Transmembrane proteins belonging to the tumor necrosis factor superfamily that play an essential role in the normal development of several ectodermally derived organs. Several isoforms of the ectodysplasins exist due to multiple ALTERNATIVE SPLICING of the MRNA for the protein. The isoforms ectodysplasin A1 and ectodysplasin A2 are considered biologically active and each bind distinct ECTODYSPLASIN RECEPTORS. Genetic mutations that result in loss of function of ectodysplasin result in ECTODERMAL DYSPLASIA 1, ANHIDROTIC.
Members of the TNF receptor family that are specific for ECTODYSPLASIN. At least two subtypes of the ectodysplasin receptor exist, each being specific for a ectodysplasin isoform. Signaling through ectodysplasin receptors plays an essential role in the normal ectodermal development. Genetic defects that result in loss of ectodysplasin receptor function results ECTODERMAL DYSPLASIA.
A ectodysplasin receptor subtype that is specific for ECTODYSPLASIN A1. It signals via the specific signaling adaptor EDAR-ASSOCIATED DEATH DOMAIN PROTEIN. Loss of function of the edar receptor is associated with AUTOSOMAL RECESSIVE ANHIDROTIC ECTODERMAL DYSPLASIA and ECTODERMAL DYSPLASIA 3, ANHIDROTIC.
A group of hereditary disorders involving tissues and structures derived from the embryonic ectoderm. They are characterized by the presence of abnormalities at birth and involvement of both the epidermis and skin appendages. They are generally nonprogressive and diffuse. Various forms exist, including anhidrotic and hidrotic dysplasias, FOCAL DERMAL HYPOPLASIA, and aplasia cutis congenita.
A tumor necrosis factor receptor-associated factor that acts as a specific signaling adaptor protein for the EDAR RECEPTOR and plays an important role in ectodermal development. It binds to edar receptor via its C-terminal death domain region and to other specific TNF receptor-associated factors via its N-terminal domain. Loss of function of edar-associated death domain protein is associated with AUTOSOMAL RECESSIVE ANHIDROTIC ECTODERMAL DYSPLASIA.
Sweat-producing structures that are embedded in the DERMIS. Each gland consists of a single tube, a coiled body, and a superficial duct.
A tube-like invagination of the EPIDERMIS from which the hair shaft develops and into which SEBACEOUS GLANDS open. The hair follicle is lined by a cellular inner and outer root sheath of epidermal origin and is invested with a fibrous sheath derived from the dermis. (Stedman, 26th ed) Follicles of very long hairs extend into the subcutaneous layer of tissue under the SKIN.
A filament-like structure consisting of a shaft which projects to the surface of the SKIN from a root which is softer than the shaft and lodges in the cavity of a HAIR FOLLICLE. It is found on most surfaces of the body.
Group of fish under the superorder Acanthopterygii, separate from the PERCIFORMES, which includes swamp eels, mullets, sticklebacks, seahorses, spiny eels, rainbowfishes, and KILLIFISHES. The name is derived from the six taxa which comprise the group. (From http://www.nanfa.org/articles/Elassoma/elassoma.htm, 8/4/2000)
One of a set of bone-like structures in the mouth used for biting and chewing.
A HEPARIN binding fibroblast growth factor that may play a role in LIMB BUDS development.
The process of TOOTH formation. It is divided into several stages including: the dental lamina stage, the bud stage, the cap stage, and the bell stage. Odontogenesis includes the production of tooth enamel (AMELOGENESIS), dentin (DENTINOGENESIS), and dental cementum (CEMENTOGENESIS).
The outer of the three germ layers of an embryo.
Cell surface receptors that bind TUMOR NECROSIS FACTORS and trigger changes which influence the behavior of cells.
The most posterior teeth on either side of the jaw, totaling eight in the deciduous dentition (2 on each side, upper and lower), and usually 12 in the permanent dentition (three on each side, upper and lower). They are grinding teeth, having large crowns and broad chewing surfaces. (Jablonski, Dictionary of Dentistry, 1992, p821)
Activins are produced in the pituitary, gonads, and other tissues. By acting locally, they stimulate pituitary FSH secretion and have diverse effects on cell differentiation and embryonic development. Activins are glycoproteins that are hetero- or homodimers of INHIBIN-BETA SUBUNITS.
A technique for maintenance or growth of animal organs in vitro. It refers to three-dimensional cultures of undisaggregated tissue retaining some or all of the histological features of the tissue in vivo. (Freshney, Culture of Animal Cells, 3d ed, p1)
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
Wnt proteins are a large family of secreted glycoproteins that play essential roles in EMBRYONIC AND FETAL DEVELOPMENT, and tissue maintenance. They bind to FRIZZLED RECEPTORS and act as PARACRINE PROTEIN FACTORS to initiate a variety of SIGNAL TRANSDUCTION PATHWAYS. The canonical Wnt signaling pathway stabilizes the transcriptional coactivator BETA CATENIN.
The external, nonvascular layer of the skin. It is made up, from within outward, of five layers of EPITHELIUM: (1) basal layer (stratum basale epidermidis); (2) spinous layer (stratum spinosum epidermidis); (3) granular layer (stratum granulosum epidermidis); (4) clear layer (stratum lucidum epidermidis); and (5) horny layer (stratum corneum epidermidis).
A technique that localizes specific nucleic acid sequences within intact chromosomes, eukaryotic cells, or bacterial cells through the use of specific nucleic acid-labeled probes.
The development of anatomical structures to create the form of a single- or multi-cell organism. Morphogenesis provides form changes of a part, parts, or the whole organism.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action during the developmental stages of an organism.
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 molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed)

Edar/Eda interactions regulate enamel knot formation in tooth morphogenesis. (1/26)

tabby and downless mutant mice have apparently identical defects in teeth, hair and sweat glands. Recently, genes responsible for these spontaneous mutations have been identified. downless (Dl) encodes Edar, a novel member of the tumour necrosis factor (TNF) receptor family, containing the characteristic extracellular cysteine rich fold, a single transmembrane region and a death homology domain close to the C terminus. tabby (Ta) encodes ectodysplasin-A (Eda) a type II membrane protein of the TNF ligand family containing an internal collagen-like domain. As predicted by the similarity in adult mutant phenotype and the structure of the proteins, we demonstrate that Eda and Edar specifically interact in vitro. We have compared the expression pattern of Dl and Ta in mouse development, taking the tooth as our model system, and find that they are not expressed in adjacent cells as would have been expected. Teeth develop by a well recorded series of epithelial-mesenchymal interactions, similar to those in hair follicle and sweat gland development, the structures found to be defective in tabby and downless mice. We have analysed the downless mutant teeth in detail, and have traced the defect in cusp morphology back to initial defects in the structure of the tooth enamel knot at E13. Significantly, the defect is distinct from that of the tabby mutant. In the tabby mutant, there is a recognisable but small enamel knot, whereas in the downless mutant the knot is absent, but enamel knot cells are organised into a different shape, the enamel rope, showing altered expression of signalling factors (Shh, Fgf4, Bmp4 and Wnt10b). By adding a soluble form of Edar to tooth germs, we were able to mimic the tabby enamel knot phenotype, demonstrating the involvement of endogenous Eda in tooth development. We could not, however, reproduce the downless phenotype, suggesting the existence of yet another ligand or receptor, or of ligand-independent activation mechanisms for Edar. Changes in the structure of the enamel knot signalling centre in downless tooth germs provide functional data directly linking the enamel knot with tooth cusp morphogenesis. We also show that the Lef1 pathway, thought to be involved in these mutants, functions independently in a parallel pathway.  (+info)

Requirement of NF-kappaB/Rel for the development of hair follicles and other epidermal appendices. (2/26)

NF-kappaB/Rel transcription factors and IkappaB kinases (IKK) are essential for inflammation and immune responses, but also for bone-morphogenesis, skin proliferation and differentiation. Determining their other functions has previously been impossible, owing to embryonic lethality of NF-kappaB/Rel or IKK-deficient animals. Using a gene targeting approach we have ubiquitously expressed an NF-kappaB super-repressor to investigate NF-kappaB functions in the adult. Mice with suppressed NF-kappaB revealed defective early morphogenesis of hair follicles, exocrine glands and teeth, identical to Eda (tabby) and Edar (downless) mutant mice. These affected epithelial appendices normally display high NF-kappaB activity, suppression of which resulted in increased apoptosis, indicating that NF-kappaB acts as a survival factor downstream of the tumor necrosis factor receptor family member EDAR. Furthermore, NF-kappaB is required for peripheral lymph node formation and macrophage function.  (+info)

WNT signals are required for the initiation of hair follicle development. (3/26)

Hair follicle morphogenesis is initiated by a dermal signal that induces the development of placodes in the overlying epithelium. To determine whether WNT signals are required for initiation of follicular development, we ectopically expressed Dickkopf 1, a potent diffusible inhibitor of WNT action, in the skin of transgenic mice. This produced a complete failure of placode formation prior to morphological or molecular signs of differentiation, and blocked tooth and mammary gland development before the bud stage. This phenotype indicates that activation of WNT signaling in the skin precedes, and is required for, localized expression of regulatory genes and initiation of hair follicle placode formation.  (+info)

Mucosal addressin cell adhesion molecule 1 plays an unexpected role in the development of mouse guard hair. (4/26)

The first wave of coat hair development is initiated around embryonic day 14 in the mouse. Whereas ectodysplasin and ectodermal dysplasia receptor, tumor necrosis factor and tumor necrosis factor receptor family molecules, respectively, were identified to be signals triggering this process, not much was known regarding their downstream molecular targets. In this report, we show that mucosal addressin cell adhesion molecule 1 and intercellular adhesion molecule 1 are induced in the keratinocytes of the hair placode as a direct consequence of ectodermal dysplasia receptor signal, and tumor-necrosis-factor-receptor-associated factor 6 is involved in this mucosal addressin cell adhesion molecule 1 expression. Experiments using an in vitro culture of skin fragments demonstrated that ectodermal-dysplasia-receptor-induced mucosal addressin cell adhesion molecule 1 expression occurs at the initial phase of follicle development before involvement of Sonic hedgehog signal. Follicle development in this culture was also suppressed to some extent, though not completely, by addition of soluble mucosal addressin cell adhesion molecule 1/IgG-Fc chimeric protein, whereas monoclonal antibody that can inhibit mucosal addressin cell adhesion molecule 1 interaction with integrin alpha4beta7 had no effect on this process. These results demonstrated for the first time that the structural proteins, mucosal addressin cell adhesion molecule 1 and intercellular adhesion molecule 1, are induced by ectodermal dysplasia receptor signal and suggested the potential involvement of mucosal addressin cell adhesion molecule 1 in the morphogenesis of follicular keratinocytes.  (+info)

Role of TRAF3 and -6 in the activation of the NF-kappa B and JNK pathways by X-linked ectodermal dysplasia receptor. (5/26)

X-linked ectodermal dysplasia receptor (XEDAR) is a recently isolated member of the tumor necrosis factor receptor family that has been shown to be highly expressed in ectodermal derivatives during embryonic development and binds to ectodysplasin-A2 (EDA-A2). By using a subclone of 293F cells with stable expression of XEDAR, we report that XEDAR activates the NF-kappaB and JNK pathways in an EDA-A2-dependent fashion. Treatment with EDA-A2 leads to the recruitment of TRAF3 and -6 to the aggregated XEDAR complex, suggesting a central role of these adaptors in the proximal aspect of XEDAR signaling. Whereas TRAF3 and -6, IKK1/IKKalpha, IKK2/IKKbeta, and NEMO/IKKgamma are involved in XEDAR-induced NF-kappaB activation, XEDAR-induced JNK activation seems to be mediated via a pathway dependent on TRAF3, TRAF6, and ASK1. Deletion and point mutagenesis studies delineate two distinct regions in the cytoplasmic domain of XEDAR, which are involved in binding to TRAF3 and -6, respectively, and play a major role in the activation of the NF-kappaB and JNK pathways. Taken together, our results establish a major role of TRAF3 and -6 in XEDAR signaling and in the process of ectodermal differentiation.  (+info)

Ectodysplasin receptor-mediated signaling is essential for embryonic submandibular salivary gland development. (6/26)

Hypohidrotic (anhidrotic) ectodermal dysplasia (HED), the most common of the approximately 150 described ectodermal dysplasias, is a disorder characterized by abnormal hair, teeth, sweat glands, and salivary glands. Mutations in the EDA (ectodysplasin-A) and EDAR (ectodysplasin-A receptor) genes are responsible for X-linked and autosomal HED, respectively. Abnormal phenotypes similar to HED are seen in Tabby (Eda(Ta)) and downless (Edar(dl)) mutant mice. Although recent studies have focused on the role of Eda/Edar signaling during hair and tooth development, very little is known about its role during embryonic submandibular salivary gland (SMG) development. To this end, we analyzed the SMG phenotypes in Tabby (Ta) and downless (dl) mutant mice and determined that Ta SMGs are hypoplastic, whereas dl SMGs are severely dysplastic. The absence of SMG ducts and acini in dl SMGs suggests that Eda/Edar signaling is essential for lumina formation and glandular histodifferentiation. Our localization of Eda and Edar proteins at sites of lumen and acini formation supports this conclusion. Moreover, the presence of SMGs in both Ta and dl mutant mice, as well as the absence of immunodetectable Eda and Edar protein in Initial Bud and Early Pseudoglandular stage SMGs, indicate that Eda/Edar-mediated signaling is important for branching morphogenesis and histodifferentiation, but not for initial gland formation. To initially delineate the morphoregulatory role of Eda/Edar-mediated signaling during embryonic SMG development, we cultured embryonic day 14 SMGs with enhanced or abrogated Eda/Edar signaling. Eda supplementation induced a significant increase in SMG branching, and enhanced activation of NF-kappaB. Abrogating Eda/Edar signaling by adding the soluble form of Edar to bind endogenous ligand in embryonic SMGs results in a significant dose-dependent decrease in branching morphogenesis. Taken together, our results suggest that the Eda/Edar/NF-kappaB pathway exerts its effect on SMG epithelial cell proliferation, lumina formation, and histodifferentiation.  (+info)

CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members. (7/26)

Familial cylindromatosis is an autosomal dominant predisposition to tumours of skin appendages called cylindromas. Familial cylindromatosis is caused by mutations in a gene encoding the CYLD protein of previously unknown function. Here we show that CYLD is a deubiquitinating enzyme that negatively regulates activation of the transcription factor NF-kappaB by specific tumour-necrosis factor receptors (TNFRs). Loss of the deubiquitinating activity of CYLD correlates with tumorigenesis. CYLD inhibits activation of NF-kappaB by the TNFR family members CD40, XEDAR and EDAR in a manner that depends on the deubiquitinating activity of CYLD. Downregulation of CYLD by RNA-mediated interference augments both basal and CD40-mediated activation of NF-kappaB. The inhibition of NF-kappaB activation by CYLD is mediated, at least in part, by the deubiquitination and inactivation of TNFR-associated factor 2 (TRAF2) and, to a lesser extent, TRAF6. These results indicate that CYLD is a negative regulator of the cytokine-mediated activation of NF-kappaB that is required for appropriate cellular homeostasis of skin appendages.  (+info)

Myodegeneration in EDA-A2 transgenic mice is prevented by XEDAR deficiency. (8/26)

EDA-A1 and EDA-A2 are members of the tumor necrosis factor family of ligands. The products of alternative splicing of the ectodysplasin (EDA) gene, EDA-A1 and EDA-A2 differ by an insertion of two amino acids and bind to distinct receptors. The longer isoform, EDA-A1, binds to EDAR and plays an important role in sweat gland, hair, and tooth development; mutations in EDA, EDAR, or the downstream adaptor EDARADD cause hypohidrotic ectodermal dysplasia. EDA-A2 engages the receptor XEDAR, but its role in the whole organism is less clear. We have generated XEDAR-deficient mice by gene targeting and transgenic mice expressing secreted forms of EDA-A1 or EDA-A2 downstream of the skeletal muscle-specific myosin light-chain 2 or skin-specific keratin 5 promoter. Mice lacking XEDAR were indistinguishable from their wild-type littermates, but EDA-A2 transgenic mice exhibited multifocal myodegeneration. This phenotype was not observed in the absence of XEDAR. Skeletal muscle in EDA-A1 transgenic mice was unaffected, but their sebaceous glands were hypertrophied and hyperplastic, consistent with a role for EDA-A1 in the development of these structures. These data indicate that XEDAR-transduced signals are dispensable for development of ectoderm-derived organs but might play a role in skeletal muscle homeostasis.  (+info)

Ectodysplasins are a group of signaling proteins that play crucial roles in the development and differentiation of ectodermal tissues, including the skin, hair, nails, teeth, and sweat glands. They are involved in various signaling pathways and help regulate cell growth, migration, and pattern formation during embryogenesis. Mutations in genes encoding ectodysplasins can lead to genetic disorders characterized by abnormalities in these tissues, such as ectodermal dysplasia syndromes.

Ectodysplasin receptors are a group of proteins that belong to the tumor necrosis factor (TNF) receptor superfamily. They play crucial roles in the development and function of ectodermal tissues, which include the skin, hair, nails, teeth, and sweat glands.

There are two main types of Ectodysplasin receptors: EDAR (Ectodysplasin A Receptor) and XEDAR (X-linked Ectodysplasin A Receptor). These receptors bind to their respective ligands, Ectodysplasin A (EDA) and Ectodysplasin A2 (EDA2), which are also members of the TNF family.

When EDA or EDA2 binds to EDAR or XEDAR, it activates a signaling pathway that involves several downstream molecules, including TRAF6 (TNF Receptor-Associated Factor 6) and NF-κB (Nuclear Factor kappa-light-chain-enhancer of activated B cells). This signaling cascade ultimately leads to the regulation of gene expression and cellular responses that are essential for ectodermal development.

Mutations in the genes encoding EDA, EDAR, or XEDAR have been associated with various genetic disorders, such as ectodermal dysplasias, which are characterized by abnormalities in the development of ectodermal tissues.

The EDA receptor (Ectodysplasin A receptor) is a gene that encodes a transmembrane protein involved in the development and maintenance of various tissues, including the skin and hair follicles. The Edar receptor plays a crucial role in the signaling pathway that regulates the formation and patterning of these structures during embryonic development. Mutations in this gene have been associated with several human genetic disorders, such as ectodermal dysplasia, which is characterized by abnormalities in the hair, teeth, nails, and sweat glands.

Ectodermal dysplasia (ED) is a group of genetic disorders that affect the development and formation of ectodermal tissues, which include the skin, hair, nails, teeth, and sweat glands. The condition is usually present at birth or appears in early infancy.

The symptoms of ED can vary widely depending on the specific type and severity of the disorder. Common features may include:

* Sparse or absent hair
* Thin, wrinkled, or rough skin
* Abnormal or missing teeth
* Nail abnormalities
* Absent or reduced sweat glands, leading to heat intolerance and problems regulating body temperature
* Ear abnormalities, which can result in hearing loss
* Eye abnormalities

ED is caused by mutations in genes that are involved in the development of ectodermal tissues. Most cases of ED are inherited in an autosomal dominant or autosomal recessive pattern, meaning that a child can inherit the disorder even if only one parent (dominant) or both parents (recessive) carry the mutated gene.

There is no cure for ED, but treatment is focused on managing the symptoms and improving quality of life. This may include measures to maintain body temperature, such as cooling vests or frequent cool baths; dental treatments to replace missing teeth; hearing aids for hearing loss; and skin care regimens to prevent dryness and irritation.

Edar-associated death domain protein (EDARADD) is a gene that encodes for a protein involved in the signaling pathway of the ectodysplasin A receptor (EDAR). The EDAR signaling pathway plays crucial roles in the development of various organs, including skin, hair, teeth, and sweat glands.

The EDARADD protein contains a death domain that interacts with the death domain of EDAR upon activation by ectodysplasin A (EDA). This interaction leads to the recruitment of additional signaling proteins and ultimately activates downstream targets, which regulate cellular processes such as proliferation, differentiation, and apoptosis.

Mutations in the EDARADD gene have been associated with several human genetic disorders, including ectodermal dysplasias, hypohidrotic ectodermal dysplasia (HED), and an autosomal recessive form of cleft lip/palate. These conditions are characterized by abnormalities in the development of structures derived from the ectoderm, such as skin, hair, teeth, nails, and sweat glands.

Sweat glands are specialized tubular structures in the skin that produce and secrete sweat, also known as perspiration. They are part of the body's thermoregulatory system, helping to maintain optimal body temperature by releasing water and heat through evaporation. There are two main types of sweat glands: eccrine and apocrine.

1. Eccrine sweat glands: These are distributed throughout the body, with a higher concentration on areas like the palms, soles, and forehead. They are responsible for producing a watery, odorless sweat that primarily helps to cool down the body through evaporation.

2. Apocrine sweat glands: These are mainly found in the axillary (armpit) region and around the anogenital area. They become active during puberty and produce a thick, milky fluid that does not have a strong odor on its own but can mix with bacteria on the skin's surface, leading to body odor.

Sweat glands are controlled by the autonomic nervous system, meaning they function involuntarily in response to various stimuli such as emotions, physical activity, or changes in environmental temperature.

A hair follicle is a part of the human skin from which hair grows. It is a complex organ that consists of several layers, including an outer root sheath, inner root sheath, and matrix. The hair follicle is located in the dermis, the second layer of the skin, and is surrounded by sebaceous glands and erector pili muscles.

The hair growth cycle includes three phases: anagen (growth phase), catagen (transitional phase), and telogen (resting phase). During the anagen phase, cells in the matrix divide rapidly to produce new hair fibers that grow out of the follicle. The hair fiber is made up of a protein called keratin, which also makes up the outer layers of the skin and nails.

Hair follicles are important for various biological functions, including thermoregulation, sensory perception, and social communication. They also play a role in wound healing and can serve as a source of stem cells that can differentiate into other cell types.

Medically, hair is defined as a threadlike structure that grows from the follicles found in the skin of mammals. It is primarily made up of a protein called keratin and consists of three parts: the medulla (the innermost part or core), the cortex (middle layer containing keratin filaments) and the cuticle (outer layer of overlapping scales).

Hair growth occurs in cycles, with each cycle consisting of a growth phase (anagen), a transitional phase (catagen), and a resting phase (telogen). The length of hair is determined by the duration of the anagen phase.

While hair plays a crucial role in protecting the skin from external factors like UV radiation, temperature changes, and physical damage, it also serves as an essential aspect of human aesthetics and identity.

I'm sorry for any confusion, but "Smegmamorpha" is not a recognized term in medical or scientific fields. It seems like it might be a made-up word, possibly a combination of "smegma," which refers to the secretions found in the genital area, and "-morpha," which is often used in taxonomy to denote a subgroup or form. However, I cannot find any legitimate scientific or medical use for this term.

A tooth is a hard, calcified structure found in the jaws (upper and lower) of many vertebrates and used for biting and chewing food. In humans, a typical tooth has a crown, one or more roots, and three layers: the enamel (the outermost layer, hardest substance in the body), the dentin (the layer beneath the enamel), and the pulp (the innermost layer, containing nerves and blood vessels). Teeth are essential for proper nutrition, speech, and aesthetics. There are different types of teeth, including incisors, canines, premolars, and molars, each designed for specific functions in the mouth.

Fibroblast Growth Factor 4 (FGF4) is a growth factor that belongs to the fibroblast growth factor family. It plays a crucial role in various biological processes, including embryonic development, cell survival, proliferation, and differentiation. Specifically, FGF4 has been implicated in the development of the musculoskeletal system, where it helps regulate the growth and patterning of limbs and bones.

FGF4 exerts its effects by binding to specific receptors on the surface of target cells, known as fibroblast growth factor receptors (FGFRs). This interaction triggers a cascade of intracellular signaling events that ultimately lead to changes in gene expression and cell behavior.

In addition to its role in development, FGF4 has also been implicated in various pathological processes, including cancer. For example, elevated levels of FGF4 have been observed in certain types of tumors, where it may contribute to tumor growth and progression by promoting the survival and proliferation of cancer cells.

Odontogenesis is the process of tooth development that involves the formation and calcification of teeth. It is a complex process that requires the interaction of several types of cells, including epithelial cells, mesenchymal cells, and odontoblasts. The process begins during embryonic development with the formation of dental lamina, which gives rise to the tooth bud. As the tooth bud grows and differentiates, it forms the various structures of the tooth, including the enamel, dentin, cementum, and pulp. Odontogenesis is completed when the tooth erupts into the oral cavity. Abnormalities in odontogenesis can result in developmental dental anomalies such as tooth agenesis, microdontia, or odontomas.

Ectoderm is the outermost of the three primary germ layers in a developing embryo, along with the endoderm and mesoderm. The ectoderm gives rise to the outer covering of the body, including the skin, hair, nails, glands, and the nervous system, which includes the brain, spinal cord, and peripheral nerves. It also forms the lining of the mouth, anus, nose, and ears. Essentially, the ectoderm is responsible for producing all the epidermal structures and the neural crest cells that contribute to various derivatives such as melanocytes, adrenal medulla, smooth muscle, and peripheral nervous system components.

Tumor Necrosis Factor (TNF) Receptors are cell surface receptors that bind to tumor necrosis factor cytokines. They play crucial roles in the regulation of a variety of immune cell functions, including inflammation, immunity, and cell survival or death (apoptosis).

There are two major types of TNF receptors: TNFR1 (also known as p55 or CD120a) and TNFR2 (also known as p75 or CD120b). TNFR1 is widely expressed in most tissues, while TNFR2 has a more restricted expression pattern and is mainly found on immune cells.

TNF receptors have an intracellular domain called the death domain, which can trigger signaling pathways leading to apoptosis when activated by TNF ligands. However, they can also activate other signaling pathways that promote cell survival, differentiation, and inflammation. Dysregulation of TNF receptor signaling has been implicated in various diseases, including cancer, autoimmune disorders, and neurodegenerative conditions.

In the context of dentistry, a molar is a type of tooth found in the back of the mouth. They are larger and wider than other types of teeth, such as incisors or canines, and have a flat biting surface with multiple cusps. Molars are primarily used for grinding and chewing food into smaller pieces that are easier to swallow. Humans typically have twelve molars in total, including the four wisdom teeth.

In medical terminology outside of dentistry, "molar" can also refer to a unit of mass in the apothecaries' system of measurement, which is equivalent to 4.08 grams. However, this usage is less common and not related to dental or medical anatomy.

Activins are a type of protein that belongs to the transforming growth factor-beta (TGF-β) superfamily. They are produced and released by various cells in the body, including those in the ovaries, testes, pituitary gland, and other tissues. Activins play important roles in regulating several biological processes, such as cell growth, differentiation, and apoptosis (programmed cell death).

Activins bind to specific receptors on the surface of cells, leading to the activation of intracellular signaling pathways that control gene expression. They are particularly well-known for their role in reproductive biology, where they help regulate follicle stimulation and hormone production in the ovaries and testes. Activins also have been implicated in various disease processes, including cancer, fibrosis, and inflammation.

There are three main isoforms of activin in humans: activin A, activin B, and inhibin A. While activins and inhibins share similar structures and functions, they have opposite effects on the activity of the pituitary gland. Activins stimulate the production of follicle-stimulating hormone (FSH), while inhibins suppress it. This delicate balance between activins and inhibins helps regulate reproductive function and other physiological processes in the body.

Organ culture techniques refer to the methods used to maintain or grow intact organs or pieces of organs under controlled conditions in vitro, while preserving their structural and functional characteristics. These techniques are widely used in biomedical research to study organ physiology, pathophysiology, drug development, and toxicity testing.

Organ culture can be performed using a variety of methods, including:

1. Static organ culture: In this method, the organs or tissue pieces are placed on a porous support in a culture dish and maintained in a nutrient-rich medium. The medium is replaced periodically to ensure adequate nutrition and removal of waste products.
2. Perfusion organ culture: This method involves perfusing the organ with nutrient-rich media, allowing for better distribution of nutrients and oxygen throughout the tissue. This technique is particularly useful for studying larger organs such as the liver or kidney.
3. Microfluidic organ culture: In this approach, microfluidic devices are used to create a controlled microenvironment for organ cultures. These devices allow for precise control over the flow of nutrients and waste products, as well as the application of mechanical forces.

Organ culture techniques can be used to study various aspects of organ function, including metabolism, secretion, and response to drugs or toxins. Additionally, these methods can be used to generate three-dimensional tissue models that better recapitulate the structure and function of intact organs compared to traditional two-dimensional cell cultures.

Membrane proteins are a type of protein that are embedded in the lipid bilayer of biological membranes, such as the plasma membrane of cells or the inner membrane of mitochondria. These proteins play crucial roles in various cellular processes, including:

1. Cell-cell recognition and signaling
2. Transport of molecules across the membrane (selective permeability)
3. Enzymatic reactions at the membrane surface
4. Energy transduction and conversion
5. Mechanosensation and signal transduction

Membrane proteins can be classified into two main categories: integral membrane proteins, which are permanently associated with the lipid bilayer, and peripheral membrane proteins, which are temporarily or loosely attached to the membrane surface. Integral membrane proteins can further be divided into three subcategories based on their topology:

1. Transmembrane proteins, which span the entire width of the lipid bilayer with one or more alpha-helices or beta-barrels.
2. Lipid-anchored proteins, which are covalently attached to lipids in the membrane via a glycosylphosphatidylinositol (GPI) anchor or other lipid modifications.
3. Monotopic proteins, which are partially embedded in the membrane and have one or more domains exposed to either side of the bilayer.

Membrane proteins are essential for maintaining cellular homeostasis and are targets for various therapeutic interventions, including drug development and gene therapy. However, their structural complexity and hydrophobicity make them challenging to study using traditional biochemical methods, requiring specialized techniques such as X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and single-particle cryo-electron microscopy (cryo-EM).

Wnt proteins are a family of secreted signaling molecules that play crucial roles in the regulation of fundamental biological processes, including cell proliferation, differentiation, migration, and survival. They were first discovered in 1982 through genetic studies in Drosophila melanogaster (fruit flies) and have since been found to be highly conserved across various species, from invertebrates to humans.

Wnt proteins exert their effects by binding to specific receptors on the target cell surface, leading to the activation of several intracellular signaling pathways:

1. Canonical Wnt/β-catenin pathway: In the absence of Wnt ligands, β-catenin is continuously degraded by a destruction complex consisting of Axin, APC (Adenomatous polyposis coli), and GSK3β (Glycogen synthase kinase 3 beta). When Wnt proteins bind to their receptors Frizzled and LRP5/6, the formation of a "signalosome" complex leads to the inhibition of the destruction complex, allowing β-catenin to accumulate in the cytoplasm and translocate into the nucleus. Here, it interacts with TCF/LEF (T-cell factor/lymphoid enhancer-binding factor) transcription factors to regulate the expression of target genes involved in cell proliferation, differentiation, and survival.
2. Non-canonical Wnt pathways: These include the Wnt/Ca^2+^ pathway and the planar cell polarity (PCP) pathway. In the Wnt/Ca^2+^ pathway, Wnt ligands bind to Frizzled receptors and activate heterotrimeric G proteins, leading to an increase in intracellular Ca^2+^ levels and activation of downstream targets such as protein kinase C (PKC) and calcium/calmodulin-dependent protein kinase II (CAMKII). These signaling events ultimately regulate cell movement, adhesion, and gene expression. In the PCP pathway, Wnt ligands bind to Frizzled receptors and coreceptor complexes containing Ror2 or Ryk, leading to activation of small GTPases such as RhoA and Rac1, which control cytoskeletal organization and cell polarity.

Dysregulation of Wnt signaling has been implicated in various human diseases, including cancer, developmental disorders, and degenerative conditions. In cancer, aberrant activation of the canonical Wnt/β-catenin pathway contributes to tumor initiation, progression, and metastasis by promoting cell proliferation, survival, and epithelial-mesenchymal transition (EMT). Inhibitors targeting different components of the Wnt signaling pathway are currently being developed as potential therapeutic strategies for cancer treatment.

The epidermis is the outermost layer of the skin, composed mainly of stratified squamous epithelium. It forms a protective barrier that prevents water loss and inhibits the entry of microorganisms. The epidermis contains no blood vessels, and its cells are nourished by diffusion from the underlying dermis. The bottom-most layer of the epidermis, called the stratum basale, is responsible for generating new skin cells that eventually move up to replace dead cells on the surface. This process of cell turnover takes about 28 days in adults.

The most superficial part of the epidermis consists of dead cells called squames, which are constantly shed and replaced. The exact rate at which this happens varies depending on location; for example, it's faster on the palms and soles than elsewhere. Melanocytes, the pigment-producing cells, are also located in the epidermis, specifically within the stratum basale layer.

In summary, the epidermis is a vital part of our integumentary system, providing not only physical protection but also playing a crucial role in immunity and sensory perception through touch receptors called Pacinian corpuscles.

In situ hybridization (ISH) is a molecular biology technique used to detect and localize specific nucleic acid sequences, such as DNA or RNA, within cells or tissues. This technique involves the use of a labeled probe that is complementary to the target nucleic acid sequence. The probe can be labeled with various types of markers, including radioisotopes, fluorescent dyes, or enzymes.

During the ISH procedure, the labeled probe is hybridized to the target nucleic acid sequence in situ, meaning that the hybridization occurs within the intact cells or tissues. After washing away unbound probe, the location of the labeled probe can be visualized using various methods depending on the type of label used.

In situ hybridization has a wide range of applications in both research and diagnostic settings, including the detection of gene expression patterns, identification of viral infections, and diagnosis of genetic disorders.

Morphogenesis is a term used in developmental biology and refers to the process by which cells give rise to tissues and organs with specific shapes, structures, and patterns during embryonic development. This process involves complex interactions between genes, cells, and the extracellular environment that result in the coordinated movement and differentiation of cells into specialized functional units.

Morphogenesis is a dynamic and highly regulated process that involves several mechanisms, including cell proliferation, death, migration, adhesion, and differentiation. These processes are controlled by genetic programs and signaling pathways that respond to environmental cues and regulate the behavior of individual cells within a developing tissue or organ.

The study of morphogenesis is important for understanding how complex biological structures form during development and how these processes can go awry in disease states such as cancer, birth defects, and degenerative disorders.

Developmental gene expression regulation refers to the processes that control the activation or repression of specific genes during embryonic and fetal development. These regulatory mechanisms ensure that genes are expressed at the right time, in the right cells, and at appropriate levels to guide proper growth, differentiation, and morphogenesis of an organism.

Developmental gene expression regulation is a complex and dynamic process involving various molecular players, such as transcription factors, chromatin modifiers, non-coding RNAs, and signaling molecules. These regulators can interact with cis-regulatory elements, like enhancers and promoters, to fine-tune the spatiotemporal patterns of gene expression during development.

Dysregulation of developmental gene expression can lead to various congenital disorders and developmental abnormalities. Therefore, understanding the principles and mechanisms governing developmental gene expression regulation is crucial for uncovering the etiology of developmental diseases and devising potential therapeutic strategies.

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.

A ligand, in the context of biochemistry and medicine, is a molecule that binds to a specific site on a protein or a larger biomolecule, such as an enzyme or a receptor. This binding interaction can modify the function or activity of the target protein, either activating it or inhibiting it. Ligands can be small molecules, like hormones or neurotransmitters, or larger structures, like antibodies. The study of ligand-protein interactions is crucial for understanding cellular processes and developing drugs, as many therapeutic compounds function by binding to specific targets within the body.

"Entrez Gene: EDA2R ectodysplasin A2 receptor". Hashimoto T, Cui CY, Schlessinger D (2006). "Repertoire of mouse ectodysplasin-A ... Tumor necrosis factor receptor superfamily member 27 is a protein that in humans is encoded by the EDA2R gene. EDA-A1 and EDA- ... 2003). "Role of TRAF3 and -6 in the activation of the NF-kappa B and JNK pathways by X-linked ectodermal dysplasia receptor". J ... This protein is a type III transmembrane protein of the TNFR (tumor necrosis factor receptor) superfamily, and contains 3 ...
IPR034052 Tumor necrosis factor receptor EDAR, N-terminal. IPR047526 Tumor necrosis factor receptor superfamily member 19/27/ ... J:334712 Wark AR, et al., Ectodysplasin Signaling through XEDAR Is Required for Mammary Gland Morphogenesis. J Invest Dermatol ...
EDA: ectodysplasin A. *EDAR: ectodysplasin A receptor. *EDARADD: EDAR associated via death domain ...
... two isoforms of ectodysplasin A; EDA-A1 isoform, binds to EDA-A1 receptor (EDAR); EDA-A2 isoform, binds to EDA-A2 receptor ( ... 2009), which activates receptors belonging to the frizzled (Dann et al. 2001) and LRP (LDL receptor-related protein) (May et al ... 1998). Both murine and human receptors comprise regions highly homologous to the TNF receptors, accounting for trimerization ... Mutation screening of the Ectodysplasin-A receptor gene EDAR in hypohidrotic ectodermal dysplasia. Eur J Hum Genet 16:673-679 ...
Recent positive selection of a human androgen receptor/ectodysplasin A2 receptor haplotype and its relationship to male pattern ... The androgen receptor binds testosterone, and increased sensitivity is associated with more severe MPB15. Three large-scale MPB ... See Box1 for an overview of heritability definitions.) The Xq12 locus within the androgen receptor gene (AR) was the first ... Genetic variation in the human androgen receptor gene is the major determinant of common early-onset androgenetic alopecia. Am ...
Variants of the ectodysplasin A1 receptor gene underlying homozygous cases of autosomal recessive hypohidrotic ectodermal ... Ectodysplasin A in biological fluids of ectodermal dysplasia. J. Dent. Res. 96, 217-224. Podzus, J., Kowalczyk-Quintas, C., ... Prenatal treatment of X-linked hypohidrotic ectodermal dysplasia using recombinant ectodysplasin in a canine model. J. ... Generation and characterization of function blocking anti-ectodysplasin A (EDA) monoclonal antibodies that induce ectodermal ...
... like/TNV receptor signaling pathway, which involves ectodysplasin (EDA), the EDR receptor (EDAR), the EDAR-associated death ... ectodysplasin) receptor. [18] Autosomal recessive hypohidrotic ectodermal dysplasia may also result from mutations in the ... Mutations of PVRL1, encoding a cell-cell adhesion molecule/herpesvirus receptor, in cleft lip/palate-ectodermal dysplasia. Nat ... 15, 16] Ectodysplasin is important in promoting cell survival, growth, and differentiation. Using specialized techniques, ...
The ectodysplasin A receptor (EDAR) gene has a range of pleiotropic effects, including sweat gland density, incisor shoveling, ...
... like/TNV receptor signaling pathway, which involves ectodysplasin (EDA), the EDR receptor (EDAR), the EDAR-associated death ... ectodysplasin) receptor. [18] Autosomal recessive hypohidrotic ectodermal dysplasia may also result from mutations in the ... Mutations of PVRL1, encoding a cell-cell adhesion molecule/herpesvirus receptor, in cleft lip/palate-ectodermal dysplasia. Nat ... 15, 16] Ectodysplasin is important in promoting cell survival, growth, and differentiation. Using specialized techniques, ...
... ectodysplasin-A receptor). This gene is known to be involved in gill-raker development in zebrafish, where edar knockouts ... hitting with high confidence against the ectodysplasin-A receptor (edar) gene (E-value 1e-20; ID% 97.62 in Brown Trout ... Colosimo, P. F. et al. Widespread parallel evolution in sticklebacks by repeated fixation of Ectodysplasin alleles. Science 307 ...
Ectodysplasin A Receptor Blocking Peptide. 33R-6971 Fitzgerald 100 ug. 216 EUR ... Description: A synthetic peptide for use as a blocking control in assays to test for specificity of TGF beta Receptor I ... Description: A synthetic peptide for use as a blocking control in assays to test for specificity of MC4 Receptor antibody, ... Description: A synthetic Dopamine Receptor 2 Blocking peptide for use as a blocking control in assays to test for specificity ...
Edaradd ELISA Kit, Mouse Ectodysplasin-A receptor-associated ad. EF014766 Lifescience Market 96 Tests. ... Pig VEGFR1(Vascular Endothelial Growth Factor Receptor 1) ELISA Kit. *Pig VEGFR2(Vascular Endothelial Growth Factor Receptor 2 ... Mouse sRAGE(Soluble receptor for advanced glycation endproducts) ELISA Kit. *Mouse SRD5a1(Steroid 5 Alpha Reductase 1) ELISA ... Mouse BMX(BMX Non Receptor Tyrosine Kinase) ELISA Kit. *Mouse C1QTNF9(C1q and Tumor Necrosis Factor Related Protein 9) ELISA ...
EDAR (ectodysplasin A receptor) 2008 2016-07-01 Active Alu retrotransposons in the human genome. A. Bennett et al. 0 Short ... EDAR (ectodysplasin A receptor) 2007 2016-07-01 Nutritional iron deficiency: an evolutionary perspective. S. Denic et al. 0 ... The genetic and evolutionary balances in human NK cell receptor diversity. P. Parham 0 Killer Inhibitory Receptor Composition ... DRD4 (dopamine receptor D4) 2007 2016-06-30 The evolution of neuron types and cortical histology in apes and humans C. Sherwood ...
Expression of ectodysplasin A1 and ectodysplasin receptor in initiating primary wool follicles. In Proceedings of the Fifth ... Parsons, Y., Webb, G., & Bottema, C. (1998). Assignment of the growth hormone receptor gene to band q17 of the homoeologous ... Pal, S., Thomson, A., Bottema, C., & Roach, P. (2003). α-Tocopherol modulates the low density lipoprotein receptor of human ... Bursill, C., Roach, P., Bottema, C., & Pal, S. (2001). Green tea upregulates the low-density lipoprotein receptor through the ...
04060 Cytokine-cytokine receptor interaction. 100340021. 09180 Brite Hierarchies. 09183 Protein families: signaling and ... ectodysplasin-A. Organism. ocu Oryctolagus cuniculus (rabbit). Pathway. ocu04060 Cytokine-cytokine receptor interaction. ...
Three different genes have been associated with FPHL, Ectodysplasin A2 Receptor (EDA2R), Androgen Receptor (AR), Aromatase ... The etiology of FPHL is in part associated with decreasing free estrogen levels and possibly end organ receptor affinity. ... Three different genes have been associated with FPHL, Ectodysplasin A2 Receptor (EDA2R), Androgen Receptor (AR), Aromatase ... The etiology of FPHL is in part associated with decreasing free estrogen levels and possibly end organ receptor affinity. ...
Mutation screening of the ectodysplasin-A receptor gene EDAR inhypohidrotic ectodermal dysplasia. Eur J Hum Genet. 2008; 16: ...
Molecular and therapeutic characterization of anti-ectodysplasin A receptor (EDAR) agonist monoclonal antibodies ... The expression of Wnt ligands Wnt3, Wnt7a and Wnt9b was also altered, along with genes involved in Bmp, ectodysplasin (Eda), ... Hence, small doses of Wnt agonists that target inhibitors of receptor binding, when delivered in a controlled manner and during ... as shown to be effective for the delivery of recombinant ectodysplasin (Hermes et al., 2014). Alternatively, early postnatal ...
ectodysplasin-A receptor. protein-coding. .leftmenu ul li ul { padding-left: 10px;} ORF ...
I am reading on wikipedia that a certain mutation in the Ectodysplasin A receptor known as rs3827760 or 370A is responsible ...
eda: ectodysplasin A eda2r: ectodysplasin A2 receptor edar: ectodysplasin A receptor ...
EDAR (Ectodysplasin A Receptor): * EDAR Antikörper * EDAR ELISA Kits * EDAR Proteine EDARADD (EDAR-Associated Death Domain): * ... Ectodysplasin (EDA-A1) ist in der Lage, an den TNF-Rezeptor EDAR zu binden, was zur Bildung eines Komplexes aus EDAD, TRAF6, ...
The murine mutant is deficient in the main element ectodermal signaling molecule ectodysplasin-A1 (EDA), which is necessary ... during prenatal development to trigger signal transduction from its receptor EDAR, initiating development and morphogenesis of ... The murine mutant is deficient in the main element ectodermal signaling molecule ectodysplasin-A1 (EDA), which is necessary ...
Our gene expression analysis in muscle tissues indicated upregulation of ectodysplasin A2 receptor (EDA2R) in tumour-bearing ... Caquexia , Atrofia Muscular , Neoplasias , Transdução de Sinais , Receptor Xedar , Animais , Camundongos , Caquexia/ ... Tumour-induced oncostatin M (OSM) upregulated muscle EDA2R expression, and muscle-specific oncostatin M receptor (OSMR)- ... Receptor Xedar/metabolismo , Humanos , Ligantes , Receptores de Oncostatina M/metabolismo , Oncostatina M/metabolismo ...
... and a mutation of ectodysplasin A receptor (EDAR) gene (c.871G,A) were detected by whole genome sequencing in four HED patients ... ACE inhibitors or angiotensin receptor blockers, beta-receptor blockers while the proportion of antiarrhythmic drugs was lower ... Objective:To investigate the effects of Da Jianzhongtang on substance P (SP), mast cells (MC), Toll like receptor 2 (TLR2), ... Results: Three reported mutations of ectodysplasin A (EDA) gene (c.2T,C, c.161A,G, c.467G,A) ...
TNF signaling via the ligand-receptor pair ectodysplasin and edar controls the function of epithelial signaling centers and is ... Regulation of hair follicle development by the TNF signal ectodysplasin and its receptor Edar. Development. 2002, 129: 2541-53. ... Organizing Malawi cichlid dentitions with the spacer gene wnt7b and ectodysplasin. Left panel: wnt7b is expressed in the zone ... Pummila M, Fliniaux I, Jaatinen R, James MJ, Laurikkala J, Schneider P, Thesleff I, Mikkola ML: Ectodysplasin has a dual role ...
A new variant of the ectodysplasin A receptor death domain gene associated with anhidrotic ectodermal dysplasia in a Turkish ...
... as well as the ectodermal development receptor ectodysplasin. Therefore, defects at the level of NEMO lead to problems with ... including the toll-like receptors (TLR) as well as cytokine receptors, such as the IL-1 (interleukin 12) receptor). IRAK4 and ... Toll-like receptor signaling defects*What every physician needs to know:*Are you sure your patient has a toll-like receptor ... Toll-like receptor signaling defects. What every physician needs to know:. This chapter discusses Toll-like receptor signaling ...
Mutation of genes encoding the ligand EDA, its transmembrane receptor EDAR, and the intracellular signal transducer EDARADD ... dogs and humans the growth and function of sebaceous glands and eyelid Meibomian glands depend on the ectodysplasin signalling ...
... like/TNV receptor signaling pathway, which involves ectodysplasin (EDA), the EDR receptor (EDAR), the EDAR-associated death ... Mutations of PVRL1, encoding a cell-cell adhesion molecule/herpesvirus receptor, in cleft lip/palate-ectodermal dysplasia. Nat ...

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