A class of cell surface receptors for PURINES that prefer ATP or ADP over ADENOSINE. P2 purinergic receptors are widespread in the periphery and in the central and peripheral nervous system.
A purinergic P2X neurotransmitter receptor that plays a role in pain sensation signaling and regulation of inflammatory processes.
Compounds that bind to and block the stimulation of PURINERGIC P2X RECEPTORS. Included under this heading are antagonists for specific P2X receptor subtypes.
Compounds that bind to and stimulate PURINERGIC P2X RECEPTORS. Included under this heading are agonists for specific P2X receptor subtypes.
A subclass of purinergic P2 receptors that signal by means of a ligand-gated ion channel. They are comprised of three P2X subunits which can be identical (homotrimeric form) or dissimilar (heterotrimeric form).
A purinergic P2X neurotransmitter receptor involved in sensory signaling of TASTE PERCEPTION, chemoreception, visceral distension, and NEUROPATHIC PAIN. The receptor comprises three P2X3 subunits. The P2X3 subunits are also associated with P2X2 RECEPTOR subunits in a heterotrimeric receptor variant.
A subclass of purinergic P2Y receptors that have a preference for ATP and UTP. The activated P2Y2 receptor acts through a G-PROTEIN-coupled PHOSPHATIDYLINOSITOL and intracellular CALCIUM SIGNALING pathway.
A widely distributed purinergic P2X receptor subtype that plays a role in pain sensation. P2X4 receptors found on MICROGLIA cells may also play a role in the mediation of allodynia-related NEUROPATHIC PAIN.
A subclass of purinergic P2Y receptors that have a preference for ATP and ADP. The activated P2Y1 receptor signals through the G-PROTEIN-coupled activation of PHOSPHOLIPASE C and mobilization of intracellular CALCIUM.
Compounds that bind to and block the stimulation of PURINERGIC P2 RECEPTORS.
Compounds that bind to and stimulate PURINERGIC P2Y RECEPTORS. Included under this heading are agonists for specific P2Y receptor subtypes.
Cell surface proteins that bind PURINES with high affinity and trigger intracellular changes which influence the behavior of cells. The best characterized classes of purinergic receptors in mammals are the P1 receptors, which prefer ADENOSINE, and the P2 receptors, which prefer ATP or ADP.
A subclass of purinergic P2 receptors whose signaling is coupled through a G-PROTEIN signaling mechanism.
Compounds that bind to and stimulate PURINERGIC P2 RECEPTORS.
A purinergic P2X neurotransmitter receptor involved in sensory signaling of TASTE PERCEPTION, chemoreception, visceral distension and NEUROPATHIC PAIN. The receptor comprises three P2X2 subunits. The P2X2 subunits also have been found associated with P2X3 RECEPTOR subunits in a heterotrimeric receptor variant.
Drugs that bind to and block the activation of PURINERGIC RECEPTORS.
Compounds that bind to and activate PURINERGIC RECEPTORS.
An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.
A subclass of purinergic P2Y receptors that have a preference for ADP binding and are coupled to GTP-BINDING PROTEIN ALPHA SUBUNIT, GI. The P2Y12 purinergic receptors are found in PLATELETS where they play an important role regulating PLATELET ACTIVATION.
A purinergic P2X neurotransmitter receptor found at high levels in the BRAIN and IMMUNE SYSTEM.
A purinergic P2X neurotransmitter receptor found at sympathetically innervated SMOOTH MUSCLE. It may play a functional role regulating the juxtoglomerular apparatus of the KIDNEY.
Uridine 5'-(tetrahydrogen triphosphate). A uracil nucleotide containing three phosphate groups esterified to the sugar moiety.
A polyanionic compound with an unknown mechanism of action. It is used parenterally in the treatment of African trypanosomiasis and it has been used clinically with diethylcarbamazine to kill the adult Onchocerca. (From AMA Drug Evaluations Annual, 1992, p1643) It has also been shown to have potent antineoplastic properties.
This is the active form of VITAMIN B 6 serving as a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. During transamination of amino acids, pyridoxal phosphate is transiently converted into pyridoxamine phosphate (PYRIDOXAMINE).
Compounds that bind to and block the stimulation of PURINERGIC P2Y RECEPTORS. Included under this heading are antagonists for specific P2Y receptor subtypes.
A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.
Signal transduction mechanisms whereby calcium mobilization (from outside the cell or from intracellular storage pools) to the cytoplasm is triggered by external stimuli. Calcium signals are often seen to propagate as waves, oscillations, spikes, sparks, or puffs. The calcium acts as an intracellular messenger by activating calcium-responsive proteins.
A class of cell surface receptors that prefer ADENOSINE to other endogenous PURINES. Purinergic P1 receptors are widespread in the body including the cardiovascular, respiratory, immune, and nervous systems. There are at least two pharmacologically distinguishable types (A1 and A2, or Ri and Ra).
Compounds that act on PURINERGIC RECEPTORS or influence the synthesis, storage, uptake, metabolism, or release of purinergic transmitters.
A calcium-activated enzyme that catalyzes the hydrolysis of ATP to yield AMP and orthophosphate. It can also act on ADP and other nucleoside triphosphates and diphosphates. EC 3.6.1.5.
Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position.
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.
Compounds that bind to and stimulate PURINERGIC P1 RECEPTORS.
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 strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company.
Compounds that bind to and block the stimulation of PURINERGIC P1 RECEPTORS.
An interleukin-1 subtype that is synthesized as an inactive membrane-bound pro-protein. Proteolytic processing of the precursor form by CASPASE 1 results in release of the active form of interleukin-1beta from the membrane.
A series of heterocyclic compounds that are variously substituted in nature and are known also as purine bases. They include ADENINE and GUANINE, constituents of nucleic acids, as well as many alkaloids such as CAFFEINE and THEOPHYLLINE. Uric acid is the metabolic end product of purine metabolism.
Inbred C57BL mice are a strain of laboratory mice that have been produced by many generations of brother-sister matings, resulting in a high degree of genetic uniformity and homozygosity, making them widely used for biomedical research, including studies on genetics, immunology, cancer, and neuroscience.
The basic cellular units of nervous tissue. Each neuron consists of a body, an axon, and dendrites. Their purpose is to receive, conduct, and transmit impulses in the NERVOUS SYSTEM.
A strain of albino rat developed at the Wistar Institute that has spread widely at other institutions. This has markedly diluted the original strain.
Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes.
A nucleoside that is composed of ADENINE and D-RIBOSE. Adenosine or adenosine derivatives play many important biological roles in addition to being components of DNA and RNA. Adenosine itself is a neurotransmitter.
Established cell cultures that have the potential to propagate indefinitely.
A musculomembranous sac along the URINARY TRACT. URINE flows from the KIDNEYS into the bladder via the ureters (URETER), and is held there until URINATION.
Use of electric potential or currents to elicit biological responses.
The excretory duct of the testes that carries SPERMATOZOA. It rises from the SCROTUM and joins the SEMINAL VESICLES to form the ejaculatory duct.
Nucleotides in which the base moiety is substituted with one or more sulfur atoms.
The communication from a NEURON to a target (neuron, muscle, or secretory cell) across a SYNAPSE. In chemical synaptic transmission, the presynaptic neuron releases a NEUROTRANSMITTER that diffuses across the synaptic cleft and binds to specific synaptic receptors, activating them. The activated receptors modulate specific ion channels and/or second-messenger systems in the postsynaptic cell. In electrical synaptic transmission, electrical signals are communicated as an ionic current flow across ELECTRICAL SYNAPSES.
A uracil nucleotide containing a pyrophosphate group esterified to C5 of the sugar moiety.
An agent derived from licorice root. It is used for the treatment of digestive tract ulcers, especially in the stomach. Antidiuretic side effects are frequent, but otherwise the drug is low in toxicity.
A glycoprotein enzyme present in various organs and in many cells. The enzyme catalyzes the hydrolysis of a 5'-ribonucleotide to a ribonucleoside and orthophosphate in the presence of water. It is cation-dependent and exists in a membrane-bound and soluble form. EC 3.1.3.5.
A selective adrenergic alpha-1 antagonist used in the treatment of HEART FAILURE; HYPERTENSION; PHEOCHROMOCYTOMA; RAYNAUD DISEASE; PROSTATIC HYPERTROPHY; and URINARY RETENTION.
Unstriated and unstriped muscle, one of the muscles of the internal organs, blood vessels, hair follicles, etc. Contractile elements are elongated, usually spindle-shaped cells with centrally located nuclei. Smooth muscle fibers are bound together into sheets or bundles by reticular fibers and frequently elastic nets are also abundant. (From Stedman, 25th ed)
A subtype of ADENOSINE RECEPTOR that is found expressed in a variety of tissues including the BRAIN and DORSAL HORN NEURONS. The receptor is generally considered to be coupled to the GI, INHIBITORY G-PROTEIN which causes down regulation of CYCLIC AMP.
Adenine nucleotides are molecules that consist of an adenine base attached to a ribose sugar and one, two, or three phosphate groups, including adenosine monophosphate (AMP), adenosine diphosphate (ADP), and adenosine triphosphate (ATP), which play crucial roles in energy transfer and signaling processes within cells.
Substances used for their pharmacological actions on any aspect of neurotransmitter systems. Neurotransmitter agents include agonists, antagonists, degradation inhibitors, uptake inhibitors, depleters, precursors, and modulators of receptor function.
A subclass of phospholipases that hydrolyze the phosphoester bond found in the third position of GLYCEROPHOSPHOLIPIDS. Although the singular term phospholipase C specifically refers to an enzyme that catalyzes the hydrolysis of PHOSPHATIDYLCHOLINE (EC 3.1.4.3), it is commonly used in the literature to refer to broad variety of enzymes that specifically catalyze the hydrolysis of PHOSPHATIDYLINOSITOLS.
A process leading to shortening and/or development of tension in muscle tissue. Muscle contraction occurs by a sliding filament mechanism whereby actin filaments slide inward among the myosin filaments.
The voltage differences across a membrane. For cellular membranes they are computed by subtracting the voltage measured outside the membrane from the voltage measured inside the membrane. They result from differences of inside versus outside concentration of potassium, sodium, chloride, and other ions across cells' or ORGANELLES membranes. For excitable cells, the resting membrane potentials range between -30 and -100 millivolts. Physical, chemical, or electrical stimuli can make a membrane potential more negative (hyperpolarization), or less negative (depolarization).
The monomeric units from which DNA or RNA polymers are constructed. They consist of a purine or pyrimidine base, a pentose sugar, and a phosphate group. (From King & Stansfield, A Dictionary of Genetics, 4th ed)
Solutions that have a lesser osmotic pressure than a reference solution such as blood, plasma, or interstitial fluid.
Compounds that contain the triphenylmethane aniline structure found in rosaniline. Many of them have a characteristic magenta color and are used as COLORING AGENTS.
Interstitial space between cells, occupied by INTERSTITIAL FLUID as well as amorphous and fibrous substances. For organisms with a CELL WALL, the extracellular space includes everything outside of the CELL MEMBRANE including the PERIPLASM and the cell wall.
A group of homologous proteins which form the intermembrane channels of GAP JUNCTIONS. The connexins are the products of an identified gene family which has both highly conserved and highly divergent regions. The variety contributes to the wide range of functional properties of gap junctions.

Expression of both P1 and P2 purine receptor genes by human articular chondrocytes and profile of ligand-mediated prostaglandin E2 release. (1/2286)

OBJECTIVE: To assess the expression and function of purine receptors in articular chondrocytes. METHODS: Reverse transcriptase-polymerase chain reaction (RT-PCR) was used to screen human chondrocyte RNA for expression of P1 and P2 purine receptor subtypes. Purine-stimulated prostaglandin E2 (PGE2) release from chondrocytes, untreated or treated with recombinant human interleukin-1alpha (rHuIL-1alpha), was assessed by radioimmunoassay. RESULTS: RT-PCR demonstrated that human articular chondrocytes transcribe messenger RNA for the P1 receptor subtypes A2a and A2b and the P2 receptor subtype P2Y2, but not for the P1 receptor subtypes A1 and A3. The P1 receptor agonists adenosine and 5'-N-ethylcarboxamidoadenosine did not change PGE2 release from chondrocytes. The P2Y2 agonists ATP and UTP stimulated a small release of PGE2 that was potentiated after pretreatment with rHuIL-1alpha. PGE2 release in response to ATP and UTP cotreatment was not additive, but release in response to coaddition of ATP and bradykinin (BK) or UTP and BK was additive, consistent with ATP and UTP competition for the same receptor site. The potentiation of PGE2 release in response to ATP and UTP after rHuIL-1alpha pretreatment was mimicked by phorbol myristate acetate. CONCLUSION: Human chondrocytes express both P1 and P2 purine receptor subtypes. The function of the P1 receptor subtype is not yet known, but stimulation of the P2Y2 receptor increases IL-1-mediated PGE2 release.  (+info)

A2B adenosine and P2Y2 receptors stimulate mitogen-activated protein kinase in human embryonic kidney-293 cells. cross-talk between cyclic AMP and protein kinase c pathways. (2/2286)

Mitogen-activated protein kinase (MAPK) cascades underlie long-term mitogenic, morphogenic, and secretory activities of purinergic receptors. In HEK-293 cells, N-ethylcarboxamidoadenosine (NECA) activates endogenous A2BARs that signal through Gs and Gq/11. UTP activates P2Y2 receptors and signals only through Gq/11. The MAPK isoforms, extracellular-signal regulated kinase 1/2 (ERK), are activated by NECA and UTP. H-89 blocks ERK activation by forskolin, but weakly affects the response to NECA or UTP. ERK activation by NECA or UTP is unaffected by a tyrosine kinase inhibitor (genistein), attenuated by a phospholipase C inhibitor (U73122), and is abolished by a MEK inhibitor (PD098059) or dominant negative Ras. Inhibition of protein kinase C (PKC) by GF 109203X failed to block ERK activation by NECA or UTP, however, another PKC inhibitor, Ro 31-8220, which unlike GF 109203X, can block the zeta-isoform, and prevents UTP- but not NECA-induced ERK activation. In the presence of forskolin, Ro 31-8220 loses its ability to block UTP-stimulated ERK activation. PKA has opposing effects on B-Raf and c-Raf-1, both of which are found in HEK-293 cells. The data are explained by a model in which ERK activity is modulated by differential effects of PKC zeta and PKA on Raf isoforms.  (+info)

Selective expression of purinoceptor cP2Y1 suggests a role for nucleotide signalling in development of the chick embryo. (3/2286)

Responses to extracellular nucleotides (e.g., ATP, ADP, etc.) have been demonstrated in a number of embryonic cell types suggesting they may be important signalling molecules during embryonic development. Here the authors describe for the first time the expression of a G-protein-coupled receptor for extracellular ATP, chick P2Y1 (cP2Y1), during embryonic development of the chick. During the first 10 days of embryonic development, cP2Y1 is expressed in a developmentally regulated manner in the limb buds, mesonephros, brain, somites, and facial primordia, suggesting that this receptor may have a role in the development of each of these systems.  (+info)

Hetero-oligomeric assembly of P2X receptor subunits. Specificities exist with regard to possible partners. (4/2286)

P2X receptors are a distinct family of ligand-gated ion channels activated by extracellular ATP. Each of the seven identified subunit proteins (P2X1 through P2X7) has been reported to form functional homo-oligomeric channels when expressed in heterologous systems. Functional studies of native receptors, together with patterns of subunit gene expression, suggest that hetero-oligomeric assembly among members of this family may also occur. This prediction is supported by reports describing hetero-oligomeric assembly for three different recombinant subunit combinations. In this report, we systematically examined the ability of all members of the P2X receptor family to interact using a co-immunoprecipitation assay. The seven P2X receptor subunits were differentially epitope-tagged and expressed in various combinations in human embryonic kidney 293 cells. It was found that six of the seven subunits formed homo-oligomeric complexes, the exception being P2X6. When co-assembly between pairs of subunits was examined, all were able to form hetero-oligomeric assemblies with the exception of P2X7. Whereas P2X1, P2X2, P2X5, and P2X6 were able to assemble with most subunits, P2X3 and P2X4 presented a more restricted pattern of co-association. These results suggest that hetero-oligomeric assembly might underlie functional discrepancies observed between P2X responses seen in the native and recombinant settings, while providing for an increased diversity of signaling by ATP.  (+info)

Confocal calcium imaging reveals an ionotropic P2 nucleotide receptor in the paranodal membrane of rat Schwann cells. (5/2286)

1. The paranodal Schwann cell region is of major importance for the function of a myelinated axon. In the present study we searched for a possible ionotropic effect of extracellular ATP in this Schwann cell compartment. 2. Whole-cell patch-clamp recordings from cultured rat Schwann cells revealed that ATP and 2'-3'-O-(4-benzoylbenzoyl)-adenosine 5'-triphosphate (BzATP) induced a non-specific cation current. The effect of ATP was much enhanced in a Ca2+- and Mg2+-free solution. ADP, UTP and alpha,beta-methylene adenosine 5'-triphosphate (alpha,beta-meATP) had no effect. 3. Confocal Ca2+ imaging of myelinating Schwann cells in isolated rat spinal roots showed a BzATP-induced rise in the free intracellular Ca2+ concentration in the paranodal Schwann cell cytoplasm whereas alpha,beta-meATP and 2-(methylthio)-adenosine 5'-triphosphate were without effect. In contrast to the known metabotropic effect of UTP on these Schwann cell regions, the BzATP-induced Ca2+ signal was not transient, was unaffected by depletion of intracellular Ca2+ stores and dependent on the presence of extracellular Ca2+. 4. These results suggest that an ionotropic ATP receptor with electrophysiological and pharmacological characteristics of the P2X7 subtype of nucleotide receptors is functionally active in myelinating Schwann cells of peripheral nerves. Such a receptor might contribute to Schwann cell reactions in nerve injury or neuropathy.  (+info)

P2 purinoceptor saturation by adenosine triphosphate impairs renal autoregulation in dogs. (6/2286)

Recent studies have suggested a role for P2 purinoceptors on vascular smooth muscle cells in the mechanism of renal autoregulation. Experiments were performed in anesthetized dogs (n = 9) to examine renal blood flow (RBF) autoregulatory efficiency before and after saturation of P2 purinoceptors with acute intra-arterial administration of ATP (1 mg/kg per min). Dogs were pretreated with the nitric oxide synthase inhibitor nitro-L-arginine (NLA) (50 microg/kg per min), to avoid endothelial P2 receptor-mediated effects on nitric oxide release caused by the intra-arterial ATP infusions. NLA treatment decreased RBF (5.3+/-0.3 to 3.6+/-0.2 ml/min per g) and sodium excretion (3.6+/-0.4 to 0.9+/-0.2 ml/min per g) without producing significant changes in GFR (0.92+/-0.04 to 0.90+/-0.06 ml/min per g) or RBF autoregulatory efficiency. ATP administration to NLA-treated dogs resulted in further decreases in RBF (2.8+/-0.2 ml/min per g), GFR (0.58+/-0.05 ml/min per g), and sodium excretion (0.6+/-0.2 micromol/min per g). In addition, there was marked impairment of RBF autoregulatory efficiency during ATP infusion. The slopes of the arterial pressure-blood flow relationships at renal arterial pressures of >75 mmHg were significantly altered, from 0.003+/-0.001 to 0.2+/-0.002 ml/min per g per mmHg. Discontinuation of ATP infusion restored RBF autoregulatory efficiency. Norepinephrine (5 microg/kg per min) administration in these NLA-treated dogs decreased RBF (2.5+/-0.3 ml/min per g; n = 4) to a similar extent, compared with ATP, but did not impair RBF autoregulation. These results support the hypothesis that P2 purinoceptors may be involved in mediating autoregulatory adjustments in renal vascular resistance.  (+info)

Ecto-ATPase activity of alpha-sarcoglycan (adhalin). (7/2286)

alpha-Sarcoglycan is a component of the sarcoglycan complex of dystrophin-associated proteins. Mutations of any of the sarcoglycan genes cause specific forms of muscular dystrophies, collectively termed sarcoglycanopathies. Importantly, a deficiency of any specific sarcoglycan affects the expression of the others. Thus, it appears that the lack of sarcoglycans deprives the muscle cell of an essential, yet unknown function. In the present study, we provide evidence for an ecto-ATPase activity of alpha-sarcoglycan. alpha-Sarcoglycan binds ATP in a Mg2+-dependent and Ca2+-independent manner. The binding is inhibited by 3'-O-(4-benzoyl)benzoyl ATP and ADP. Sequence analysis reveals the existence of a consensus site for nucleotide binding in the extracellular domain of the protein. An antibody against this sequence inhibits the binding of ATP. A dystrophin.dystrophin-associated protein preparation demonstrates a Mg-ATPase activity that is inhibited by the antibody but not by inhibitors of endo-ATPases. In addition, we demonstrate the presence in the sarcolemmal membrane of a P2X-type purinergic receptor. These data suggest that alpha-sarcoglycan may modulate the activity of P2X receptors by buffering the extracellular ATP concentration. The absence of alpha-sarcoglycan in sarcoglycanopathies leaves elevated the concentration of extracellular ATP and the persistent activation of P2X receptors, leading to intracellular Ca2+ overload and muscle fiber death.  (+info)

Cell type-specific ATP-activated responses in rat dorsal root ganglion neurons. (8/2286)

1. The aim of our study is to clarify the relationship between expression pattern of P2X receptors and the cell type of male adult rat (Wistar) dorsal root ganglion (DRG) neurons. We identified the nociceptive cells of acutely dissociated DRG neurons from adult rats type using capsaicin sensitivity. 2. Two types of ATP-activated currents, one with fast, the other with slow desensitization, were found under voltage-clamp conditions. In addition, cells with fast but not slow desensitization responded to capsaicin, indicating that there was a relationship between current kinetics and capsaicin-sensitivity. 3. Both types of neurons were responsive to ATP and alpha, beta methylene-ATP (alpha,betameATP). The concentration of alpha,(beta)meATP producing half-maximal activation (EC50) of neurons with fast desensitization was less (11 microM) than that of neurons with slow desensitization (63 microM), while the Hill coefficients were similar. Suramin and pyridoxal-phosphate-6-azophenyl-2',4'-disulphonic acid tetrasodium (PPADS) antagonized alpha,betameATP-induced currents in both types of neurons. 4. In situ hybridization revealed that small cells of the DRG predominantly expressed mRNAs of P2X3 and medium-sized cells expressed mRNAs of P2X2 and P2X3. In contrast, both of mRNAs were not detected in large cells of the DRG. 5. These results suggest that capsaicin-sensitive, small-sized DRG neurons expressed mainly the homomeric P2X3 subunit and that capsaicin-insensitive, medium-sized DRG neurons expressed the heteromultimeric receptor with P2X2 and P2X3.  (+info)

Purinergic P2 receptors are a type of cell surface receptor that bind to purine nucleotides and nucleosides, such as ATP (adenosine triphosphate) and ADP (adenosine diphosphate), and mediate various physiological responses. These receptors are divided into two main families: P2X and P2Y.

P2X receptors are ionotropic receptors, meaning they form ion channels that allow the flow of ions across the cell membrane upon activation. There are seven subtypes of P2X receptors (P2X1-7), each with distinct functional and pharmacological properties.

P2Y receptors, on the other hand, are metabotropic receptors, meaning they activate intracellular signaling pathways through G proteins. There are eight subtypes of P2Y receptors (P2Y1, P2Y2, P2Y4, P2Y6, P2Y11, P2Y12, P2Y13, and P2Y14), each with different G protein coupling specificities and downstream signaling pathways.

Purinergic P2 receptors are widely expressed in various tissues, including the nervous system, cardiovascular system, respiratory system, gastrointestinal tract, and immune system. They play important roles in regulating physiological functions such as neurotransmission, vasodilation, platelet aggregation, smooth muscle contraction, and inflammation. Dysregulation of purinergic P2 receptors has been implicated in various pathological conditions, including pain, ischemia, hypertension, atherosclerosis, and cancer.

Purinergic P2X7 receptors are a type of ligand-gated ion channel that are activated by the binding of extracellular adenosine triphosphate (ATP) to the P2X7 receptor subunit. These receptors play important roles in various physiological and pathophysiological processes, including inflammation, immune response, pain perception, and cell death.

Upon activation of P2X7 receptors, there is an increase in membrane permeability to small cations such as Na+, K+, and Ca2+, which can lead to the depolarization of the cell membrane. Prolonged activation of these receptors can result in the formation of large pores that allow for the passage of larger molecules, including inflammatory mediators and even small proteins. This can ultimately lead to the induction of apoptosis or necrosis in certain cells.

P2X7 receptors are widely expressed in various tissues, including the brain, spinal cord, immune cells, and epithelial cells. In recent years, there has been growing interest in targeting P2X7 receptors for therapeutic purposes, particularly in the context of inflammatory diseases and chronic pain.

Purinergic P2X receptor antagonists are pharmaceutical agents that block the activation of P2X receptors, which are ligand-gated ion channels found in the cell membranes of various cell types, including excitable cells such as neurons and muscle cells. These receptors are activated by extracellular adenosine triphosphate (ATP) and play important roles in a variety of physiological processes, including neurotransmission, pain perception, and inflammation.

P2X receptor antagonists work by binding to the receptor and preventing ATP from activating it, thereby blocking its downstream effects. These drugs have potential therapeutic uses in various medical conditions, such as chronic pain, urinary incontinence, and ischemia-reperfusion injury. However, their development and use are still in the early stages of research, and more studies are needed to fully understand their mechanisms of action and safety profiles.

Purinergic P2X receptors are a type of ionotropic receptor, which are ligand-gated ion channels that open to allow ions to flow across the cell membrane in response to the binding of a neurotransmitter or other signaling molecule. Specifically, purinergic P2X receptors are activated by extracellular adenosine triphosphate (ATP) and related nucleotides.

Agonists of purinergic P2X receptors are substances that bind to and activate these receptors, causing them to open and allow ions to flow through. Examples of natural agonists of purinergic P2X receptors include ATP, adenosine diphosphate (ADP), and uridine triphosphate (UTP). There are also synthetic agonists that have been developed for research purposes, such as α,β-methylene ATP and benzoylbenzoyl ATP.

Agonists of purinergic P2X receptors have a variety of effects on different cell types, depending on the specific receptor subtype that is activated. For example, activation of P2X1 receptors on smooth muscle cells can cause contraction, while activation of P2X7 receptors on immune cells can trigger the release of pro-inflammatory cytokines.

Understanding the effects of purinergic P2X receptor agonists is important for a variety of research areas, including neuroscience, immunology, and cardiovascular biology. It may also have implications for the development of new therapeutic strategies for various diseases.

Purinergic P2X receptors are a type of ligand-gated ion channel that are activated by the binding of extracellular ATP (adenosine triphosphate) and other purinergic agonists. These receptors play important roles in various physiological processes, including neurotransmission, pain perception, and immune response.

P2X receptors are composed of three subunits that form a functional ion channel. There are seven different subunits (P2X1-7) that can assemble to form homo- or heterotrimeric receptor complexes with distinct functional properties.

Upon activation by ATP, P2X receptors undergo conformational changes that allow for the flow of cations, such as calcium (Ca^2+^), sodium (Na^+^), and potassium (K^+^) ions, across the cell membrane. This ion flux can lead to a variety of downstream signaling events, including the activation of second messenger systems and changes in gene expression.

Purinergic P2X receptors have been implicated in a number of pathological conditions, including chronic pain, inflammation, and neurodegenerative diseases. As such, they are an active area of research for the development of novel therapeutic strategies.

Purinergic P2X3 receptors are a type of ligand-gated ion channel that are activated by the binding of adenosine triphosphate (ATP) and related nucleotides. These receptors are primarily expressed on sensory neurons, including nociceptive neurons that detect and transmit pain signals.

P2X3 receptors are homomeric or heteromeric complexes composed of P2X3 subunits, which form a functional ion channel upon activation by ATP. These receptors play an important role in the transmission of nociceptive information from the periphery to the central nervous system.

Activation of P2X3 receptors leads to the opening of the ion channel and the influx of cations, such as calcium and sodium ions, into the neuron. This depolarizes the membrane and can trigger action potentials that transmit pain signals to the brain.

P2X3 receptors have been implicated in various pain conditions, including inflammatory pain, neuropathic pain, and cancer-related pain. As a result, P2X3 receptor antagonists are being investigated as potential therapeutic agents for the treatment of chronic pain.

Purinergic P2Y2 receptors are a type of G-protein coupled receptor (GPCR) that bind to and are activated by extracellular nucleotides, such as ATP and UTP. These receptors play a role in various physiological processes, including regulation of inflammation, smooth muscle contraction, and wound healing.

P2Y2 receptors are widely expressed in various tissues, including the respiratory, gastrointestinal, and urinary tracts, as well as the skin and central nervous system. They have been shown to play a role in the pathophysiology of several diseases, such as cystic fibrosis, asthma, and cancer.

Activation of P2Y2 receptors leads to a variety of cellular responses, including increased intracellular calcium levels, activation of protein kinases, and regulation of gene expression. These downstream signaling events can ultimately lead to changes in cell behavior, such as increased proliferation, migration, or secretion of cytokines and other mediators.

In summary, Purinergic P2Y2 receptors are a type of GPCR that bind to extracellular nucleotides and play a role in various physiological processes and diseases. Activation of these receptors leads to downstream signaling events that can ultimately affect cell behavior.

Purinergic P2X4 receptors are a type of ionotropic purinergic receptor that are activated by adenosine triphosphate (ATP) and related nucleotides. They belong to the P2X receptor family, which includes seven subtypes (P2X1-7) that form trimeric channels permeable to cations such as calcium, sodium, and potassium.

The P2X4 receptor is widely expressed in various tissues, including the central and peripheral nervous systems, immune cells, and epithelial cells. It plays a role in several physiological processes, including neurotransmission, inflammation, and pain perception. Activation of P2X4 receptors leads to an increase in intracellular calcium concentration and membrane depolarization, which can modulate synaptic transmission and cell excitability.

P2X4 receptors have also been implicated in various pathological conditions, such as neuropathic pain, neuroinflammation, and ischemic injury. They are involved in the release of pro-inflammatory cytokines and chemokines from immune cells, contributing to the development of chronic inflammation and tissue damage.

In summary, purinergic P2X4 receptors are a type of ATP-gated ion channel that play important roles in physiological and pathological processes, including neurotransmission, inflammation, and pain perception.

Purinergic P2Y1 receptors are a type of G-protein coupled receptor (GPCR) that bind to purine nucleotides, such as adenosine triphosphate (ATP) and adenosine diphosphate (ADP). These receptors play a role in various physiological processes, including platelet activation, smooth muscle contraction, and neurotransmission.

The P2Y1 receptor, in particular, is activated by ADP and has been shown to be involved in platelet aggregation, vascular smooth muscle contraction, and neuronal excitability. It signals through the Gq/11 family of G proteins, leading to the activation of phospholipase C-β (PLC-β) and the production of inositol trisphosphate (IP3) and diacylglycerol (DAG), which ultimately result in calcium mobilization and protein kinase C (PKC) activation.

In a medical context, P2Y1 receptors have been implicated in various pathological conditions, including thrombosis, hypertension, and neurodegenerative disorders. Therefore, drugs that target these receptors may have therapeutic potential for the treatment of these conditions.

Purinergic P2 receptor antagonists are pharmaceutical agents that block the activity of P2 receptors, which are a type of cell surface receptor that binds extracellular nucleotides such as ATP and ADP. These receptors play important roles in various physiological processes, including neurotransmission, inflammation, and platelet aggregation.

P2 receptors are divided into two main subfamilies: P2X and P2Y. The P2X receptors are ligand-gated ion channels that allow the flow of ions across the cell membrane upon activation, while the P2Y receptors are G protein-coupled receptors that activate intracellular signaling pathways.

Purinergic P2 receptor antagonists are used in clinical medicine to treat various conditions, such as chronic pain, urinary incontinence, and cardiovascular diseases. For example, the P2X3 receptor antagonist gefapixant is being investigated for the treatment of refractory chronic cough, while the P2Y12 receptor antagonists clopidogrel and ticagrelor are used to prevent thrombosis in patients with acute coronary syndrome.

Overall, purinergic P2 receptor antagonists offer a promising therapeutic approach for various diseases by targeting specific receptors involved in pathological processes.

Purinergic P2Y receptor agonists are substances that bind and activate purinergic P2Y receptors, which are a type of G-protein coupled receptors found on the cell membrane. These receptors are activated by extracellular nucleotides such as ATP (adenosine triphosphate), ADP (adenosine diphosphate), UTP (uridine triphosphate) and UDP (uridine diphosphate).

When a purinergic P2Y receptor agonist binds to the receptor, it triggers a series of intracellular signaling events that can lead to various cellular responses, such as modulation of neurotransmission, regulation of vascular tone, and activation of immune cells.

Purinergic P2Y receptor agonists have potential therapeutic applications in several medical conditions, including cardiovascular diseases, inflammatory disorders, and neurological disorders. However, the use of these agents must be carefully monitored due to their potential to cause adverse effects, such as vasoconstriction, platelet aggregation, and inflammation.

Purinergic receptors are a type of cell surface receptor that bind and respond to purines and pyrimidines, which are nucleotides and nucleosides. These receptors are involved in various physiological processes, including neurotransmission, muscle contraction, and inflammation. There are two main types of purinergic receptors: P1 receptors, which are activated by adenosine, and P2 receptors, which are activated by ATP and other nucleotides.

P2 receptors are further divided into two subtypes: P2X and P2Y. P2X receptors are ionotropic receptors that form cation channels upon activation, allowing the flow of ions such as calcium and sodium into the cell. P2Y receptors, on the other hand, are metabotropic receptors that activate G proteins upon activation, leading to the activation or inhibition of various intracellular signaling pathways.

Purinergic receptors have been found to play a role in many diseases and conditions, including neurological disorders, cardiovascular disease, and cancer. They are also being studied as potential targets for drug development.

Purinergic P2Y receptors are a subtype of purinergic receptors that are activated by nucleotides, such as ATP (adenosine triphosphate), ADP (adenosine diphosphate), UTP (uridine triphosphate), and UDP (uridine diphosphate). These receptors are G protein-coupled receptors, which means they transmit signals through heterotrimeric G proteins.

There are eight subtypes of P2Y receptors, named P2Y1, P2Y2, P2Y4, P2Y6, P2Y11, P2Y12, P2Y13, and P2Y14. Each subtype has a different preference for the type of nucleotide that activates it, as well as distinct downstream signaling pathways.

P2Y receptors play important roles in various physiological processes, including platelet aggregation, smooth muscle contraction and relaxation, neurotransmission, inflammation, and cell proliferation and differentiation. In the medical field, P2Y receptors have been implicated in several diseases, such as thrombosis, hypertension, chronic pain, and cancer, making them potential targets for drug development.

Purinergic P2 receptor agonists are substances that bind and activate purinergic P2 receptors, which are a type of cell surface receptor found in many tissues throughout the body. These receptors are activated by extracellular nucleotides, such as ATP (adenosine triphosphate) and ADP (adenosine diphosphate), and play important roles in various physiological processes, including neurotransmission, muscle contraction, and inflammation.

P2 receptors are divided into two main subfamilies: P2X and P2Y. P2X receptors are ligand-gated ion channels that allow the flow of ions across the cell membrane when activated, while P2Y receptors are G protein-coupled receptors that activate intracellular signaling pathways.

Purinergic P2 receptor agonists can be synthetic or naturally occurring compounds that selectively bind to and activate specific subtypes of P2 receptors. They have potential therapeutic applications in various medical conditions, such as pain management, cardiovascular diseases, and neurological disorders. However, their use must be carefully monitored due to the potential for adverse effects, including desensitization of receptors and activation of unwanted signaling pathways.

Purinergic P2X2 receptors are a type of ionotropic receptor, which are ligand-gated ion channels that open to allow the flow of ions across the cell membrane in response to the binding of a specific molecule (ligand). In the case of P2X2 receptors, the ligands are ATP and other purinergic agonists.

P2X2 receptors are composed of three subunits that assemble to form a functional ion channel. When ATP binds to the extracellular domain of the receptor, it triggers a conformational change that opens the channel, allowing cations such as calcium (Ca²+), sodium (Na⁺) and potassium (K⁺) to flow into the cell.

P2X2 receptors are widely expressed in both the peripheral and central nervous systems, where they play important roles in various physiological processes, including neurotransmission, pain perception, and vasoconstriction. They have also been implicated in several pathological conditions, such as chronic pain, epilepsy, and bladder dysfunction.

P2X2 receptors are of particular interest in pharmacology due to their potential as targets for drug development. For example, P2X2 receptor antagonists have been shown to be effective in reducing pain hypersensitivity in animal models of chronic pain.

Purinergic antagonists are a class of drugs that block the action of purinergic receptors, which are specialized proteins found on the surface of cells that respond to purines such as ATP and ADP. These receptors play important roles in various physiological processes, including neurotransmission, inflammation, and cell death.

Purinergic antagonists work by binding to these receptors and preventing them from being activated by purines. This can have a variety of effects depending on the specific receptor that is blocked. For example, some purinergic antagonists are used in the treatment of conditions such as chronic pain, depression, and Parkinson's disease because they block receptors that play a role in these conditions.

It's important to note that while purinergic antagonists can be useful therapeutically, they can also have side effects and potential risks. As with any medication, it's important to use them only under the guidance of a healthcare professional.

Purinergic agonists are substances that bind to and activate purinergic receptors, which are a type of cell surface receptor found in many tissues throughout the body. These receptors are activated by endogenous molecules called purines, including adenosine triphosphate (ATP) and uridine triphosphate (UTP), as well as their breakdown products such as adenosine.

Purinergic agonists can have a variety of effects on different tissues, depending on the type of purinergic receptor that they activate. For example, ATP acting as a purinergic agonist can cause smooth muscle contraction, increase heart rate and blood pressure, and modulate neurotransmission in the brain.

Purinergic agonists are used in research to study the functions of purinergic receptors and their roles in various physiological processes. They also have potential therapeutic applications, such as in the treatment of cardiovascular diseases, pain, and neurological disorders. However, it is important to note that the use of purinergic agonists as drugs must be carefully studied and regulated due to their potential for adverse effects.

Adenosine Triphosphate (ATP) is a high-energy molecule that stores and transports energy within cells. It is the main source of energy for most cellular processes, including muscle contraction, nerve impulse transmission, and protein synthesis. ATP is composed of a base (adenine), a sugar (ribose), and three phosphate groups. The bonds between these phosphate groups contain a significant amount of energy, which can be released when the bond between the second and third phosphate group is broken, resulting in the formation of adenosine diphosphate (ADP) and inorganic phosphate. This process is known as hydrolysis and can be catalyzed by various enzymes to drive a wide range of cellular functions. ATP can also be regenerated from ADP through various metabolic pathways, such as oxidative phosphorylation or substrate-level phosphorylation, allowing for the continuous supply of energy to cells.

Purinergic P2Y12 receptors are a type of G protein-coupled receptor that bind to and are activated by adenosine diphosphate (ADP). These receptors play an important role in regulating platelet activation and aggregation, which is crucial for the normal hemostatic response to vascular injury.

The P2Y12 receptor is a key component of the platelet signaling pathway that leads to the activation of integrin αIIbβ3, which mediates platelet aggregation. Inhibition of the P2Y12 receptor with drugs such as clopidogrel or ticagrelor is a standard treatment for preventing thrombosis in patients at risk of arterial occlusion, such as those with acute coronary syndrome or following percutaneous coronary intervention.

P2Y12 receptors are also expressed on other cell types, including immune cells and neurons, where they play roles in inflammation, neurotransmission, and other physiological processes.

Purinergic P2X5 receptors are a type of ionotropic purinergic receptor that are activated by adenosine triphosphate (ATP) and related nucleotides. They belong to the P2X receptor family, which includes seven subtypes (P2X1-7) that form trimeric channels permeable to cations such as calcium, sodium, and potassium.

The P2X5 receptor is composed of three identical subunits that contain two transmembrane domains, an intracellular N-terminus, and a large extracellular loop with conserved amino acid residues involved in ATP binding. The activation of P2X5 receptors leads to the opening of the ion channel, resulting in membrane depolarization and the initiation of downstream signaling pathways.

P2X5 receptors are widely expressed in various tissues, including the nervous system, immune system, and cardiovascular system. In the nervous system, they play important roles in pain sensation, neuroinflammation, and synaptic plasticity. In the immune system, P2X5 receptors regulate the activation and migration of immune cells, such as macrophages and dendritic cells. In the cardiovascular system, they contribute to the regulation of vascular tone and blood pressure.

Dysregulation of P2X5 receptor function has been implicated in various pathological conditions, including chronic pain, neurodegenerative diseases, and inflammatory disorders. Therefore, targeting P2X5 receptors represents a promising therapeutic strategy for the treatment of these conditions.

Purinergic P2X1 receptors are a type of ligand-gated ion channel that is activated by the binding of ATP (adenosine triphosphate), a purine nucleotide. These receptors are permeable to cations such as calcium, sodium, and potassium ions. P2X1 receptors are widely expressed in various tissues, including the cardiovascular system, nervous system, and urinary system. They play a role in several physiological processes, including neurotransmission, smooth muscle contraction, and platelet aggregation.

P2X1 receptors are composed of three subunits that form a homotrimeric complex. Upon activation by ATP, the channel opens, allowing cations to flow through the membrane. This ion flux can trigger various intracellular signaling pathways and modulate cellular functions.

In summary, Purinergic P2X1 receptors are a type of ATP-activated ion channel that play important roles in several physiological processes and are widely expressed in various tissues throughout the body.

Uridine Triphosphate (UTP) is a nucleotide that plays a crucial role in the synthesis and repair of DNA and RNA. It consists of a nitrogenous base called uracil, a pentose sugar (ribose), and three phosphate groups. UTP is one of the four triphosphates used in the biosynthesis of RNA during transcription, where it donates its uracil base to the growing RNA chain. Additionally, UTP serves as an energy source and a substrate in various biochemical reactions within the cell, including phosphorylation processes and the synthesis of glycogen and other molecules.

Suramin is a medication that has been used for the treatment of African sleeping sickness, which is caused by trypanosomes. It works as a reverse-specific protein kinase CK inhibitor and also blocks the attachment of the parasite to the host cells. Suramin is not absorbed well from the gastrointestinal tract and is administered intravenously.

It should be noted that Suramin is an experimental treatment for other conditions such as cancer, neurodegenerative diseases, viral infections and autoimmune diseases, but it's still under investigation and has not been approved by FDA for those uses.

Pyridoxal phosphate (PLP) is the active form of vitamin B6 and functions as a cofactor in various enzymatic reactions in the human body. It plays a crucial role in the metabolism of amino acids, carbohydrates, lipids, and neurotransmitters. Pyridoxal phosphate is involved in more than 140 different enzyme-catalyzed reactions, making it one of the most versatile cofactors in human biochemistry.

As a cofactor, pyridoxal phosphate helps enzymes carry out their functions by facilitating chemical transformations in substrates (the molecules on which enzymes act). In particular, PLP is essential for transamination, decarboxylation, racemization, and elimination reactions involving amino acids. These processes are vital for the synthesis and degradation of amino acids, neurotransmitters, hemoglobin, and other crucial molecules in the body.

Pyridoxal phosphate is formed from the conversion of pyridoxal (a form of vitamin B6) by the enzyme pyridoxal kinase, using ATP as a phosphate donor. The human body obtains vitamin B6 through dietary sources such as whole grains, legumes, vegetables, nuts, and animal products like poultry, fish, and pork. It is essential to maintain adequate levels of pyridoxal phosphate for optimal enzymatic function and overall health.

Purinergic P2Y receptor antagonists are a class of pharmaceutical compounds that block the activity of P2Y purinergic receptors, which are a type of G protein-coupled receptor found on the surface of various cells throughout the body. These receptors are activated by extracellular nucleotides such as ATP and ADP, and play important roles in regulating a variety of physiological processes, including inflammation, platelet aggregation, and neurotransmission.

P2Y receptor antagonists are used in the treatment of several medical conditions. For example, they can be used to prevent platelet aggregation and thrombosis in patients with cardiovascular disease or those at risk for stroke. They may also have potential therapeutic applications in the treatment of chronic pain, inflammatory disorders, and neurological conditions such as epilepsy and Parkinson's disease.

Some examples of P2Y receptor antagonists include clopidogrel (Plavix), ticlopidine (Ticlid), and cangrelor (Kengreal), which are used to prevent platelet aggregation and thrombosis, and suramin, a non-selective P2 receptor antagonist that has been investigated for its potential anti-cancer effects.

Calcium is an essential mineral that is vital for various physiological processes in the human body. The medical definition of calcium is as follows:

Calcium (Ca2+) is a crucial cation and the most abundant mineral in the human body, with approximately 99% of it found in bones and teeth. It plays a vital role in maintaining structural integrity, nerve impulse transmission, muscle contraction, hormonal secretion, blood coagulation, and enzyme activation.

Calcium homeostasis is tightly regulated through the interplay of several hormones, including parathyroid hormone (PTH), calcitonin, and vitamin D. Dietary calcium intake, absorption, and excretion are also critical factors in maintaining optimal calcium levels in the body.

Hypocalcemia refers to low serum calcium levels, while hypercalcemia indicates high serum calcium levels. Both conditions can have detrimental effects on various organ systems and require medical intervention to correct.

Calcium signaling is the process by which cells regulate various functions through changes in intracellular calcium ion concentrations. Calcium ions (Ca^2+^) are crucial second messengers that play a critical role in many cellular processes, including muscle contraction, neurotransmitter release, gene expression, and programmed cell death (apoptosis).

Intracellular calcium levels are tightly regulated by a complex network of channels, pumps, and exchangers located on the plasma membrane and intracellular organelles such as the endoplasmic reticulum (ER) and mitochondria. These proteins control the influx, efflux, and storage of calcium ions within the cell.

Calcium signaling is initiated when an external signal, such as a hormone or neurotransmitter, binds to a specific receptor on the plasma membrane. This interaction triggers the opening of ion channels, allowing extracellular Ca^2+^ to flow into the cytoplasm. In some cases, this influx of calcium ions is sufficient to activate downstream targets directly. However, in most instances, the increase in intracellular Ca^2+^ serves as a trigger for the release of additional calcium from internal stores, such as the ER.

The release of calcium from the ER is mediated by ryanodine receptors (RyRs) and inositol trisphosphate receptors (IP3Rs), which are activated by specific second messengers generated in response to the initial external signal. The activation of these channels leads to a rapid increase in cytoplasmic Ca^2+^, creating a transient intracellular calcium signal known as a "calcium spark" or "calcium puff."

These localized increases in calcium concentration can then propagate throughout the cell as waves of elevated calcium, allowing for the spatial and temporal coordination of various cellular responses. The duration and amplitude of these calcium signals are finely tuned by the interplay between calcium-binding proteins, pumps, and exchangers, ensuring that appropriate responses are elicited in a controlled manner.

Dysregulation of intracellular calcium signaling has been implicated in numerous pathological conditions, including neurodegenerative diseases, cardiovascular disorders, and cancer. Therefore, understanding the molecular mechanisms governing calcium homeostasis and signaling is crucial for the development of novel therapeutic strategies targeting these diseases.

Purinergic P1 receptors are a type of G-protein coupled receptor that bind to nucleotides such as adenosine. These receptors are involved in a variety of physiological processes, including modulation of neurotransmitter release, cardiovascular function, and immune response. There are four subtypes of P1 receptors (A1, A2A, A2B, and A3) that have different signaling pathways and functions. Activation of these receptors can lead to a variety of cellular responses, including inhibition or stimulation of adenylyl cyclase activity, changes in intracellular calcium levels, and activation of various protein kinases. They play important roles in the central nervous system, cardiovascular system, respiratory system, gastrointestinal system, and immune system.

Purinergic agents are substances that act on purinergic receptors, which are a type of cell surface receptor found in many organs and tissues throughout the body. These receptors are activated by endogenous molecules called purines, including adenosine triphosphate (ATP) and adenosine diphosphate (ADP), as well as uridine triphosphate (UTP) and other related compounds.

Purinergic agents can be either agonists or antagonists of purinergic receptors. Agonists are molecules that bind to the receptor and activate it, leading to a physiological response. Antagonists, on the other hand, bind to the receptor but do not activate it, instead blocking the ability of agonists to bind and activate the receptor.

Purinergic agents have a wide range of therapeutic applications, including in the treatment of cardiovascular diseases, neurological disorders, inflammatory conditions, and pain management. For example, certain purinergic agonists can be used to induce vasodilation and improve blood flow, while antagonists may be useful in treating conditions such as chronic pain or epilepsy.

It's worth noting that the study of purinergic signaling is a rapidly evolving field, and new insights into the roles of purinergic agents in various physiological processes are being discovered regularly.

Apyrase is an enzyme that catalyzes the hydrolysis of nucleoside triphosphates (like ATP or GTP) to nucleoside diphosphates (like ADP or GDP), releasing inorganic phosphate in the process. It can also hydrolyze nucleoside diphosphates to nucleoside monophosphates, releasing inorganic pyrophosphate.

This enzyme is widely distributed in nature and has been found in various organisms, including bacteria, plants, and animals. In humans, apyrases are present in different tissues, such as the brain, platelets, and red blood cells. They play essential roles in several biological processes, including signal transduction, metabolism regulation, and inflammatory response modulation.

There are two major classes of apyrases: type I (also known as nucleoside diphosphate kinase) and type II (also known as NTPDase). Type II apyrases have higher substrate specificity for nucleoside triphosphates, while type I apyrases can hydrolyze both nucleoside tri- and diphosphates.

In the medical field, apyrases are sometimes used in research to study platelet function or neurotransmission, as they can help regulate purinergic signaling by controlling extracellular levels of ATP and ADP. Additionally, some studies suggest that apyrase activity might be involved in certain pathological conditions, such as atherosclerosis, thrombosis, and neurological disorders.

Adenosine diphosphate (ADP) is a chemical compound that plays a crucial role in energy transfer within cells. It is a nucleotide, which consists of a adenosine molecule (a sugar molecule called ribose attached to a nitrogenous base called adenine) and two phosphate groups.

In the cell, ADP functions as an intermediate in the conversion of energy from one form to another. When a high-energy phosphate bond in ADP is broken, energy is released and ADP is converted to adenosine triphosphate (ATP), which serves as the main energy currency of the cell. Conversely, when ATP donates a phosphate group to another molecule, it is converted back to ADP, releasing energy for the cell to use.

ADP also plays a role in blood clotting and other physiological processes. In the coagulation cascade, ADP released from damaged red blood cells can help activate platelets and initiate the formation of a blood clot.

"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.

Purinergic P1 receptor agonists are substances that bind to and activate purinergic P1 receptors, which are a type of G protein-coupled receptor found in many tissues throughout the body. These receptors are activated by endogenous nucleotides such as adenosine and its metabolites.

Purinergic P1 receptors include four subtypes: A1, A2A, A2B, and A3. Each of these subtypes has distinct signaling pathways and physiological roles. For example, A1 receptor activation can lead to vasodilation, bradycardia, and anti-inflammatory effects, while A2A receptor activation can increase cyclic AMP levels and have anti-inflammatory effects.

Purinergic P1 receptor agonists are used in various therapeutic applications, including as cardiovascular drugs, antiplatelet agents, and anti-inflammatory agents. Some examples of purinergic P1 receptor agonists include adenosine, regadenoson, and dipyridamole.

It's important to note that the use of these substances should be under medical supervision due to their potential side effects and interactions with other medications.

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.

Sprague-Dawley rats are a strain of albino laboratory rats that are widely used in scientific research. They were first developed by researchers H.H. Sprague and R.C. Dawley in the early 20th century, and have since become one of the most commonly used rat strains in biomedical research due to their relatively large size, ease of handling, and consistent genetic background.

Sprague-Dawley rats are outbred, which means that they are genetically diverse and do not suffer from the same limitations as inbred strains, which can have reduced fertility and increased susceptibility to certain diseases. They are also characterized by their docile nature and low levels of aggression, making them easier to handle and study than some other rat strains.

These rats are used in a wide variety of research areas, including toxicology, pharmacology, nutrition, cancer, and behavioral studies. Because they are genetically diverse, Sprague-Dawley rats can be used to model a range of human diseases and conditions, making them an important tool in the development of new drugs and therapies.

Purinergic P1 receptor antagonists are a class of pharmaceutical drugs that block the activity of purinergic P1 receptors, which are a type of G-protein coupled receptor found in many tissues throughout the body. These receptors are activated by extracellular nucleotides such as adenosine and ATP, and play important roles in regulating a variety of physiological processes, including cardiovascular function, neurotransmission, and immune response.

Purinergic P1 receptor antagonists work by binding to these receptors and preventing them from being activated by nucleotides. This can have various therapeutic effects, depending on the specific receptor subtype that is targeted. For example, A1 receptor antagonists have been shown to improve cardiac function in heart failure, while A2A receptor antagonists have potential as anti-inflammatory and neuroprotective agents.

However, it's important to note that the use of purinergic P1 receptor antagonists is still an area of active research, and more studies are needed to fully understand their mechanisms of action and therapeutic potential.

Interleukin-1 beta (IL-1β) is a member of the interleukin-1 cytokine family and is primarily produced by activated macrophages in response to inflammatory stimuli. It is a crucial mediator of the innate immune response and plays a key role in the regulation of various biological processes, including cell proliferation, differentiation, and apoptosis. IL-1β is involved in the pathogenesis of several inflammatory diseases, such as rheumatoid arthritis, inflammatory bowel disease, and atherosclerosis. It exerts its effects by binding to the interleukin-1 receptor, which triggers a signaling cascade that leads to the activation of various transcription factors and the expression of target genes.

Purines are heterocyclic aromatic organic compounds that consist of a pyrimidine ring fused to an imidazole ring. They are fundamental components of nucleotides, which are the building blocks of DNA and RNA. In the body, purines can be synthesized endogenously or obtained through dietary sources such as meat, seafood, and certain vegetables.

Once purines are metabolized, they are broken down into uric acid, which is excreted by the kidneys. Elevated levels of uric acid in the body can lead to the formation of uric acid crystals, resulting in conditions such as gout or kidney stones. Therefore, maintaining a balanced intake of purine-rich foods and ensuring proper kidney function are essential for overall health.

C57BL/6 (C57 Black 6) is an inbred strain of laboratory mouse that is widely used in biomedical research. The term "inbred" refers to a strain of animals where matings have been carried out between siblings or other closely related individuals for many generations, resulting in a population that is highly homozygous at most genetic loci.

The C57BL/6 strain was established in 1920 by crossing a female mouse from the dilute brown (DBA) strain with a male mouse from the black strain. The resulting offspring were then interbred for many generations to create the inbred C57BL/6 strain.

C57BL/6 mice are known for their robust health, longevity, and ease of handling, making them a popular choice for researchers. They have been used in a wide range of biomedical research areas, including studies of cancer, immunology, neuroscience, cardiovascular disease, and metabolism.

One of the most notable features of the C57BL/6 strain is its sensitivity to certain genetic modifications, such as the introduction of mutations that lead to obesity or impaired glucose tolerance. This has made it a valuable tool for studying the genetic basis of complex diseases and traits.

Overall, the C57BL/6 inbred mouse strain is an important model organism in biomedical research, providing a valuable resource for understanding the genetic and molecular mechanisms underlying human health and disease.

Neurons, also known as nerve cells or neurocytes, are specialized cells that constitute the basic unit of the nervous system. They are responsible for receiving, processing, and transmitting information and signals within the body. Neurons have three main parts: the dendrites, the cell body (soma), and the axon. The dendrites receive signals from other neurons or sensory receptors, while the axon transmits these signals to other neurons, muscles, or glands. The junction between two neurons is called a synapse, where neurotransmitters are released to transmit the signal across the gap (synaptic cleft) to the next neuron. Neurons vary in size, shape, and structure depending on their function and location within the nervous system.

"Wistar rats" are a strain of albino rats that are widely used in laboratory research. They were developed at the Wistar Institute in Philadelphia, USA, and were first introduced in 1906. Wistar rats are outbred, which means that they are genetically diverse and do not have a fixed set of genetic characteristics like inbred strains.

Wistar rats are commonly used as animal models in biomedical research because of their size, ease of handling, and relatively low cost. They are used in a wide range of research areas, including toxicology, pharmacology, nutrition, cancer, cardiovascular disease, and behavioral studies. Wistar rats are also used in safety testing of drugs, medical devices, and other products.

Wistar rats are typically larger than many other rat strains, with males weighing between 500-700 grams and females weighing between 250-350 grams. They have a lifespan of approximately 2-3 years. Wistar rats are also known for their docile and friendly nature, making them easy to handle and work with in the laboratory setting.

A "knockout" mouse is a genetically engineered mouse in which one or more genes have been deleted or "knocked out" using molecular biology techniques. This allows researchers to study the function of specific genes and their role in various biological processes, as well as potential associations with human diseases. The mice are generated by introducing targeted DNA modifications into embryonic stem cells, which are then used to create a live animal. Knockout mice have been widely used in biomedical research to investigate gene function, disease mechanisms, and potential therapeutic targets.

Adenosine is a purine nucleoside that is composed of a sugar (ribose) and the base adenine. It plays several important roles in the body, including serving as a precursor for the synthesis of other molecules such as ATP, NAD+, and RNA.

In the medical context, adenosine is perhaps best known for its use as a pharmaceutical agent to treat certain cardiac arrhythmias. When administered intravenously, it can help restore normal sinus rhythm in patients with paroxysmal supraventricular tachycardia (PSVT) by slowing conduction through the atrioventricular node and interrupting the reentry circuit responsible for the arrhythmia.

Adenosine can also be used as a diagnostic tool to help differentiate between narrow-complex tachycardias of supraventricular origin and those that originate from below the ventricles (such as ventricular tachycardia). This is because adenosine will typically terminate PSVT but not affect the rhythm of VT.

It's worth noting that adenosine has a very short half-life, lasting only a few seconds in the bloodstream. This means that its effects are rapidly reversible and generally well-tolerated, although some patients may experience transient symptoms such as flushing, chest pain, or shortness of breath.

A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.

The urinary bladder is a muscular, hollow organ in the pelvis that stores urine before it is released from the body. It expands as it fills with urine and contracts when emptying. The typical adult bladder can hold between 400 to 600 milliliters of urine for about 2-5 hours before the urge to urinate occurs. The wall of the bladder contains several layers, including a mucous membrane, a layer of smooth muscle (detrusor muscle), and an outer fibrous adventitia. The muscles of the bladder neck and urethra remain contracted to prevent leakage of urine during filling, and they relax during voiding to allow the urine to flow out through the urethra.

Electric stimulation, also known as electrical nerve stimulation or neuromuscular electrical stimulation, is a therapeutic treatment that uses low-voltage electrical currents to stimulate nerves and muscles. It is often used to help manage pain, promote healing, and improve muscle strength and mobility. The electrical impulses can be delivered through electrodes placed on the skin or directly implanted into the body.

In a medical context, electric stimulation may be used for various purposes such as:

1. Pain management: Electric stimulation can help to block pain signals from reaching the brain and promote the release of endorphins, which are natural painkillers produced by the body.
2. Muscle rehabilitation: Electric stimulation can help to strengthen muscles that have become weak due to injury, illness, or surgery. It can also help to prevent muscle atrophy and improve range of motion.
3. Wound healing: Electric stimulation can promote tissue growth and help to speed up the healing process in wounds, ulcers, and other types of injuries.
4. Urinary incontinence: Electric stimulation can be used to strengthen the muscles that control urination and reduce symptoms of urinary incontinence.
5. Migraine prevention: Electric stimulation can be used as a preventive treatment for migraines by applying electrical impulses to specific nerves in the head and neck.

It is important to note that electric stimulation should only be administered under the guidance of a qualified healthcare professional, as improper use can cause harm or discomfort.

The vas deferens is a muscular tube that carries sperm from the epididymis to the urethra during ejaculation in males. It is a part of the male reproductive system and is often targeted in surgical procedures like vasectomy, which is a form of permanent birth control.

Thionucleotides are chemical compounds that are analogs of nucleotides, which are the building blocks of DNA and RNA. In thionucleotides, one or more of the oxygen atoms in the nucleotide's chemical structure is replaced by a sulfur atom. This modification can affect the way the thionucleotide interacts with other molecules, including enzymes that work with nucleotides and nucleic acids.

Thionucleotides are sometimes used in research to study the biochemistry of nucleic acids and their interactions with other molecules. They can also be used as inhibitors of certain enzymes, such as reverse transcriptase, which is an important target for HIV/AIDS therapy. However, thionucleotides are not normally found in natural biological systems and are not themselves components of DNA or RNA.

Synaptic transmission is the process by which a neuron communicates with another cell, such as another neuron or a muscle cell, across a junction called a synapse. It involves the release of neurotransmitters from the presynaptic terminal of the neuron, which then cross the synaptic cleft and bind to receptors on the postsynaptic cell, leading to changes in the electrical or chemical properties of the target cell. This process is critical for the transmission of signals within the nervous system and for controlling various physiological functions in the body.

Uridine diphosphate (UDP) is a nucleotide diphosphate that consists of a pyrophosphate group, a ribose sugar, and the nucleobase uracil. It plays a crucial role as a coenzyme in various biosynthetic reactions, including the synthesis of glycogen, proteoglycans, and other polysaccharides. UDP is also involved in the detoxification of bilirubin, an end product of hemoglobin breakdown, by converting it to a water-soluble form that can be excreted through the bile. Additionally, UDP serves as a precursor for the synthesis of other nucleotides and their derivatives.

Carbenoxolone is a synthetic derivative of glycyrrhizin, which is found in the root of the licorice plant. It has been used in the treatment of gastric and duodenal ulcers due to its ability to increase the mucosal resistance and promote healing. Carbenoxolone works by inhibiting the enzyme 11-beta-hydroxysteroid dehydrogenase, which leads to an increase in the levels of cortisol and other steroids in the body. This can have various effects on the body, including anti-inflammatory and immunosuppressive actions.

However, long-term use of carbenoxolone has been associated with serious side effects such as hypertension, hypokalemia (low potassium levels), and edema (fluid retention). Therefore, its use is generally limited to short-term treatment of gastric and duodenal ulcers.

Medical Definition: Carbenoxolone

A synthetic derivative of glycyrrhizin, used in the treatment of gastric and duodenal ulcers due to its ability to increase mucosal resistance and promote healing. It is an inhibitor of 11-beta-hydroxysteroid dehydrogenase, leading to increased levels of cortisol and other steroids in the body, with potential anti-inflammatory and immunosuppressive effects. However, long-term use is associated with serious side effects such as hypertension, hypokalemia, and edema.

5'-Nucleotidase is an enzyme that is found on the outer surface of cell membranes, including those of liver cells and red blood cells. Its primary function is to catalyze the hydrolysis of nucleoside monophosphates, such as adenosine monophosphate (AMP) and guanosine monophosphate (GMP), to their corresponding nucleosides, such as adenosine and guanosine, by removing a phosphate group from the 5' position of the nucleotide.

Abnormal levels of 5'-Nucleotidase in the blood can be indicative of liver or bone disease. For example, elevated levels of this enzyme in the blood may suggest liver damage or injury, such as that caused by hepatitis, cirrhosis, or alcohol abuse. Conversely, low levels of 5'-Nucleotidase may be associated with certain types of anemia, including aplastic anemia and paroxysmal nocturnal hemoglobinuria.

Medical professionals may order a 5'-Nucleotidase test to help diagnose or monitor the progression of these conditions. It is important to note that other factors, such as medication use or muscle damage, can also affect 5'-Nucleotidase levels, so results must be interpreted in conjunction with other clinical findings and diagnostic tests.

**Prazosin** is an antihypertensive drug, which belongs to the class of medications called alpha-blockers. It works by relaxing the muscles in the blood vessels, which helps to lower blood pressure and improve blood flow. Prazosin is primarily used to treat high blood pressure (hypertension), but it may also be used for the management of symptoms related to enlarged prostate (benign prostatic hyperplasia).

In a medical definition context:

Prazosin: A selective α1-adrenergic receptor antagonist, used in the treatment of hypertension and benign prostatic hyperplasia. It acts by blocking the action of norepinephrine on the smooth muscle of blood vessels, resulting in vasodilation and decreased peripheral vascular resistance. This leads to a reduction in blood pressure and an improvement in urinary symptoms associated with an enlarged prostate.

Smooth muscle, also known as involuntary muscle, is a type of muscle that is controlled by the autonomic nervous system and functions without conscious effort. These muscles are found in the walls of hollow organs such as the stomach, intestines, bladder, and blood vessels, as well as in the eyes, skin, and other areas of the body.

Smooth muscle fibers are shorter and narrower than skeletal muscle fibers and do not have striations or sarcomeres, which give skeletal muscle its striped appearance. Smooth muscle is controlled by the autonomic nervous system through the release of neurotransmitters such as acetylcholine and norepinephrine, which bind to receptors on the smooth muscle cells and cause them to contract or relax.

Smooth muscle plays an important role in many physiological processes, including digestion, circulation, respiration, and elimination. It can also contribute to various medical conditions, such as hypertension, gastrointestinal disorders, and genitourinary dysfunction, when it becomes overactive or underactive.

Adenosine A1 receptor is a type of G protein-coupled receptor that binds to the endogenous purine nucleoside adenosine. When activated, it inhibits the production of cyclic AMP (cAMP) in the cell by inhibiting adenylyl cyclase activity. This results in various physiological effects, such as decreased heart rate and reduced force of heart contractions, increased potassium conductance, and decreased calcium currents. The Adenosine A1 receptor is widely distributed throughout the body, including the brain, heart, kidneys, and other organs. It plays a crucial role in various biological processes, including cardiovascular function, neuroprotection, and inflammation.

Adenine nucleotides are molecules that consist of a nitrogenous base called adenine, which is linked to a sugar molecule (ribose in the case of adenosine monophosphate or AMP, and deoxyribose in the case of adenosine diphosphate or ADP and adenosine triphosphate or ATP) and one, two, or three phosphate groups. These molecules play a crucial role in energy transfer and metabolism within cells.

AMP contains one phosphate group, while ADP contains two phosphate groups, and ATP contains three phosphate groups. When a phosphate group is removed from ATP, energy is released, which can be used to power various cellular processes such as muscle contraction, nerve impulse transmission, and protein synthesis. The reverse reaction, in which a phosphate group is added back to ADP or AMP to form ATP, requires energy input and often involves the breakdown of nutrients such as glucose or fatty acids.

In addition to their role in energy metabolism, adenine nucleotides also serve as precursors for other important molecules, including DNA and RNA, coenzymes, and signaling molecules.

Neurotransmitter agents are substances that affect the synthesis, storage, release, uptake, degradation, or reuptake of neurotransmitters, which are chemical messengers that transmit signals across a chemical synapse from one neuron to another. These agents can be either agonists, which mimic the action of a neurotransmitter and bind to its receptor, or antagonists, which block the action of a neurotransmitter by binding to its receptor without activating it. They are used in medicine to treat various neurological and psychiatric disorders, such as depression, anxiety, and Parkinson's disease.

Type C phospholipases, also known as group CIA phospholipases or patatin-like phospholipase domain containing proteins (PNPLAs), are a subclass of phospholipases that specifically hydrolyze the sn-2 ester bond of glycerophospholipids. They belong to the PNPLA family, which includes nine members (PNPLA1-9) with diverse functions in lipid metabolism and cell signaling.

Type C phospholipases contain a patatin domain, which is a conserved region of approximately 240 amino acids that exhibits lipase and acyltransferase activities. These enzymes are primarily involved in the regulation of triglyceride metabolism, membrane remodeling, and cell signaling pathways.

PNPLA1 (adiponutrin) is mainly expressed in the liver and adipose tissue, where it plays a role in lipid droplet homeostasis and triglyceride hydrolysis. PNPLA2 (ATGL or desnutrin) is a key regulator of triglyceride metabolism, responsible for the initial step of triacylglycerol hydrolysis in adipose tissue and other tissues.

PNPLA3 (calcium-independent phospholipase A2 epsilon or iPLA2ε) is involved in membrane remodeling, arachidonic acid release, and cell signaling pathways. Mutations in PNPLA3 have been associated with an increased risk of developing nonalcoholic fatty liver disease (NAFLD), alcoholic liver disease, and hepatic steatosis.

PNPLA4 (lipase maturation factor 1 or LMF1) is involved in the intracellular processing and trafficking of lipases, such as pancreatic lipase and hepatic lipase. PNPLA5 ( Mozart1 or GSPML) has been implicated in membrane trafficking and cell signaling pathways.

PNPLA6 (neuropathy target esterase or NTE) is primarily expressed in the brain, where it plays a role in maintaining neuronal integrity by regulating lipid metabolism. Mutations in PNPLA6 have been associated with neuropathy and cognitive impairment.

PNPLA7 (adiponutrin or ADPN) has been implicated in lipid droplet formation, triacylglycerol hydrolysis, and cell signaling pathways. Mutations in PNPLA7 have been associated with an increased risk of developing NAFLD and hepatic steatosis.

PNPLA8 (diglyceride lipase or DGLα) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA9 (calcium-independent phospholipase A2 gamma or iPLA2γ) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA10 (calcium-independent phospholipase A2 delta or iPLA2δ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA11 (calcium-independent phospholipase A2 epsilon or iPLA2ε) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA12 (calcium-independent phospholipase A2 zeta or iPLA2ζ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA13 (calcium-independent phospholipase A2 eta or iPLA2η) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA14 (calcium-independent phospholipase A2 theta or iPLA2θ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA15 (calcium-independent phospholipase A2 iota or iPLA2ι) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA16 (calcium-independent phospholipase A2 kappa or iPLA2κ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA17 (calcium-independent phospholipase A2 lambda or iPLA2λ) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA18 (calcium-independent phospholipase A2 mu or iPLA2μ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA19 (calcium-independent phospholipase A2 nu or iPLA2ν) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA20 (calcium-independent phospholipase A2 xi or iPLA2ξ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA21 (calcium-independent phospholipase A2 omicron or iPLA2ο) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA22 (calcium-independent phospholipase A2 pi or iPLA2π) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA23 (calcium-independent phospholipase A2 rho or iPLA2ρ) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA24 (calcium-independent phospholipase A2 sigma or iPLA2σ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA25 (calcium-independent phospholipase A2 tau or iPLA2τ) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA26 (calcium-independent phospholipase A2 upsilon or iPLA2υ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA27 (calcium-independent phospholipase A2 phi or iPLA2φ) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA28 (calcium-independent phospholipase A2 chi or iPLA2χ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA29 (calcium-independent phospholipase A2 psi or iPLA2ψ) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA30 (calcium-independent phospholipase A2 omega or iPLA2ω) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA31 (calcium-independent phospholipase A2 pi or iPLA2π) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA32 (calcium-independent phospholipase A2 rho or iPLA2ρ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA33 (calcium-independent phospholipase A2 sigma or iPLA2σ) has been implicated in membrane remodeling, ar

Muscle contraction is the physiological process in which muscle fibers shorten and generate force, leading to movement or stability of a body part. This process involves the sliding filament theory where thick and thin filaments within the sarcomeres (the functional units of muscles) slide past each other, facilitated by the interaction between myosin heads and actin filaments. The energy required for this action is provided by the hydrolysis of adenosine triphosphate (ATP). Muscle contractions can be voluntary or involuntary, and they play a crucial role in various bodily functions such as locomotion, circulation, respiration, and posture maintenance.

Membrane potential is the electrical potential difference across a cell membrane, typically for excitable cells such as nerve and muscle cells. It is the difference in electric charge between the inside and outside of a cell, created by the selective permeability of the cell membrane to different ions. The resting membrane potential of a typical animal cell is around -70 mV, with the interior being negative relative to the exterior. This potential is generated and maintained by the active transport of ions across the membrane, primarily through the action of the sodium-potassium pump. Membrane potentials play a crucial role in many physiological processes, including the transmission of nerve impulses and the contraction of muscle cells.

Nucleotides are the basic structural units of nucleic acids, such as DNA and RNA. They consist of a nitrogenous base (adenine, guanine, cytosine, thymine or uracil), a pentose sugar (ribose in RNA and deoxyribose in DNA) and one to three phosphate groups. Nucleotides are linked together by phosphodiester bonds between the sugar of one nucleotide and the phosphate group of another, forming long chains known as polynucleotides. The sequence of these nucleotides determines the genetic information carried in DNA and RNA, which is essential for the functioning, reproduction and survival of all living organisms.

A hypotonic solution is a type of fluid that has a lower osmotic pressure than another fluid. In the context of medical and physiological terms, it typically refers to a solution that has a lower solute concentration (and therefore lower osmolarity) than the fluids found in the body's cells.

When a hypotonic solution is introduced into the body or comes into contact with body tissues, water molecules tend to move from the area of lower solute concentration (the hypotonic solution) to the area of higher solute concentration (the body's fluids), in an attempt to equalize the osmotic pressure. This movement of water can cause cells to swell and potentially burst if the difference in osmolarity is significant or if the exposure is prolonged.

Hypotonic solutions are sometimes used medically for specific purposes, such as in irrigation solutions or in certain types of intravenous fluids, where careful control of osmotic pressure is required. However, it's important to use them appropriately and under medical supervision to avoid potential adverse effects.

Rosaniline dyes are a type of basic dye that were first synthesized in the late 19th century. They are named after rosaniline, which is a primary chemical used in their production. Rosaniline dyes are characterized by their ability to form complexes with metal ions, which can then bind to proteins and other biological molecules. This property makes them useful as histological stains, which are used to highlight specific structures or features within tissues and cells.

Rosaniline dyes include a range of different chemicals, such as methyl violet, crystal violet, and basic fuchsin. These dyes are often used in combination with other staining techniques to provide contrast and enhance the visibility of specific cellular components. For example, they may be used to stain nuclei, cytoplasm, or other structures within cells, allowing researchers and clinicians to visualize and analyze tissue samples more effectively.

It's worth noting that some rosaniline dyes have been found to have potential health hazards, particularly when used in certain forms or concentrations. Therefore, it's important to follow proper safety protocols when handling these chemicals and to use them only under the guidance of trained professionals.

The extracellular space is the region outside of cells within a tissue or organ, where various biological molecules and ions exist in a fluid medium. This space is filled with extracellular matrix (ECM), which includes proteins like collagen and elastin, glycoproteins, and proteoglycans that provide structural support and biochemical cues to surrounding cells. The ECM also contains various ions, nutrients, waste products, signaling molecules, and growth factors that play crucial roles in cell-cell communication, tissue homeostasis, and regulation of cell behavior. Additionally, the extracellular space includes the interstitial fluid, which is the fluid component of the ECM, and the lymphatic and vascular systems, through which cells exchange nutrients, waste products, and signaling molecules with the rest of the body. Overall, the extracellular space is a complex and dynamic microenvironment that plays essential roles in maintaining tissue structure, function, and homeostasis.

Connexins are a family of proteins that form the structural units of gap junctions, which are specialized channels that allow for the direct exchange of small molecules and ions between adjacent cells. These channels play crucial roles in maintaining tissue homeostasis, coordinating cellular activities, and enabling communication between cells. In humans, there are 21 different connexin genes that encode for these proteins, with each isoform having unique properties and distributions within the body. Mutations in connexin genes have been linked to a variety of human diseases, including hearing loss, skin disorders, and heart conditions.

P is for purinergic, P2 refers to ATP receptors, as opposed to P1 adenosine adenosine receptors. P2X receptors are ATP ... which is accomplished by P2 receptors. Almost every cell type expresses P2 receptors. Purinergic signalling also has a ... P2X receptors are ionotropic receptors while P2Y are GPCR type receptors. P2X receptor family encompasses 7 genes. P2Y family ... Depending on the nature of the receptor they are found to be of two types: P2Y receptors (metabotropic) P2X receptors ( ...
Hechler, B; Gachet, C (1988). "P2 receptors and platelet function". Purinergic Signalling. 27 (2011 September, 7(3)): 293-303. ... Thrombin receptor activating peptide-6 (TRAP-6) activates platelets through the thrombin receptor protease activated receptor-1 ... Activation of the P2Y1 receptor initiates platelet aggregation in response to ADP. The P2Y1 receptor is required for ADP- ... When it is added to saline-diluted whole blood in the test cuvette, it stimulates the ADP receptors on platelets, activating ...
... s modulate P2 purinergic signaling, and P1 receptors. In addition, ectonucleotidases generate extracellular ... Impact of Ectoenzymes on P2 and P1 Receptor Signaling", Advances in Pharmacology, Pharmacology of Purine and Pyrimidine ... Beldi, G; Enjyoji, K; Wu, Y; Miller, L; Banz, Y; Sun, X; Robson, SC (Jan 1, 2008). "The role of purinergic signaling in the ... The contribution of ectonucleotidases in the modulation of purinergic signaling depends on the availability and preference of ...
... is classified as a purinergic P2 receptor (P2Y12) antagonist. Other compounds in the same mechanistic class include ... August 2007). "Rapid and reversible modulation of platelet function in man by a novel P2Y(12) ADP-receptor antagonist, INS50589 ... It is characterized as a reversible, competitive receptor antagonist. The IC50 for antagonism of ADP-induced (P2Y12-mediated) ... modifications to dinucleoside polyphosphates and nucleotides that confer antagonist properties at the platelet P2Y12 receptor ...
Jacob F, Pérez Novo C, Bachert C, Van Crombruggen K (September 2013). "Purinergic signaling in inflammatory cells: P2 receptor ... The purinergic signalling complex of a cell is sometimes referred to as the "purinome". Purinergic receptors, represented by ... Purinergic receptors are specific classes of membrane receptors that mediate various physiological functions such as the ... There are three known distinct classes of purinergic receptors, known as P1, P2X, and P2Y receptors. Cell signalling events ...
"Comparative hydrolysis of P2 receptor agonists by NTPDases 1, 2, 3 and 8". Purinergic Signalling. 1 (2): 193-204. doi:10.1007/ ... NTPDase1 hydrolyzes P2 receptor ligands, namely ATP, ADP, UTP and UDP with similar efficacy. NTPDase1 can therefore affect P2 ... "Impact of ectoenzymes on p2 and p1 receptor signaling". Pharmacology of Purine and Pyrimidine Receptors. Advances in ... Sepúlveda C, Palomo I, Fuentes E (2016). "Role of adenosine A2b receptor overexpression in tumor progression". Life Sciences. ...
There are various types of purinergic receptors, the most common expressed in the Hensen's cells is the P2 subtype. Another ... Purinergic receptors have been found in the cells of the Organ of Corti, which are able to mediate physiological and ... and the purinergic receptors that found in the Hensen's cells are all important in providing a suitable electrical and micro ... loss function of the purinergic receptors expressed in the Hensen's cells in the cochlea may lead to noise-induced hearing loss ...
P2 receptors) or adenosine (P1 receptors). P2 receptors have further been divided into five subclasses: P2X, P2Y, P2Z, P2U, and ... IUPHAR GPCR Database - Adenosine receptors IUPHAR GPCR Database - P2Y receptors Purinergic+Receptors at the U.S. National ... the first purinergic receptor in plants, DORN1, was discovered. There are three known distinct classes of purinergic receptors ... Zemkova, Hana (January 2021). "Special Issue of International Journal of Molecular Sciences (IJMS) "Purinergic P2 Receptors: ...
Indeed, we owe our present understanding of purinergic signaling and the current classification of P2 receptors to Geoff ... Much of our understanding of purinergic signalling and the current classification of purinergic receptors is attributed to the ... Di Virgilio, F. (22 October 2012). "Purines, Purinergic Receptors, and Cancer". Cancer Research. 72 (21): 5441-5447. doi: ... He coined the term "purinergic signalling" in 1972 in a key paper that has since been cited more than 2,000 times by other key ...
IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology. Purinergic+P2+receptors ... P2Y receptors are a family of purinergic G protein-coupled receptors, stimulated by nucleotides such as adenosine triphosphate ... Receptor (biochemistry) Purinergic signalling Membrane protein Receptor theory Abbracchio MP, Burnstock G, Boeynaems JM, ... Human P2Y receptors have the following G protein coupling: The gaps in P2Y receptor numbering is due to that several receptors ...
P2 purinoceptor InterPro: IPR002286 Purinergic receptor P2Y1 (P2RY1) Purinergic receptor P2Y2 (P2RY2) Purinergic receptor P2Y4 ... Succinate receptor 1 (SUCNR1, GPR91) P2 purinoceptor InterPro: IPR002286 Purinergic receptor P2Y12 (P2RY12) Purinergic receptor ... P2RY4) Purinergic receptor P2Y6 (P2RY6) Purinergic receptor P2Y8 (P2RY8) Purinergic receptor P2Y11 (P2RY11) Hydroxycarboxylic ... IPR002188 P2 purinoceptor InterPro: IPR002286 Purinergic receptor P2Y10 (P2RY10, P2Y10) Protease-activated receptor InterPro: ...
... coli P2 laboratory, biosafety-level-2 laboratory P2 receptor, a purinergic and pyrimidinergic cell surface receptor P2, a ... P2, P02, P.2, or P-2 might refer to several subjects: P2 (storage media), a "Professional Plug-in" solid state data storage ... an iconic 1920s racing automobile Prodrive P2, an automobile built by Prodrive Volvo P2 platform, an automobile platform P2 ( ... "P2" (song), a 2020 song by Lil Uzi Vert from the album Eternal Atake P2 (panel building), a design for blocks of flats used in ...
... which can be detected by P2 purinergic receptors, or nerve growth factor, which can be detected by Tropomyosin receptor kinase ... each of which express a distinct repertoire of ion channels and receptors. Their specializations allow the receptors to ... A nociceptor ("pain receptor" from Latin nocere 'to harm or hurt') is a sensory neuron that responds to damaging or potentially ... The specific receptors for these intense stimuli were called nociceptors. In mammals, nociceptors are found in any area of the ...
... receptors, purinergic p2 MeSH D12.776.543.750.725.500 - receptor, notch1 MeSH D12.776.543.750.725.750 - receptor, notch2 MeSH ... receptor, adenosine a3 MeSH D12.776.543.750.100.700.720 - receptors, purinergic p2 MeSH D12.776.543.750.100.800.100 - receptors ... receptor, adenosine a3 MeSH D12.776.543.750.810.720 - receptors, purinergic p2 MeSH D12.776.543.750.850.249 - bacterial ... receptor, par-1 MeSH D12.776.543.750.810.150 - receptors, cyclic amp MeSH D12.776.543.750.810.700 - receptors, purinergic p1 ...
There are two main types of purinergic receptors, P1 binding to adenosine, and P2 binding to ATP or ADP, presenting different ... Therefore, there are four main transmembrane receptor types: G protein coupled receptors (GPCRs), tyrosine kinase receptors ( ... PAR1 and PAR4 receptors), platelet-derived thromboxane A2 (TxA2) (TP receptor) and ADP (P2Y1 and P2Y12 receptors) that is ... Adenosine acts by binding to purinergic receptors and influencing adenylyl cyclase activity and the formation of cAMP and PKA ...
This receptor is a P2Y purinergic receptor for UDP-glucose and other UDP-sugars coupled to G-proteins. It has been implicated ... Müller CE (2003). "P2-pyrimidinergic receptors and their ligands". Curr. Pharm. Des. 8 (26): 2353-2369. doi:10.2174/ ... 2003). "Characterization of the UDP-glucose receptor (re-named here the P2Y14 receptor) adds diversity to the P2Y receptor ... "Entrez Gene: P2RY14 purinergic receptor P2Y, G-protein coupled, 14". Gerard C, Gerard NP (1994). "C5A anaphylatoxin and its ...
It appears to be relatively selective for P2X receptors, having no appreciable activity at α1 adrenergic, muscarinic M2 and M3 ... PPADS (pyridoxalphosphate-6-azophenyl-2',4'-disulfonic acid) is a selective purinergic P2X antagonist. It is able to block ... Lambrecht, G. (1992). "PPADS, a novel functionally selective antagonist of P2 purinoreceptor mediated responses". European ... histamine H1, and adenosine A1 receptors. PPADS tetrasodium salt, Santa Cruz Biotechnology Ziganshin, AU (December 1993). " ...
Histological staining by another research group examined the distribution of purinergic receptor subtypes throughout the RVM. ... All on-cells showed a response to the non-specific P2 agonist uridine triphosphate (UTP). Activation of on cells by ATP was ... Close, L.N. (January 2009). "Purinergic Receptor Immunoreactivity in the Rostral Ventromedial Medulla". Neuroscience. 158 (2): ... NK1 agonism induced hypersensitivity is dependent on 5-HT3 receptors, and modulated by GABAA and NMDA receptors as well. ...
Subsequently, he identified a unique expression of highly ATP-sensitive P2X1/5 receptors in cortical astrocytes and ... Burnstock, Geoffrey; Verkhratsky, Alexei (2012). Purinergic Signalling in the Nervous System. Springer Verlag. p. 715. ISBN 978 ... Kirischuk, S.; Scherer, J.; Kettenmann, H.; Verkhratsky, A. (1995). "Activation of P2-purinoreceptors triggered Ca2'release ... In particular, he discovered functional NMDA receptors in cortical astroglia, and demonstrated their synaptic activation and ...
... purinergic P1 receptor - purinergic P2 receptor - purinergic receptor - pyridine - pyrimidine - pyruvate - pyruvate oxidation ... interleukin receptor - interleukin-1 receptor - interleukin-2 receptor - interleukin-3 - interleukin-3 receptor - intermediate ... G protein-coupled receptor - G3P - GABA - GABA receptor - GABA-A receptor - gag-onc fusion protein - galanin - gamete - gamma- ... IgE receptor - IGF type 1 receptor - IGF type 2 receptor - IgG - IgM - immediate-early protein - immune cell - immune system - ...
The adenosine receptors (or P1 receptors) are a class of purinergic G protein-coupled receptors with adenosine as the ... "Towards a revised nomenclature for P1 and P2 receptors". Trends Pharmacol. Sci. 18 (3): 79-82. doi:10.1016/S0165-6147(96)01038- ... The adenosine A1 receptor has been found to be ubiquitous throughout the entire body. This receptor has an inhibitory function ... Adenosine receptors play a key role in the homeostasis of bone. The A1 receptor has been shown to stimulate osteoclast ...
One study in mice showed that blockade of P2X7 receptors attenuates onset of liver fibrosis. Purinergic receptor P2X receptor ... Gartland A, Buckley KA, Hipskind RA, Bowler WB, Gallagher JA (2003). "P2 receptors in bone--modulation of osteoclast formation ... The P2X7 subunits can form homomeric receptors only with a typical P2X receptor structure. The P2X7 receptor is a ligand-gated ... P2RX7 purinergic receptor P2X, ligand-gated ion channel, 7". Faria RX, Freitas HR, Reis RA (June 2017). "P2X7 receptor large ...
... purinergic receptor P2X, ligand-gated ion channel, 1". North RA (2002). "Molecular physiology of P2X receptors". Physiol ... 2004). "Increased mitogenic and decreased contractile P2 receptors in smooth muscle cells by shear stress in human vessels with ... "A study of P2X1 receptor function in murine megakaryocytes and human platelets reveals synergy with P2Y receptors". Br. J. ... receptor form disulfide bonds and are involved in receptor trafficking to the cell surface". Mol. Pharmacol. 61 (2): 303-11. ...
Stimulation of the dopamine receptors in the area postrema activates these vomiting centers of the brain; this is why nausea is ... The results showed that most responses to ATP are excitatory and that they are mediated by particular P2 purinoceptors found in ... Kodama, N.; Funahashi, M.; Mitoh, Y.; Minagi, S.; Matsuo, R. (2007). "Purinergic modulation of area postrema neuronal ... The high density of dopamine receptors in the area postrema makes it very sensitive to the dopamine-enhancing drugs. ...
... and neurokinin 1 receptor (NK1R), as well as activation of metabotropic glutamate receptors and release of BDNF. Persistent ... The resultant patterning along the neuraxis leads to segmentation of the neuroepithelium into progenitor domains (p0, p1 p2, p3 ... October 2005). "Astrocytic purinergic signaling coordinates synaptic networks". Science. 310 (5745): 113-6. Bibcode:2005Sci... ... and kainate subtypes of ionotropic glutamate receptors follows. It is the activation of these receptors that potentiates the ...
P2×7 purinergic signaling in dilated cardiomyopathy induced by auto-immunity against muscarinic M 2 receptors: Autoantibody ... P2×7 purinergic signaling in dilated cardiomyopathy induced by auto-immunity against muscarinic M 2 receptors: Autoantibody ... P2×7 purinergic signaling in dilated cardiomyopathy induced by auto-immunity against muscarinic M 2 receptors: Autoantibody ... P2×7 purinergic signaling in dilated cardiomyopathy induced by auto-immunity against muscarinic M 2 receptors : Autoantibody ...
P is for purinergic, P2 refers to ATP receptors, as opposed to P1 adenosine adenosine receptors. P2X receptors are ATP ... which is accomplished by P2 receptors. Almost every cell type expresses P2 receptors. Purinergic signalling also has a ... P2X receptors are ionotropic receptors while P2Y are GPCR type receptors. P2X receptor family encompasses 7 genes. P2Y family ... Depending on the nature of the receptor they are found to be of two types: P2Y receptors (metabotropic) P2X receptors ( ...
An increase in cell number was caused by low doses of the nonspecific P2 receptor agonist ATP, the P2Y2 receptor agonist UTP (p ... Purinergic receptors are part of a functional signaling system for proliferation and differentiation of human epidermal ... P2 receptor expression profiles in human vascular smooth muscle and endothelial cells. Wang, L., Karlsson, L., Moses, S., ... NHERF binds to the tail of the purinergic P2Y1 receptor, a seven-transmembrane receptor with an intracellular C-terminal tail ...
Vasoconstriction and Purinergic P2 Receptors , ResearchGate, the professional network for scientists. ... The effect of purinergic P2 receptor blockade on skeletal muscle exercise hyperemia in miniature swine ... as the sensitivity or expression of channels and receptors (i.e., ASICs channels, TRPv1, P2 and COX-2 receptors) (Antunes- ... ATP could play an important role in skeletal muscle blood flow regulation by inducing vasodilation via purinergic P2 receptors ...
Calbiochem A P₂-purinergic receptor agonist that acts as a potent insulin secretagogue. - Find MSDS or SDS, a COA, data sheets ... Primary Target: A P2-purinergic receptor agonist 119134. Purchase on Sigma-Aldrich Prices are subject to change without notice ... A P₂-purinergic receptor agonist that acts as a potent insulin secretagogue.. More,, A P₂-purinergic receptor agonist that acts ... A P2-purinergic receptor agonist that acts as a potent insulin secretagogue. Substrate and inhibitor of ADP-dependent enzyme ...
Erratum: Comparative hrydrolysis of P2 receptor agonists by NTPDases 1, 2, 3 and 8. (Purinergic Sign Purinergic Signalling, 1 3 ... Comparative hydrolysis of P2 receptor agonists by NTPDases 1, 2, 3 and 8. Purinergic signalling, 1 2, 193-204 ... Comparative hydrolysis of P2 receptor agonists by NTPDases 1, 2, 3 and 8 Purinergic Signalling, 1 2, 193-204 ... Comparative hydrolysis of P2 receptor agonists by NTPDases 1, 2, 3 and 8 Purinergic Signalling, 1 , 193-204 ...
Peptide-induced keratinocyte migration was mediated by purinergic receptors and metalloproteases. In contrast, SALPs did not ... Studies with melittin and SPINK9 point out that purinergic receptors are involved in the activation of metalloproteases30,31. ... Melittin modulates keratinocyte function through P2 receptor-dependent ADAM activation. J. Biol. Chem. 287, 23678-23689, ... Peptide-induced keratinocyte migration depends on purinergic receptors and metalloproteases.. (A) HaCaT cells were scratched ...
P2) G protein coupled receptors (GPCRs). CD39 has intrinsic ecto-ATPase activity. Expression of CD39 is induced on T cells and ... of vascular and placental trophoblastic tissues and appears to modulate the functional expression of type 2 purinergic ( ...
N2 - Purinergic P2 receptors and gap junctions are two groups of proteins involved in the transmission of ICWs (intercellular ... AB - Purinergic P2 receptors and gap junctions are two groups of proteins involved in the transmission of ICWs (intercellular ... Purinergic P2 receptors and gap junctions are two groups of proteins involved in the transmission of ICWs (intercellular ... abstract = "Purinergic P2 receptors and gap junctions are two groups of proteins involved in the transmission of ICWs ( ...
... which subsequently activates the P2 purinergic receptors [9]. Blocking P2 receptors using pyridoxalphosphate-6-azophenyl-2,4- ... It is thus tempting to speculate that ATP release by PANX1 and subsequent P2 receptors activation are also involved in the ... in addition to that of ATP release and P2 receptors, in the PANX1-mediated regulation of NB malignant properties. ... Metabotropic NMDA receptor signaling couples Src family kinases to pannexin-1 during excitotoxicity. Nat Neurosci. 2016;19:432- ...
Targeting Neuroinflammation via Purinergic P2 Receptors for Disease Modification in Drug-Refractory Epilepsy. Tobias Engel, ...
keywords = "Animals, Infarction, Middle Cerebral Artery, Ischemia, Rats, Receptors, Purinergic P2, Stroke, Uridine Diphosphate/ ... Changes in receptor localization or receptor expression were evaluated using immunohistochemistry and quantitative flow ... Changes in receptor localization or receptor expression were evaluated using immunohistochemistry and quantitative flow ... Changes in receptor localization or receptor expression were evaluated using immunohistochemistry and quantitative flow ...
Receptors, Purinergic P2 / metabolism; Stress, Mechanical ... author keywords: ATP; Collagen gel; P2 receptor; bone; NF-kappa ... Receptors, Purinergic P2 / physiology; Stress, Mechanical ...
Yet it was not until 1972 that Burnstock introduced the concept of purinergic nerves and suggested that ATP might fulfil the ... und die damit verbundene Existenz von sogenannten P2-Rezeptoren (früher purinerge Rezeptoren) allgemein anerkannt wurde. Heute ... structure-activity relationship studies of analogues of the P2 receptor antagonists Suramin and NF023 at native P2 receptor ... Pharmacological evaluation of NF279 as a P2 receptor antagonist : ...
Zemková; Hana . Purinergic P2 Receptors: Structure and Function 2.0 . International Journal of Molecular Sciences. 2023; 24(6 ... Zemková; Hana . Special Issue of International Journal of Molecular Sciences (IJMS) "Purinergic P2 Receptors: Structure and ... Our focus is on the role of TRPV1, purinergic P2X receptors and inflammatory cytokines. In our research we use mainly ... Zemkova, is studying the relationship between the structure and function of P2X receptor channels and their role in electrical ...
Purinergic P2 Receptors Medicine & Life Sciences 66% * TRPV1 receptor Medicine & Life Sciences 65% ... keywords = "ATP, GERD, PAR2, Pain, Purinergic receptors, TRPV1",. author = "Annamaria Altomare and {Luca Guarino (Sara ... and roles for ATP and the purine and pyrimidine receptor subfamilies P1, P2X, and P2Y in the pathogenesis of GERD symptoms. ... and roles for ATP and the purine and pyrimidine receptor subfamilies P1, P2X, and P2Y in the pathogenesis of GERD symptoms.", ...
Zemková; Hana . Purinergic P2 Receptors: Structure and Function 2.0 . International Journal of Molecular Sciences. 2023; 24(6 ... Zemková; Hana . Special Issue of International Journal of Molecular Sciences (IJMS) "Purinergic P2 Receptors: Structure and ... P2X receptor perspective . Neuropharmacology. 2023; 234(Aug 15)); 109542 . IF = 4.7 [ASEP] [ doi ] Rupert; Marian - ... 4-NAPE is mediated by TRPV1 receptors under inflammatory conditions . Frontiers in Molecular Neuroscience. 2023; 16(22 June)); ...
P2 Receptors Scientific Review. Our Purine Receptor review gives an overview of the subtypes and structures of the P2 receptor ... Home / Pharmacology / Ion Channels / Ligand-gated Ion Channels / Purinergic (P2X) Receptors / Purinergic (P2X) Receptor ... Fischer et al (2013) Natural compounds with P2X7 receptor-modulating properties. Purinergic Signal 10 313 PMID: 24163006 ... Hoque et al (2012) P2X7 receptor-mediated purinergic signaling promotes liver injury in acetaminophen hepatotoxicity in mice. ...
The purinergic P2X receptor agonist 2-MeSATP and the P2Y agonist UTP significantly enhanced nNOS translocation; and ... the non-selective P2 receptor antagonist suramin completely blocked them. In addition, the increase in the nNOS translocation ... Consistent with the expression of P2X and P2Y receptors in the spinal cord, ATP and UTP increased the [Ca2+]i in primary ... ATP is involved in nNOS translocation mediated by protein kinase C via activation of P2X and P2Y receptors and nNOS ...
The possible involvement of P2 purinergic receptors is discussed.. Assuntos. Trifosfato de Adenosina/fisiologia , Matriz ... Both T cell receptor (TcR)-CD3 complex and CD2 increase the tyrosine kinase activity of p56lck. CD2 can mediate TcR-CD3- ... Human T cells can be activated and induced to proliferate through either the antigen-specific receptor complex (TcR-CD3) or the ... T cell activation by triggering the T cell receptor (TcR)-CD3 complex leads to a dramatic increase in tyrosine phosphorylation ...
This novel mechanism of receptor control might be a target for future studies aiming at decreasing dysregulated P2X3 receptor ... P2X3 receptor function is unexpectedly enhanced by pharmacological block of natriuretic peptide receptor-A (NPR-A), outlining a ... Tonic inhibition of P2X3 receptor activity by BNP/NPR-A/PKG pathways occurs via two distinct mechanisms: P2X3 serine ... We demonstrated that in mouse trigeminal neurons endogenous BNP acts on NPR-A receptors to determine constitutive depression of ...
... and postsynaptically through purinergic receptors classified as P1 and P2 receptors. P1 receptors are adenosine receptors, ... Our group is planning to examine the mRNA and protein expressions of purinergic receptors in the different stages of this ... Investigating the role of purinergic receptors in the pathophysiology of schizophrenia using human induced pluripotent stem ... Investigating the role of purinergic receptors in the pathophysiology of schizophrenia using human induced pluripotent stem ...
Autocrine regulation of TGF-β1-induced cell migration by exocytosis of ATP and activation of P2 receptors in human lung cancer ... Purinergic Signal 10:487-497. https://doi.org/10.1007/s11302-014-9411-x ... the active ligand TGF-β1 binds to its receptor (well summarized in [68]). Two receptor subunits are known, receptor type I and ... Our study adds TGF-β1 receptors as additional receptors to the subset of receptors that localize at upper airways motile cilia ...
Receptors, G-Protein-Coupled [D12.776.543.750.695] * Receptors, Purinergic [D12.776.543.750.695.700] * Receptors, Purinergic P2 ... Receptors, Purinergic [D12.776.543.750.720.700] * Receptors, Purinergic P2 [D12.776.543.750.720.700.720] * Receptors, ... 2011; PURINOCEPTOR P2X5 (now RECEPTORS, PURINERGIC P2X5) was indexed under RECEPTORS, PURINERGIC P2 1996-2010. History Note. ... A purinergic P2X neurotransmitter receptor found at high levels in the BRAIN and IMMUNE SYSTEM.. Terms. Receptors, Purinergic ...
Both ADP character on P2Y1 and P2Y13 receptors, and ATP underlying through HIV-infected experts, grow hydrogen feeling page 5 ... 02019; Purinergic bladder document. services; receptors in new readers. P2X1 and P2X5 communication review the 444Genre P2X ... The P2 teacher role enzymes is previouscarousel from Federal catalog in so. The data new life and fame purine support 2 collect ... These disorders aim receptors to the unifying breakdown that is cu book( Gachet, 2001). view preview that Posts in FREE new ...
Purine receptors in NMJ.. Purine receptors are divided into 2 large groups: adenosine or P1 receptors and P2 receptors, which ... receptors. Physiol Rev. 82: 1013-1067.. *43. Surprenant. A.. North. R. A.. 2009. Signaling at purinergic 2X. receptors. Annu ... are G protein-coupled receptors, while P2 receptors are consist of two distinct families: P2X receptors, which are ligand-gated ... As for P2 receptors, the following is known at present time. P2X7 receptor subunits were found on presynaptic motor nerve ...
Incubation of blood with ATP in the presence of selective P2 receptor antagonists showed that the stimulatory effect of ATP on ... Purinergic receptors involved in the immunomodulatory effects of ATP in human blood. / Swennen, E.L.R.; Bast, A.; Dagnelie, P.C ... Swennen, E.L.R. ; Bast, A. ; Dagnelie, P.C. / Purinergic receptors involved in the immunomodulatory effects of ATP in human ... Swennen, E. L. R., Bast, A., & Dagnelie, P. C. (2006). Purinergic receptors involved in the immunomodulatory effects of ATP in ...
PPADS, the non-selective P2-receptor antagonist (3-30 microm), Brilliant blue G (1-100 nm) the P2X7 -selective antagonist and ... the P2X7 receptor has only recently been localized in neurones, and functional responses mediated by these neuronal P2X7 ... and blockade of the kainate receptor-mediated transmission by CNQX (10-100 microm) and gadolinium (100 microm), decreased ATP ... receptors (P2X7 R) are largely unknown. Here we studied the effect of P2X7 R activation on the release of neurotransmitters ...

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