and scoliosis.

Cell differentiation is the process by which a less specialized cell, or stem cell, becomes a more specialized cell type with specific functions and structures. This process involves changes in gene expression, which are regulated by various intracellular signaling pathways and transcription factors. Differentiation results in the development of distinct cell types that make up tissues and organs in multicellular organisms. It is a crucial aspect of embryonic development, tissue repair, and maintenance of homeostasis in the body.

The three types of type I BMP receptors are ACVR1, BMPR1A and BMPR1B. Bone+Morphogenetic+Protein+Receptors,+Type+I at the U.S. ... Bone morphogenetic protein type I receptors are single pass, type I transmembrane proteins. They belong to a class of receptor ... Receptors, Transmembrane receptors, S/T domain, GS domain, Bone morphogenetic protein, EC 2.7.11, All stub articles, ... serine/threonine kinases that bind members of the TGF beta superfamily of ligands-the bone morphogenetic proteins. ...
... , type 1: ACVR1 BMPR1A BMPR1B Bone morphogenetic protein receptor, type 2 Both type 1 and 2 ... Bone morphogenetic protein Miyazono K, Kamiya Y, Morikawa M (January 2010). "Bone morphogenetic protein receptors and signal ... Bone morphogenetic protein receptors are serine-threonine kinase receptors. Transforming growth factor beta family proteins ... "High resolution structures of the bone morphogenetic protein type II receptor in two crystal forms: implications for ligand ...
Bone morphogenetic protein receptor type-1B also known as CDw293 (cluster of differentiation w293) is a protein that in humans ... kinase receptors: type I receptors of about 50-55 kD and type II receptors of about 70-80 kD. Type II receptors bind ligands in ... "Bone morphogenetic protein type IA receptor signaling regulates postnatal osteoblast function and bone remodeling". J. Biol. ... Bone morphogenetic protein, Clusters of differentiation, GS domain, Receptors, Transmembrane receptors, S/T domain, EC 2.7.11) ...
... such as the activin type 2 receptor; and bone morphogenetic protein receptor, type IA. Other LU domain proteins are small ... Three-finger proteins or three-finger protein domains (3FP or TFPD) are a protein superfamily consisting of small, roughly 60- ... Protein articles without symbol, Protein folds, Protein families). ... Ploug M, Ellis V (August 1994). "Structure-function relationships in the receptor for urokinase-type plasminogen activator. ...
... such as the activin type 2 receptor; and bone morphogenetic protein receptor, type IA. Other LU domain proteins are small ... Besides uPAR, other receptors with LU domains include members of the transforming growth factor beta receptor (TGF-beta) ... Tsetlin VI (February 2015). "Three-finger snake neurotoxins and Ly6 proteins targeting nicotinic acetylcholine receptors: ... The LU domain (Ly-6 antigen/uPAR) is an evolutionarily conserved protein domain of the three-finger protein superfamily. This ...
"Enhanced expression of type I receptors for bone morphogenetic proteins during bone formation". J. Bone Miner. Res. 10 (11): ... The bone morphogenetic protein receptor, type IA also known as BMPR1A is a protein which in humans is encoded by the BMPR1A ... kinase receptors: type I receptors of about 50-55 kD and type II receptors of about 70-80 kD. Type II receptors bind ligands in ... "Bone morphogenetic protein type IA receptor signaling regulates postnatal osteoblast function and bone remodeling". J. Biol. ...
It is a bone morphogenetic protein receptor, type 1. Activins are dimeric growth and differentiation factors which belong to ... and type II receptors are required for binding ligands and for expression of type I receptors. Type I and II receptors form a ... resulting in phosphorylation of type I receptors by type II receptors. This gene encodes activin A type I receptor which ... and two type II (II and IIB) receptors. These receptors are all transmembrane proteins, composed of a ligand-binding ...
... type II receptor for bone morphogenetic protein-4 that forms differential heteromeric complexes with bone morphogenetic protein ... BMP4 bone morphogenetic protein 4". Miyazono K, Kamiya Y, Morikawa M (January 2010). "Bone morphogenetic protein receptors and ... "Cloning and characterization of a human type II receptor for bone morphogenetic proteins". Proc. Natl. Acad. Sci. U.S.A. 92 (17 ... "Synergistic effects of different bone morphogenetic protein type I receptors on alkaline phosphatase induction". J. Cell Sci. ...
1995). "Cloning and characterization of a human type II receptor for bone morphogenetic proteins". Proc. Natl. Acad. Sci. U.S.A ... This gene encodes the substrate of breast tumor kinase, an Src-type non-receptor tyrosine kinase. The encoded protein possesses ... Mitchell PJ, Sara EA, Crompton MR (Oct 2000). "A novel adaptor-like protein which is a substrate for the non-receptor tyrosine ... Signal-transducing adaptor protein 2 is a protein that in humans is encoded by the STAP2 gene. ...
"TrkC binds to the bone morphogenetic protein type II receptor to suppress bone morphogenetic protein signaling". Cancer ... Other example of tyrosine kinase receptors include the insulin receptor, the IGF-1 receptor, the MuSK protein receptor, the ... Each type of Trk receptor tends to bind specific neurotrophins: TrkA is the receptor for NGF, TrkB the receptor for BDNF and NT ... Tropomyosin receptor kinase C (TrkC), also known as NT-3 growth factor receptor, neurotrophic tyrosine kinase receptor type 3, ...
2007). "Repulsive guidance molecule RGMa alters utilization of bone morphogenetic protein (BMP) type II receptors by BMP2 and ... Repulsive guidance molecule A (RGMa) is a bone morphogenetic protein (BMP) co-receptor of the repulsive guidance molecule ... Li J, Ye L, Kynaston HG, Jiang WG (February 2012). "Repulsive guidance molecules, novel bone morphogenetic protein co-receptors ... All three RGM proteins appear capable of binding selected BMPs (bone morphogenetic proteins). RGMs may play inhibitory roles in ...
SMAD1 is a receptor regulated SMAD (R-SMAD) and is activated by bone morphogenetic protein type 1 receptor kinase. GRCm38: ... This protein mediates the signals of the bone morphogenetic proteins (BMPs), which are involved in a range of biological ... this protein can be phosphorylated and activated by the BMP receptor kinase. The phosphorylated form of this protein forms a ... Developmental genes and proteins, MH1 domain, MH2 domain, R-SMAD, Human proteins). ...
SMAD5 is a receptor regulated SMAD (R-SMAD) and is activated by bone morphogenetic protein type 1 receptor kinase. It may play ... Like many other TGFβ family members SMAD5 is involved in cell signalling and modulates signals of bone morphogenetic proteins ( ... Developmental genes and proteins, MH1 domain, MH2 domain, R-SMAD, Transcription factors, Human proteins, All stub articles, ... Mothers against decapentaplegic homolog 5 also known as SMAD5 is a protein that in humans is encoded by the SMAD5 gene. SMAD5, ...
Bone morphogenetic protein receptor type II or BMPR2 is a serine/threonine receptor kinase encoded by the BMPR2 gene. It binds ... This causes the recruitment of a BMP type I receptor, which the type II receptor phosphorylates. The type I receptor ... Bone morphogenetic protein, Developmental genes and proteins, TS domain, S/T kinase, Receptors, EC 2.7.11). ... BMPR2 is expressed on both human and animal granulosa cells, and is a crucial receptor for bone morphogenetic protein 15 (BMP15 ...
When a bone morphogenetic protein binds to a receptor (BMP type 1 receptor kinase) it causes SMAD9 to interact with SMAD anchor ... SMAD9 is a receptor regulated SMAD (R-SMAD) and is activated by bone morphogenetic protein type 1 receptor kinase. There are ... The SMAD proteins are homologs of both the drosophila protein, mothers against decapentaplegic (MAD) and the C. elegans protein ... Developmental genes and proteins, MH1 domain, MH2 domain, R-SMAD, Transcription factors, Human proteins, All stub articles, ...
"Proteins associated with type II bone morphogenetic protein receptor (BMPR-II) and identified by two-dimensional gel ... The glucagon receptor is a 62 kDa protein that is activated by glucagon and is a member of the class B G-protein coupled family ... Brubaker PL, Drucker DJ (2002). "Structure-function of the glucagon receptor family of G protein-coupled receptors: the ... modifying protein-directed G protein signaling specificity for the calcitonin gene-related peptide family of receptors receptor ...
The BMPs bind to the bone morphogenetic protein receptor type II (BMPR2). Some of the proteins of the BMP family are BMP4 and ... There are five kinds of type II receptors and seven types of type I receptors in humans and other mammals. These receptors are ... Binds to Activin A Type 2B receptor Forms receptor complex with Activin A Type 1B receptor or with Activin A Type 1C receptor. ... Specifically, the type I receptor, activated by the type II receptor, phosphorylates R-SMADs that then bind to the co-SMAD, ...
"Proteins associated with type II bone morphogenetic protein receptor (BMPR-II) and identified by two-dimensional gel ... The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has three repeats of RRM ... Wada K, Inoue K, Hagiwara M (August 2002). "Identification of methylated proteins by protein arginine N-methyltransferase 1, ... Wada K, Inoue K, Hagiwara M (August 2002). "Identification of methylated proteins by protein arginine N-methyltransferase 1, ...
"Proteins associated with type II bone morphogenetic protein receptor (BMPR-II) and identified by two-dimensional gel ... U7 snRNA-associated Sm-like protein LSm10 is a protein that in humans is encoded by the LSM10 gene. LSM10 has been shown to ... "A novel zinc finger protein is associated with U7 snRNP and interacts with the stem-loop binding protein in the histone pre- ... "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173-8. Bibcode:2005Natur. ...
"Proteins associated with type II bone morphogenetic protein receptor (BMPR-II) and identified by two-dimensional gel ... "Synergistic activation of the insulin gene by a LIM-homeo domain protein and a basic helix-loop-helix protein: building a ... "Transcriptional synergy between LIM-homeodomain proteins and basic helix-loop-helix proteins: the LIM2 domain determines ... LIM homeobox transcription factor 1, alpha, also known as LMX1A, is a protein which in humans is encoded by the LMX1A gene. ...
"Proteins associated with type II bone morphogenetic protein receptor (BMPR-II) and identified by two-dimensional gel ... Nakayama M, Kikuno R, Ohara O (November 2002). "Protein-protein interactions between large proteins: two-hybrid screening using ... DNA topoisomerase 2-binding protein 1 (TOPBP1) is a scaffold protein that in humans is encoded by the TOPBP1 gene. TOPBP1 was ... TOPBP1 was first identified as a DNA damage protein through its association with BRCA1, which is a protein heavily implicated ...
The enzyme is implicated in the trafficking and signaling of type I bone morphogenetic protein (BMP) receptors in zebra fish ( ... HSAN I is the most common type among the five types of HSAN. As a heterogeneous group of diseases, HSAN I can be divided into ... Hereditary sensory and autonomic neuropathy type I (HSAN I) or hereditary sensory neuropathy type I (HSN I) is a group of ... The gene encodes SPTLC1 protein, which together with SPTLC2 protein, forms serine palmitoyltransferase (SPT) in humans. SPT is ...
2004). "Proteins associated with type II bone morphogenetic protein receptor (BMPR-II) and identified by two-dimensional gel ... Lymphocyte-specific protein 1 is a protein that in humans is encoded by the LSP1 gene. This gene encodes an intracellular F- ... Huang CK, Zhan L, Ai Y, Jongstra J (1997). "LSP1 is the major substrate for mitogen-activated protein kinase-activated protein ... Harrison RE, Sikorski BA, Jongstra J (2005). "Leukocyte-specific protein 1 targets the ERK/MAP kinase scaffold protein KSR and ...
2004). "Proteins associated with type II bone morphogenetic protein receptor (BMPR-II) and identified by two-dimensional gel ... PDZ domain-containing RING finger protein 3 is a protein that in humans is encoded by the PDZRN3 gene. GRCh38: Ensembl release ... The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 6 (3): 197-205. doi: ...
2004). "Proteins associated with type II bone morphogenetic protein receptor (BMPR-II) and identified by two-dimensional gel ... Tubulin beta-4A chain is a protein that in humans is encoded by the TUBB4A gene. Two tubulin beta-4 chain proteins are encoded ... 2005). "The glutamine-rich region of the HIV-1 Tat protein is involved in T-cell apoptosis". Journal of Biological Chemistry. ... coactivator-62 kDa/Ski-interacting protein is a nuclear matrix-associated coactivator that may couple vitamin D receptor- ...
2004). "Proteins associated with type II bone morphogenetic protein receptor (BMPR-II) and identified by two-dimensional gel ... 2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and ... transmembrane proteins: a bioinformatics assessment". Genome Res. 13 (10): 2265-70. doi:10.1101/gr.1293003. PMC 403697. PMID ...
2004). "Proteins associated with type II bone morphogenetic protein receptor (BMPR-II) and identified by two-dimensional gel ... This protein is located in the mitochondrial matrix and catalyzes the cleavage of the leader peptides of precursor proteins ... from mitochondrial protein precursors and releases of N-terminal transit peptides from precursor proteins imported into the ... which necessitates proper translocations of mitochondrial targeting proteins. Many mitochondrial proteins are synthesized in a ...
2004). "Proteins associated with type II bone morphogenetic protein receptor (BMPR-II) and identified by two-dimensional gel ... Nucleolar protein 56 is a protein that in humans is encoded by the NOP56 gene. Nop56p is a yeast nucleolar protein that is part ... The protein encoded by this gene is similar in sequence to Nop56p and is also found in the nucleolus. Multiple transcript ... Gautier T, Berges T, Tollervey D, Hurt E (Dec 1997). "Nucleolar KKE/D repeat proteins Nop56p and Nop58p interact with Nop1p and ...
2004). "Proteins associated with type II bone morphogenetic protein receptor (BMPR-II) and identified by two-dimensional gel ... Fibroblast growth factor receptor substrate 3 is a protein that in humans is encoded by the FRS3 gene. The protein encoded by ... Wang JK, Xu H, Li HC, Goldfarb M (Oct 1996). "Broadly expressed SNT-like proteins link FGF receptor stimulation to activators ... 2006). "Unique role of SNT-2/FRS2beta/FRS3 docking/adaptor protein for negative regulation in EGF receptor tyrosine kinase ...
2004). "Proteins associated with type II bone morphogenetic protein receptor (BMPR-II) and identified by two-dimensional gel ... Studies of the mouse counterpart suggest that this protein may be an actin monomer-binding protein, and its localization to ... Twinfilin-1 is a protein that in humans is encoded by the TWF1 gene. This gene encodes twinfilin, an actin monomer-binding ... "Entrez Gene: TWF1 twinfilin, actin-binding protein, homolog 1 (Drosophila)". "Eye morphology data for Twf1". Wellcome Trust ...
The three types of type I BMP receptors are ACVR1, BMPR1A and BMPR1B. Bone+Morphogenetic+Protein+Receptors,+Type+I at the U.S. ... Bone morphogenetic protein type I receptors are single pass, type I transmembrane proteins. They belong to a class of receptor ... Receptors, Transmembrane receptors, S/T domain, GS domain, Bone morphogenetic protein, EC 2.7.11, All stub articles, ... serine/threonine kinases that bind members of the TGF beta superfamily of ligands-the bone morphogenetic proteins. ...
BMPR1A: bone morphogenetic protein receptor type 1A. *BMPR2: bone morphogenetic protein receptor type 2 ...
Knockdown of Bone Morphogenetic Proteins Type 1a Receptor (BMPR1a) in Breast Cancer Cells Protects Bone from Breast Cancer- ... Knockdown of Bone Morphogenetic Proteins Type 1a Receptor (BMPR1a) in Breast Cancer Cells Protects Bone from Breast Cancer- ... The coolest new products in the research circle are here! CheKine™ microquantitative test kits and recombinant proteins help ...
bone morphogenetic protein receptor type 2; ZFN induced mutant 1, Ang. IMP. RGD. PMID:25593290. RGD:38500244. ... bone morphogenetic protein receptor type 2. IMP. RGD. PMID:25593290. RGD:38500244. NCBI chr 9:61,192,718...61,307,280 Ensembl ... compared to wild type. RGD. PMID:26077568. RGD:13800514. G. Lamp2. lysosomal-associated membrane protein 2. IMP. in hemizygote ... LDL receptor related protein 5;CRISPR/Cas9 induced mutant 1, Vari. IMP. RGD. PMID:32833527. RGD:40902996. ...
PDB Compounds: (D:) Bone morphogenetic protein receptor type IA. SCOPe Domain Sequences for d2qj9d_:. Sequence; same for both ... Family g.7.1.3: Extracellular domain of cell surface receptors [57354] (6 proteins). ... Class g: Small proteins [56992] (100 folds). *. Fold g.7: Snake toxin-like [57301] (1 superfamily). disulfide-rich fold: nearly ... SCOPe: Structural Classification of Proteins - extended. Release 2.08 (updated 2023-01-06, stable release September 2021) ...
... a bone morphogenetic protein (BMP) type I receptor, in all individuals with classic fibrodysplasia ossificans progressiva. [4, ... phenotypes are caused by mutations in the bone morphogenetic protein (BMP) type I receptor ACVR1. Hum Mutat. 2009 Mar. 30(3): ... A recurrent mutation in the BMP type I receptor ACVR1 causes inherited and sporadic fibrodysplasia ossificans progressiva. Nat ... FDA Okays First-Ever New Drug for Rare Bone Disorder * Ipsen Says European Commission Rejects Marketing Authorization for Bone ...
Possible stimuli of the observed high levels of hepcidin in IPAH include dysfunctional bone morphogenetic protein receptor type ... and mutations in the bone morphogenetic protein receptor type II (BMPR2) [4]. ... pulmonary hypertension is associated with reduced pulmonary vascular expression of type II bone morphogenetic protein receptor ... Lack of the bone morphogenetic protein BMP6 induces massive iron overload. Nat Genet 2009; 41: 478-481. ...
Several studies have shown that bone morphogenetic protein receptor type 1B (BMPR1B), also known as FecB, plays a major role in ... Protein-protein interaction (PPI) network analysis of DEGs. Known and predicted protein-protein interaction analyses of the ... The protein-protein interaction (PPI) network of differentially expressed proteins in the comparison ... HF comparison contained 98 protein-protein nodes. CDK12, FAM91A1, PGS1, SERTM1, SPAG5, SYNE1, TMEM14A, WNT4, CAMK2G and other ...
Specifically, within the BMP family, Bone Morphogenetic Protein-2 (BMP-2) was the first BMP to be characterized and has been ... As the clinical application of BMP-2 is largely implicated in bone, we focus primarily on its role in bone. However, we also ... BMP-2 has important roles during embryonic development, as well as bone remodeling and homeostasis in adulthood. Some of its ... These proteins are essential to many developmental processes, including cardiogenesis, neurogenesis, and osteogenesis. ...
Activin Receptors, Type I/metabolism. *Animals. *Bone Morphogenetic Protein Receptors/metabolism*. *Cell Differentiation/ ... We utilized transgenic zebrafish that overexpress dominant-negative forms of Bmp or Fgf receptors following heat-shock ...
Activin-like kinase type 1 receptor (ALK-1). *. Bone morphogenetic protein receptor type 2 (BMPR2) ... The BMPR2 (bone morphogenic receptor type 2) pathway is targeted by sotatercept, a novel drug. BMPR2 is the most common gene ... Similarly, other protein kinase inhibitors have also been linked to drug-induced pulmonary hypertension (3 Etiology references ... The endothelin pathway is targeted by bosentan, ambrisentan, and macitentan, which are oral endothelin-receptor antagonists ( ...
Lai, Y., Xie, C., Zhang, S., Gan, G., Wu, D., & Chen, W. (2016). Bone morphogenetic protein type I receptor inhibition induces ... This study aims to elucidate the regulatory role of bone morphogenetic protein (BMPs) during the morpho- genesis of two ... the bone morphogenetic proteins (BMPs) are known to be crucial in regulating the formation of condensations, differentiation, ... Yu, P. B., Deng, D. Y., Lai, C. S., Hong, C. C., Cuny, G. D., Bouxsein, M. L., & Bloch, K. D. (2008). BMP type I receptor ...
These lesions lead to heterotopic ossification, that is, true bone tissue formation in the axial musculature, the... ... phenotypes are caused by mutations in the bone morphogenetic protein (BMP) type I receptor ACVR1. Hum Mutat. 2009 Mar. 30(3): ... which encodes a type I BMP transmembrane receptor. A recurrent mutation in the BMP type I receptor ACVR1 causes inherited and ... A novel mutation in the activin A type 1 receptor gene was described in one patient. [10] Analysis showed that the patient was ...
Abnormal zinc transport or storage protein expression has been linked to diseases, such as cancer and chronic obstructive ... potential effects by targeting of bone morphogenetic protein receptor type 2 in pulmonary microvessels. Cell Biol Int 45(11): ... Bone morphogenic protein receptor type 2 (BMPR2) goat polyclonal antibody was from Santa Cruz (1:50, immunoblots published ... 2021). In vitro, both ZIP2 and ZIP12 were shown induced at mRNA and protein levels in vascular cells by depletion of zinc (Abdo ...
BMPR2 - bone morphogenetic protein receptor type 2 Uniprot Browser. Entrez ID. EnsEMBL ID. Preferred Name. Uniprot ID. ...
bone morphogenetic protein receptor type 1A Kinase 203 0.522. 0.731. 0.90. 0.200. None 0 0 ... bone morphogenetic protein 2 Signaling 428 0.432. 0.846. 0.99. 0.120. None 1.000. 2 0 2009. 2009. ... Protein Class N. diseases g DSI g DPI g pLI Score gda EL gda EI gda N. PMIDs N. SNPs gda First Ref. Last Ref. ... protein kinase AMP-activated non-catalytic subunit gamma 2 Enzyme modulator 122 0.582. 0.654. 1.00. 0.800. None 1.000. 18 6 ...
Bone morphogenetic protein receptor type II. 2q33-q34. 1007775. ENSG00000064036. 659. 18610. 53250. 18610. ... Bone morphogenetic protein receptor type IA. 10q22.3. 1004867. ENSG00000107779. 657. 4895. 2534. 4895. ... Angiopoietin 1 receptor. 9p21. 1010190. ENSG00000120156. 7010. 1423. 89640. 1423. TGFBR2. TGF-beta receptor type II. 3p22. ... Macrophage-stimulating protein receptor. 3p21.3. 1008355. ENSG00000164078. 4486. 7885. 2942. 7885. NTRK1. High affinity nerve ...
Type I Bone Morphogenetic Protein Receptors 13% * Activin Receptors 12% * Current challenges and opportunities in the care of ... Functional Testing of Bone Morphogenetic Protein (BMP) Pathway Variants Identified on Whole-Exome Sequencing in a Patient with ... Bone Marrow Adiposity in Models of Radiation- and Aging-Related Bone Loss Is Dependent on Cellular Senescence. Chandra, A., ... Bone Aging, Cellular Senescence, and Osteoporosis. Pignolo, R. J., Law, S. F. & Chandra, A., Apr 2021, In: JBMR Plus. 5, 4, ...
Bone Morphogenetic Protein Receptors, Type II (42) * Pulmonary Artery (31) * Pulmonary Arterial Hypertension (27) ...
Type II Bone Morphogenetic Protein Receptors 16% View all 22 research outputs ...
Heterozygous mutations within the bone morphogenetic protein type II receptor (BMPR-II) gene (BMPR2), of the transforming ... Heterozygous mutations within the bone morphogenetic protein type II receptor (BMPR-II) gene (BMPR2), of the transforming ... Heterozygous mutations within the bone morphogenetic protein type II receptor (BMPR-II) gene (BMPR2), of the transforming ... Heterozygous mutations within the bone morphogenetic protein type II receptor (BMPR-II) gene (BMPR2), of the transforming ...
Bone Morphogenetic Protein Receptor Type 1B; Bone Morphogenetic Protein Receptor, Type IB; BMP Type-1B Receptor; EC 2.7.11.30; ... BMPR-1B; Bone Morphogenetic Protein Receptor Type-1B; Serine/Threonine Receptor Kinase; Activin Receptor-Like Kinase 6; CDw293 ... Creative Biolabs is bringing our expertise to biosimilar development programs including recombinant antibody and protein ...
It shows genes and PPIs with information about pathways, protein-protein interactions (PPIs), Gene Ontology (GO) annotations ... a web resource for human protein-protein interactions. ... bone morphogenetic protein receptor, type IB. protein-O-mannose ... Regulation Of Pathway-restricted SMAD Protein Phosphorylation. *Transmembrane Receptor Protein Serine/threonine Kinase ... Protein-Protein Interactions. 63 interactors: AMHR2 APP ARHGEF6 BAMBI BMP15 BMP2 BMP4 BMP6 BMP7 BMPR1A BMPR2 CDK14 CDK4 CHN1 ...
CTD (carboxy-terminal domain, RNA polymerase II, polypeptide A) small phosphatase 2 ...
Mice with a deletion of BMP type II receptor (BMPR2+/-) were used in this study in comparison with wild-type mice. CP was ... "Bone morphogenetic protein signaling protects against cerulein-induced pancreatic fibrosis",. abstract = "Bone morphogenetic ... Bone morphogenetic protein signaling protects against cerulein-induced pancreatic fibrosis. In: PloS one. 2014 ; Vol. 9, No. 2. ... Bone morphogenetic protein signaling protects against cerulein-induced pancreatic fibrosis. PloS one. 2014 Feb 21;9(2):e89114. ...
Gene: BMPR2 (HGNC:1078) HGNC Name: bone morphogenetic protein receptor type 2 Transcripts: NM_001204.7 Disease: pulmonary ... Variant p.Trp13X (W13X) is known to escape NMD and produce a truncated protein (PMID: 20095988). Critical regions for protein ... Exon 13 does not contain regions critical for protein function and encodes ,10% of the protein. ... Protein length changes due to in-frame deletions/insertions in a non-repeat region or stop-loss variants. ...
ALK1 = activin receptor-like kinase type 1; BMPR2 = bone morphogenetic protein receptor type 2; HIV = human immunodeficiency ...
BMPR1A (bone morphogenetic protein receptor type 1A) LOVD v.3.0 Build 23 [ Current LOVD status ]. Register as submitter , Log ... Protein: Description of variant at protein level (following HGVS recommendations).. *p.(Arg345Pro) = change predicted from DNA ... Effect: The variants effect on the proteins function, in the format R/C where R is the value reported by the source and C ... p.0? = probably no protein produced. Allele: On which allele is the variant located? Does not necessarily imply inheritance! ...
... receptor 2 and bone morphogenetic protein (BMP) [32, 33]. Notch signalling regulates their preferable differentiation towards ... Type 2 alveolar cells are stem cells in adult lung. J Clin Invest 2013; 123: 3025-3036. doi:10.1172/JCI68782. ... Evidence indicates that most leucine-rich repeat-containing G-protein coupled receptor 6 (Lgr6)-expressing cells are airway ... Rab proteins, syntenin, programmed cell death 6 interacting protein and phospholipase D2 [13-15]. In contrast, MVs are a few ...
Ma Y, Ma L, Guo Q, Zhang S. Expression of bone morphogenetic protein-2 and its receptors in epithelial ovarian cancer and their ... Increased angiotensin II type-2 receptor density in hyperplasia, DCIS and invasive carcinoma of the breast is paralleled with ... Effects of angiotensin II type 2 receptor overexpression on the growth of hepatocellular carcinoma cells in vitro and in vivo. ... Functional angiotensin II type 2 receptors inhibit growth factor signaling in LNCaP and PC3 prostate cancer cell lines. ...
  • Bone morphogenetic proteins (BMPs) are multi-functional growth factors belonging to the Transforming Growth Factor-Beta (TGF-β) superfamily. (mdpi.com)
  • This study aims to elucidate the regulatory role of bone morphogenetic protein (BMPs) during the morpho- genesis of two cartilage elements in zebrafish: the scleral cartilage in the eye and the caudal fin endoskeleton. (kira6inhibitor.com)
  • [ 5 ] BMPs are members of the transforming growth factor-beta superfamily and play a role in the development of bone and other tissues. (medscape.com)
  • The contributors describe the various TGF-β family ligands, including activins and bone morphogenetic proteins (BMPs), the structures and functions of the type I and type II receptors, and how ligand-receptor binding is regulated. (cshlpress.com)
  • The transforming growth factor-β (TGF-β) superfamily consists of related multifunctional cytokines, which include TGF-βs, activins, and bone morphogenetic proteins (BMPs) and coordinate several biological responses in diverse cell types. (avhandlingar.se)
  • Recently, a lot of studies have been looking for bone regeneration using BMPs without bone grafts. (bvsalud.org)
  • Heterozygous mutations within the bone morphogenetic protein type II receptor (BMPR-II) gene (BMPR2), of the transforming growth factor beta (TGF-beta) cell-signaling superfamily, have been identified in familial and sporadic cases of PPH. (kcl.ac.uk)
  • Heterozygous mutations in the type II receptor for bone morphogenetic protein (BMPR2) underlie the majority of the inherited and familial forms of PAH. (brad.ac.uk)
  • In both hypoxia and monocrotaline-induced PAH rat models, which display reduced levels of bmpr2 transcripts, this study further indicates that the TGFbeta-MAPK axis is activated in lungs following elevation of both expression and phosphorylation of the TAK1 protein. (brad.ac.uk)
  • Recently, the CDD used DEC-Tec to find the first potent and selective inhibitors of the enzyme for bone morphogenetic protein receptor type II (BMPR2). (bcm.edu)
  • The overactivation of proteins like BMPR2 is implicated in skeletal defects and cancer, so finding inhibitors that slow down these activation processes could potentially prevent or treat these conditions. (bcm.edu)
  • The three types of type I BMP receptors are ACVR1, BMPR1A and BMPR1B. (wikipedia.org)
  • Description: A sandwich quantitative ELISA assay kit for detection of Mouse Bone Morphogenetic Protein Receptor 1A (BMPR1A) in samples from tissue homogenates, cell lysates or other biological fluids. (lscwarsaw.com)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Bone Morphogenetic Protein Receptor 1A (BMPR1A) in Tissue homogenates, cell lysates and other biological fluids. (lscwarsaw.com)
  • Using mouse primary PASMCs derived from knock-in mice, we demonstrated that BMPR-II dysfunction promotes the activation of small mothers against decapentaplegia-independent mitogen-activated protein kinase (MAPK) pathways via TGFbeta-associated kinase 1 (TAK1), resulting in a pro-proliferative and anti-apoptotic response. (brad.ac.uk)
  • In ex vivo cell-based assays, TAK1 inhibits BMP-responsive reporter activity and interacts with BMPR-II receptor. (brad.ac.uk)
  • Enhanced Expression Of The Cold-Sensing Receptor-TRPM8 In Scleroderma Endothelial Cells and Skin and Endothelial Dysfunction Following TRPM8 Activation. (utoledo.edu)
  • The genetic cause of fibrodysplasia ossificans progressiva was identified as a recurrent missense mutation in the GS activation domain of activin receptor Ia/activinlike kinase 2 ( ACVR1/ALK2 ), a bone morphogenetic protein (BMP) type I receptor, in all individuals with classic fibrodysplasia ossificans progressiva. (medscape.com)
  • A recurrent mutation in the BMP type I receptor ACVR1 causes inherited and sporadic fibrodysplasia ossificans progressiva. (medscape.com)
  • The genetic cause of fibrodysplasia ossificans progressiva lies within the ACVR1 gene, which encodes a type I BMP transmembrane receptor. (medscape.com)
  • The TGF-β family members exert their effects by binding to receptors on the cell surface, activating intracellular signaling pathways that modulate gene expression programs that control normal cell physiology, immune responses, and a variety of developmental processes. (cshlpress.com)
  • Pilliod J, Desjardins A, Pernègre C, Jamann H, Larochelle C, Fon EA, Leclerc N. Clearance of intracellular tau protein from neuronal cells via VAMP8-induced secretion. (mutagenex.com)
  • The biological activity of TGF-β members is executed by transmembrane serine/threonine kinase receptors and intracellular Smad proteins. (avhandlingar.se)
  • A novel mutation in the activin A type 1 receptor gene was described in one patient. (medscape.com)
  • We discovered that PEDF is normally secreted from glioblastoma expressing EGFRvIII a often taking place mutation in principal glioblastoma that produces a permanently turned on epidermal growth aspect receptor. (sciencepop.org)
  • Thiamet G EGFRvIII a regularly happening mutation in main glioblastoma results in a protein that is unable to bind any known ligand. (sciencepop.org)
  • They belong to a class of receptor serine/threonine kinases that bind members of the TGF beta superfamily of ligands-the bone morphogenetic proteins. (wikipedia.org)
  • Nader N, Dib M, Hodeify R, Courjaret R, Elmi A, Hammad AS, Dey R, Huang XY, Machaca K. Membrane progesterone receptor induces meiosis in Xenopus oocytes through endocytosis into signaling endosomes and interaction with APPL1 and Akt2. (mutagenex.com)
  • The present study it was concluded that the bone morphogenetic protein induces bone neoformation, being an alternative as a substitute to bone grafts and that new carrier discovery is necessary to smooth stability of this carriers in receptor site. (bvsalud.org)
  • Ovarian aging has a genetic basis that conditions the ovarian activity via a plethora of cell-signaling pathways that control the functions of different types of cells in the ovary. (encyclopedia.pub)
  • A CALMODULIN-dependent enzyme that catalyzes the phosphorylation of proteins. (bvsalud.org)
  • Other forms of signalling such as contact-dependent Notch signalling, signalling guided by mechanical and physical cues, and signalling from the extracellular matrix through adhesion receptors also provide important signals to stem cells [ 6 , 7 ]. (ersjournals.com)
  • Mutations of this gene introduce a premature stop codon and result in truncated protein versions. (medscape.com)
  • Similarly transient exposure of GSCs to bone morphogenetic protein 4 (BMP4) a well-known differentiation element IL8RA abolishes the tumor initiating and infiltrating potential [15-17]. (sciencepop.org)
  • Morphogen receptor genes and metamorphogenes: skeleton keys to metamorphosis. (medscape.com)
  • Findings suggest that fibrodysplasia ossificans progressiva maps to band 4q27-31, a region that contains at least 1 gene involved in the bone morphogenic protein (BMP) signaling pathway. (medscape.com)
  • BMP-2 has important roles during embryonic development, as well as bone remodeling and homeostasis in adulthood. (mdpi.com)
  • Roles of the G protein-coupled receptor kinase 2 and Rab5 in α1B-adrenergic receptor function and internalization. (mutagenex.com)
  • The transforming growth factor β (TGF-β) family is a large group of structurally related proteins that drive developmental programs and control cell behavior. (cshlpress.com)
  • A cardiomelic developmental field has also been postulated to relate the genetic heterogeneity of HOS (and other similar syndromes) to a cascade of molecules, including the brachyury, sonic hedgehog, bone morphogenetic protein, retinoic acid receptor, and transforming growth factor beta families. (medscape.com)
  • Epidermal growth factor receptor variant III (EGFRvIII) has been associated with glioma stemness but the immediate molecular mechanism linking both is largely unidentified. (sciencepop.org)
  • By the conclusion of this process, the cartilage has matured and will either persist into adulthood as a permanent cartilage, or will be replaced by bone (a replacement cartilage) and ossify (Hall, 2015). (kira6inhibitor.com)
  • Several types of cartilage, defined by differences in cellular and matrix composition, exist in the zebrafish (Benjamin, 1990). (kira6inhibitor.com)
  • Glycogen Synthase Kinase-3 modulates α1A-adrenergic receptor action and regulation. (mutagenex.com)
  • As heterotopic bone accumulates in fibrodysplasia ossificans progressiva, range of motion is progressively lost, leading to near complete immobility. (medscape.com)
  • Description: A sandwich ELISA kit for detection of Bone Morphogenetic Protein Receptor 1A from Mouse in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (lscwarsaw.com)
  • This sheds light upon the role of the Smad7 protein in this system. (lu.se)
  • It has been proposed that iron deficiency mimics the pulmonary effects of hypoxia through the stabilisation of hypoxia-inducible factor (HIF), which is primarily regulated by specific prolyl hydroxylase-domain enzymes (PHDs) and degradation via the von Hippel-Lindau tumour suppressor protein [ 6 , 7 ]. (ersjournals.com)
  • Delgado-Vergas M, Fort S, Tassew D, Tesfaigzi Y. Bmf Facilitates Protein Degradation and Reduces Beclin1 Ubiquitination to Inhibit Autophagy Independent of mTOR. (mutagenex.com)
  • The Tan Lab is leveraging DEC-Tec to tailor drugs to target cancer, creating novel computational algorithms to accelerate the process of identifying new drugs for therapies and developing drugs that regulate RNA-protein interactions to prevent and effectively treat a variety of diseases. (bcm.edu)
  • Specifically, within the BMP family, Bone Morphogenetic Protein-2 (BMP-2) was the first BMP to be characterized and has been well-studied. (mdpi.com)
  • Following the formation of a chondrogenic condensa- tion, aggregated cells differentiate into chondroblasts, and then into chondrocytes, ultimately secreting specialized collagen type‐II and undergoing hypertrophy. (kira6inhibitor.com)
  • Author Overview Malignant gliomas are being among the most lethal types of cancers due partly towards the stem-cell-like features and intrusive properties of the mind tumor cells. (sciencepop.org)
  • Hematopoietic stem cells (HSCs) are primitive tissue-specific somatic stem cells, responsible for the maintenance and replenishment of the bone marrow (BM) and subsequently the entire blood system. (avhandlingar.se)
  • Hematopoietic stem cells (HSCs) reside in the bone marrow (BM) of adult individuals and are ultimately responsible for the continuous production of blood cells throughout life. (avhandlingar.se)
  • Lumngwena EN, Abrahams B, Shuping L, Cicala C, Arthos J, Woodman Z. Selective transmission of some HIV-1 subtype C variants might depend on Envelope stimulating dendritic cells to secrete IL-10. (mutagenex.com)
  • In 1965, the BMP was isolated by Marshal Urist, who showed that this protein extracted from bone narrow could induce bone neoformation when implanted in sites without bone cells. (bvsalud.org)
  • Possible stimuli of the observed high levels of hepcidin in IPAH include dysfunctional bone morphogenetic protein receptor type II signalling and inflammation. (ersjournals.com)
  • The aim of this paper is to review the literature about bone morphogenetic protein type 2 (BMP-2) and on the effect in the alveolar bone augmentation. (bvsalud.org)