A pyridine nucleotide that mobilizes CALCIUM. It is synthesized from nicotinamide adenine dinucleotide (NAD) by ADP RIBOSE CYCLASE.
An ester formed between the aldehydic carbon of RIBOSE and the terminal phosphate of ADENOSINE DIPHOSPHATE. It is produced by the hydrolysis of nicotinamide-adenine dinucleotide (NAD) by a variety of enzymes, some of which transfer an ADP-ribosyl group to target proteins.
A pentose active in biological systems usually in its D-form.
A membrane-bound or cytosolic enzyme that catalyzes the synthesis of CYCLIC ADP-RIBOSE (cADPR) from nicotinamide adenine dinucleotide (NAD). This enzyme generally catalyzes the hydrolysis of cADPR to ADP-RIBOSE, as well, and sometimes the synthesis of cyclic ADP-ribose 2' phosphate (2'-P-cADPR) from NADP.
A specific subtype of muscarinic receptor that has a high affinity for the drug PIRENZEPINE. It is found in the peripheral GANGLIA where it signals a variety of physiological functions such as GASTRIC ACID secretion and BRONCHOCONSTRICTION. This subtype of muscarinic receptor is also found in neuronal tissues including the CEREBRAL CORTEX and HIPPOCAMPUS where it mediates the process of MEMORY and LEARNING.
An inorganic dye used in microscopy for differential staining and as a diagnostic reagent. In research this compound is used to study changes in cytoplasmic concentrations of calcium. Ruthenium red inhibits calcium transport through membrane channels.
The largest and uppermost of the paravertebral sympathetic ganglia.
A methylpyrrole-carboxylate from RYANIA that disrupts the RYANODINE RECEPTOR CALCIUM RELEASE CHANNEL to modify CALCIUM release from SARCOPLASMIC RETICULUM resulting in alteration of MUSCLE CONTRACTION. It was previously used in INSECTICIDES. It is used experimentally in conjunction with THAPSIGARGIN and other inhibitors of CALCIUM ATPASE uptake of calcium into SARCOPLASMIC RETICULUM.
A tetrameric calcium release channel in the SARCOPLASMIC RETICULUM membrane of SMOOTH MUSCLE CELLS, acting oppositely to SARCOPLASMIC RETICULUM CALCIUM-TRANSPORTING ATPASES. It is important in skeletal and cardiac excitation-contraction coupling and studied by using RYANODINE. Abnormalities are implicated in CARDIAC ARRHYTHMIAS and MUSCULAR DISEASES.
Enzymes that catalyze the transfer of multiple ADP-RIBOSE groups from nicotinamide-adenine dinucleotide (NAD) onto protein targets, thus building up a linear or branched homopolymer of repeating ADP-ribose units i.e., POLY ADENOSINE DIPHOSPHATE RIBOSE.
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.
A polynucleotide formed from the ADP-RIBOSE moiety of nicotinamide-adenine dinucleotide (NAD) by POLY(ADP-RIBOSE) POLYMERASES.
A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)
Ribose substituted in the 1-, 3-, or 5-position by a phosphoric acid moiety.
One of the mechanisms by which CELL DEATH occurs (compare with NECROSIS and AUTOPHAGOCYTOSIS). Apoptosis is the mechanism responsible for the physiological deletion of cells and appears to be intrinsically programmed. It is characterized by distinctive morphologic changes in the nucleus and cytoplasm, chromatin cleavage at regularly spaced sites, and the endonucleolytic cleavage of genomic DNA; (DNA FRAGMENTATION); at internucleosomal sites. This mode of cell death serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth.
Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position.
A family of intracellular CYSTEINE ENDOPEPTIDASES that play a role in regulating INFLAMMATION and APOPTOSIS. They specifically cleave peptides at a CYSTEINE amino acid that follows an ASPARTIC ACID residue. Caspases are activated by proteolytic cleavage of a precursor form to yield large and small subunits that form the enzyme. Since the cleavage site within precursors matches the specificity of caspases, sequential activation of precursors by activated caspases can occur.
A short pro-domain caspase that plays an effector role in APOPTOSIS. It is activated by INITIATOR CASPASES such as CASPASE 9. Isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.
Any cell, other than a ZYGOTE, that contains elements (such as NUCLEI and CYTOPLASM) from two or more different cells, usually produced by artificial CELL FUSION.
Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.
Pentosephosphates are monosaccharides, specifically pentoses, that have a phosphate group attached, playing crucial roles in carbohydrate metabolism, such as being intermediates in the pentose phosphate pathway and serving as precursors for nucleotide synthesis.
A class of nucleotide translocases found abundantly in mitochondria that function as integral components of the inner mitochondrial membrane. They facilitate the exchange of ADP and ATP between the cytosol and the mitochondria, thereby linking the subcellular compartments of ATP production to those of ATP utilization.
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 cell line derived from cultured tumor cells.
Enzymes that transfer the ADP-RIBOSE group of NAD or NADP to proteins or other small molecules. Transfer of ADP-ribose to water (i.e., hydrolysis) is catalyzed by the NADASES. The mono(ADP-ribose)transferases transfer a single ADP-ribose. POLY(ADP-RIBOSE) POLYMERASES transfer multiple units of ADP-ribose to protein targets, building POLY ADENOSINE DIPHOSPHATE RIBOSE in linear or branched chains.
A class of carbohydrates that contains five carbon atoms.
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.

CD38 signaling in B lymphocytes is controlled by its ectodomain but occurs independently of enzymatically generated ADP-ribose or cyclic ADP-ribose. (1/314)

CD38 is a type II transmembrane glycoprotein that is expressed by many cell types including lymphocytes. Signaling through CD38 on B lymphocytes can mediate B cell activation, proliferation, and cytokine secretion. Additionally, coligation of CD38 and the B cell Ag receptor can greatly augment B cell Ag receptor responses. Interestingly, the extracellular domain of CD38 catalyzes the conversion of NAD+ into nicotinamide, ADP-ribose (ADPR), and cyclic ADPR (cADPR). cADPR can induce intracellular calcium release in an inositol trisphosphate-independent manner and has been hypothesized to regulate CD38-mediated signaling. We demonstrate that replacement of the cytoplasmic tail and the transmembrane domains of CD38 did not impair CD38 signaling, coreceptor activity, or enzyme activity. In contrast, independent point mutations in the extracellular domain of CD38 dramatically impaired signal transduction. However, no correlation could be found between CD38-mediated signaling and the capacity of CD38 to catalyze an enzyme reaction and produce cADPR, ADPR, and/or nicotinamide. Instead, we propose that CD38 signaling and coreceptor activity in vitro are regulated by conformational changes induced in the extracellular domain upon ligand/substrate binding, rather than on actual turnover or generation of products.  (+info)

Evidence of a role for cyclic ADP-ribose in long-term synaptic depression in hippocampus. (2/314)

Ca2+ released from presynaptic and postsynaptic intracellular stores plays important roles in activity-dependent synaptic plasticity, including long-term depression (LTD) of synaptic strength. At Schaffer collateral-CA1 synapses in the hippocampus, presynaptic ryanodine receptor-gated stores appear to mobilize some of the Ca2+ necessary to induce LTD. Cyclic ADP-ribose (cADPR) has recently been proposed as an endogenous activator of ryanodine receptors in sea urchin eggs and several mammalian cell types. Here, we provide evidence that cADPR-mediated signaling pathways play a key role in inducing LTD. We show that biochemical production of cGMP increases cADPR concentration in hippocampal slices in vitro, and that blockade of cGMP-dependent protein kinase, cADPR receptors, or ryanodine-sensitive Ca2+ stores each prevent the induction of LTD at Schaffer collateral-CA1 synapses. A lack of effect of postsynaptic infusion of either cADPR antagonist indicates a probable presynaptic site of action.  (+info)

An antagonist of cADP-ribose inhibits arrhythmogenic oscillations of intracellular Ca2+ in heart cells. (3/314)

Oscillations of Ca2+ in heart cells are a major underlying cause of important cardiac arrhythmias, and it is known that Ca2+-induced release of Ca2+ from intracellular stores (the sarcoplasmic reticulum) is fundamental to the generation of such oscillations. There is now evidence that cADP-ribose may be an endogenous regulator of the Ca2+ release channel of the sarcoplasmic reticulum (the ryanodine receptor), raising the possibility that cADP-ribose may influence arrhythmogenic mechanisms in the heart. 8-Amino-cADP-ribose, an antagonist of cADP-ribose, suppressed oscillatory activity associated with overloading of intracellular Ca2+ stores in cardiac myocytes exposed to high doses of the beta-adrenoreceptor agonist isoproterenol or the Na+/K+-ATPase inhibitor ouabain. The oscillations suppressed by 8-amino-cADP-ribose included intracellular Ca2+ waves, spontaneous action potentials, after-depolarizations, and transient inward currents. Another antagonist of cADP-ribose, 8-bromo-cADP-ribose, was also effective in suppressing isoproterenol-induced oscillatory activity. Furthermore, in the presence of ouabain under conditions in which there was no arrhythmogenesis, exogenous cADP-ribose was found to be capable of triggering spontaneous contractile and electrical activity. Because enzymatic machinery for regulating the cytosolic cADP-ribose concentration is present within the cell, we propose that 8-amino-cADP-ribose and 8-bromo-cADP-ribose suppress cytosolic Ca2+ oscillations by antagonism of endogenous cADP-ribose, which sensitizes the Ca2+ release channels of the sarcoplasmic reticulum to Ca2+.  (+info)

The role of ryanodine receptors in the cyclic ADP ribose modulation of the M-like current in rodent m1 muscarinic receptor-transformed NG108-15 cells. (4/314)

1. The role of cyclic ADP ribose and ryanodine receptors in the inhibition of the M-like current (IK(M,ng)) by acetylcholine was investigated in m1 muscarinic receptor-transformed mouse neuroblastoma-rat glioma hybrid (NG108-15) cells using patch-clamp techniques and calcium microfluorimetry. 2. Acetylcholine (1-100 microM) decreased IK(M,ng) by up to 55 %. Application, via the patch pipette, of the cyclic ADP ribose antagonists 8-amino-cyclic ADP ribose (10-100 microM) and 8-bromo-cyclic ADP ribose (100-1000 microM) reduced this inhibition of IK(M,ng) in a concentration-dependent manner. The half-maximal inhibition concentrations for 8-amino- cyclic ADP ribose and 8-bromo-cyclic ADP ribose were around 40 microM and 1 mM, respectively. 3. Neither of the cyclic ADP ribose antagonists altered the amplitude of IK(M,ng) per se, or the incidence of the concurrent Ca2+-activated K+ current (IIK(Ca)) activation, also mediated by acetylcholine. 4. The ryanodine receptor modulators ryanodine (1-10 microM) and Ruthenium Red (10 microM) did not alter IK(M,ng) amplitude or IK(M,ng) inhibition mediated by acetylcholine. There was a statistically significant increase in the proportion of cells showing outward currents in the presence of Ruthenium Red. 5. Intracellular calcium levels measured with fura-2 microfluorimetry were increased with low concentrations of ryanodine (1 microM), more consistently with caffeine (10 mM), and in almost every case with both bradykinin (300 nM) and acetylcholine (100 microM). Caffeine-, but not bradykinin-evoked responses were abolished by preincubation with ryanodine (10 microM). 6. The fast 'rundown rate' of the M-current recorded in rat superior cervical ganglion cells under whole-cell conditions precluded an investigation of the effects of intracellular dialysis of cyclic ADP ribose. However, when cyclic ADP ribose (5 microM) was applied directly to the cytoplasmic face of inside-out membrane patches excised from rat superior cervical ganglion cells containing M-channels, it had no effect on the main parameters of single channel activity (conductance, mean open time or frequency of opening). 7. These results indicate that cyclic ADP ribose acts on a specific intracellular site to mediate IK(M,ng) inhibition. However, unlike previously established effects of cyclic ADP ribose, the ryanodine receptor is not required, suggesting that another molecular target may be involved. Studies at the single channel level indicate that cyclic ADP ribose may not act directly on the M-channels in inside-out patches.  (+info)

Hydrolysis of NADP+ by platelet CD38 in the absence of synthesis and degradation of cyclic ADP-ribose 2'-phosphate. (5/314)

CD38 is a multifunctional cell surface ectoenzyme that catalyzes both the synthesis of cyclic ADP-ribose from NAD+ and its hydrolysis to ADP-ribose. In this work, we investigated the metabolism of NADP+ by CD38 expressed on human platelets. Incubation of either platelet membranes or intact cells with NADP+ resulted in the rapid and time-dependent accumulation of ADP-ribose 2'-phosphate that paralleled the consumption of the substrate. However, under the same conditions, synthesis of cyclic ADP-ribose 2'-phosphate was not observed. By immunoprecipitation experiments, we identified CD38 as the enzyme responsible for the observed NADP+ glycohydrolase activity. The lack of detection of cyclic ADP-ribose 2'-phosphate was not due to its rapid hydrolysis, since direct incubation of platelet membranes with cyclic ADP-ribose 2'-phosphate did not result in the formation of ADP-ribose 2'-phosphate. By contrast, the same membrane samples expressed a significant ability to hydrolyze cyclic ADP-ribose to ADP-ribose. The absence of cyclic ADP-ribose 2'-phosphate hydrolase activity was also confirmed using high concentrations of substrate and by analysing both intact Jurkat T-lymphocytes and immunoprecipitated CD38. These results indicate that CD38, which is a multifunctional enzyme towards NAD+, displays exclusively a NADP+ glycohydrolase activity and is unable to catalyze both the synthesis and the hydrolysis of cyclic ADP-ribose 2'-phosphate.  (+info)

Effects of photoreleased cADP-ribose on calcium transients and calcium sparks in myocytes isolated from guinea-pig and rat ventricle. (6/314)

Actions of photoreleased cADP-ribose (cADPR), a novel regulator of calcium-induced calcium release (CICR) from ryanodine-sensitive stores, were investigated in cardiac myocytes. Photoreleased cADPR caused an increase in the magnitude of whole-cell calcium transients studied in mammalian cardiac ventricular myocytes (both guinea-pig and rat) using confocal microscopy). Approx. 15 s was required following photorelease of cADPR for the development of its maximal effect. Photoreleased cADPR also increased the frequency of calcium 'sparks', which are thought to be elementary events which make up the whole-cell calcium transient, and were studied in rat myocytes, but had little or no effect on spark characteristics (amplitude, rise time, decay time and distance to half amplitude). The potentiating effects of photoreleased cADPR on both whole-cell transients and the frequency of calcium sparks were prevented by cytosolic application of the antagonist 8-amino-cADPR (5 microM). These experiments, therefore, provide the first evidence in any cell type for an effect of cADPR on calcium sparks, and are the first to show the actions of photoreleased cADPR on whole-cell calcium transients in mammalian cells. The observations are consistent with the effects of cADPR in enhancing the calcium sensitivity of CICR from the sarcoplasmic reticulum in cardiac ventricular myocytes, leading to an increase in the probability of occurrence of calcium sparks and to an increase in whole-cell calcium transients. The slow time-course for development of the full effect on whole-cell calcium transients might be taken to indicate that the influence of cADPR on CICR may involve complex molecular interactions rather than a simple direct action of cADPR on the ryanodine-receptor channels.  (+info)

CD38/ADP-ribosyl cyclase: A new role in the regulation of osteoclastic bone resorption. (7/314)

The multifunctional ADP-ribosyl cyclase, CD38, catalyzes the cyclization of NAD(+) to cyclic ADP-ribose (cADPr). The latter gates Ca(2+) release through microsomal membrane-resident ryanodine receptors (RyRs). We first cloned and sequenced full-length CD38 cDNA from a rabbit osteoclast cDNA library. The predicted amino acid sequence displayed 59, 59, and 50% similarity, respectively, to the mouse, rat, and human CD38. In situ RT-PCR revealed intense cytoplasmic staining of osteoclasts, confirming CD38 mRNA expression. Both confocal microscopy and Western blotting confirmed the plasma membrane localization of the CD38 protein. The ADP-ribosyl cyclase activity of osteoclastic CD38 was next demonstrated by its ability to cyclize the NAD(+) surrogate, NGD(+), to its fluorescent derivative cGDP-ribose. We then examined the effects of CD38 on osteoclast function. CD38 activation by an agonist antibody (A10) in the presence of substrate (NAD(+)) triggered a cytosolic Ca(2+) signal. Both ryanodine receptor modulators, ryanodine, and caffeine, markedly attenuated this cytosolic Ca(2+) change. Furthermore, the anti-CD38 agonist antibody expectedly inhibited bone resorption in the pit assay and elevated interleukin-6 (IL-6) secretion. IL-6, in turn, enhanced CD38 mRNA expression. Taken together, the results provide compelling evidence for a new role for CD38/ADP-ribosyl cyclase in the control of bone resorption, most likely exerted via cADPr.  (+info)

Induction of hippocampal LTD requires nitric-oxide-stimulated PKG activity and Ca2+ release from cyclic ADP-ribose-sensitive stores. (8/314)

Long-term depression (LTD) of synaptic transmission can be induced by several mechanisms, one thought to involve Ca2+-dependent activation of postsynaptic nitric oxide (NO) synthase and subsequent diffusion of NO to the presynaptic terminal. We used the stable NO donor S-nitroso-N-acetylpenicillamine (SNAP) to study the NO-dependent form of LTD at Schaffer collateral-CA1 synapses in vitro. SNAP (100 microM) enhanced the induction of LTD via a cascade that was blocked by the N-methyl-D-aspartate receptor antagonist D-2-amino-5-phosphonopentanoic acid (50 microM), NO guanylyl cyclase inhibitor 1H-[1,2,4] oxadiazolo [4,3-a] quinoxalin-1-one (10 microM), and the PKG inhibitor KT5823 (1 microM). We further show that LTD induced by low-frequency stimulation in the absence of SNAP also is blocked by KT5823 or Rp-8-(4-chlorophenylthio)-guanosine 3',5'-cyclic monophosphorothioate (10 microM), cyclic guanosine 3',5' monophosphate-dependent protein kinase (PKG) inhibitors with different mechanisms of action. Furthermore SNAP-facilitated LTD was blocked when release from intracellular calcium stores was inhibited by ryanodine (10 microM). Finally, two cell-permeant antagonists of the cyclic ADP-ribose binding site on ryanodine receptors also were able to block the induction of LTD. These results support a cascade for induction of homosynaptic, NO-dependent LTD involving activation of guanylyl cyclase, production of guanosine 3',5' cyclic monophosphate and subsequent PKG activation. This process has an additional requirement for release of Ca2+ from ryanodine-sensitive stores, perhaps dependent on the second-messenger cyclic ADP ribose.  (+info)

Cyclic ADP-ribose (cADPR) is a molecule that functions as a second messenger in the body, playing a role in regulating various cellular processes. It is synthesized from nicotinamide adenine dinucleotide (NAD+) by the enzyme ADP-ribosyl cyclase.

Cyclic ADPR works by binding to and activating ryanodine receptors, a type of calcium channel found in the endoplasmic reticulum, a cellular organelle involved in calcium storage and release. This leads to an increase in intracellular calcium levels, which can trigger various downstream signaling pathways and physiological responses.

Cyclic ADPR has been implicated in a variety of biological processes, including the regulation of insulin secretion, immune cell function, and cardiovascular function. Dysregulation of cADPR signaling has been linked to several diseases, such as diabetes, neurodegenerative disorders, and cancer.

Adenosine diphosphate ribose (ADPR) is a molecule that plays a role in various cellular processes, including the modification of proteins and the regulation of enzyme activity. It is formed by the attachment of a diphosphate group and a ribose sugar to the adenine base of a nucleotide. ADPR is involved in the transfer of chemical energy within cells and is also a precursor in the synthesis of other important molecules, such as NAD+ (nicotinamide adenine dinucleotide). It should be noted that ADPR is not a medication or a drug, but rather a naturally occurring biomolecule.

Ribose is a simple carbohydrate, specifically a monosaccharide, which means it is a single sugar unit. It is a type of sugar known as a pentose, containing five carbon atoms. Ribose is a vital component of ribonucleic acid (RNA), one of the essential molecules in all living cells, involved in the process of transcribing and translating genetic information from DNA to proteins. The term "ribose" can also refer to any sugar alcohol derived from it, such as D-ribose or Ribitol.

ADP-ribosyl cyclase is an enzyme that catalyzes the conversion of nicotinamide adenine dinucleotide (NAD+) to cyclic ADP-ribose (cADPR). This enzyme plays a role in intracellular signaling, particularly in calcium mobilization in various cell types including immune cells and neurons. The regulation of this enzyme has been implicated in several physiological processes as well as in the pathophysiology of some diseases such as cancer and neurodegenerative disorders.

A muscarinic acetylcholine receptor (mAChR) is a type of G protein-coupled receptor (GPCR) that binds the neurotransmitter acetylcholine and mediates various responses in the body. The M1 subtype of muscarinic receptors (CHRM1) is widely distributed throughout the central and peripheral nervous system, with particularly high densities found in the cerebral cortex, hippocampus, striatum, and autonomic ganglia.

Muscarinic M1 receptors are coupled to G proteins of the Gq/11 family, which activate phospholipase C (PLC) upon receptor activation. This leads to the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) into inositol trisphosphate (IP3) and diacylglycerol (DAG), which further trigger intracellular signaling cascades.

The activation of muscarinic M1 receptors is involved in several physiological processes, including:

* Cognitive functions such as learning, memory, and attention
* Excitatory neurotransmission in the hippocampus
* Regulation of smooth muscle tone, particularly in the gastrointestinal tract and airways
* Secretion of various hormones and enzymes, including those involved in insulin release and lipid metabolism

Dysregulation of muscarinic M1 receptors has been implicated in several pathological conditions, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and irritable bowel syndrome. Therefore, targeting these receptors with pharmacological agents presents a potential therapeutic strategy for treating these disorders.

Ruthenium Red is not a medical term itself, but it is a chemical compound that has been used in some medical research and procedures. Ruthenium Red is a dye that is used as a marker in electron microscopy to stain and highlight cellular structures, particularly mitochondria, the energy-producing organelles of cells. It can also be used in experimental treatments for conditions such as heart failure and neurodegenerative diseases.

In summary, Ruthenium Red is a chemical compound with potential medical applications as a research tool and experimental treatment, rather than a standalone medical condition or diagnosis.

The superior cervical ganglion is a part of the autonomic nervous system, specifically the sympathetic division. It is a collection of nerve cell bodies (ganglion) that are located in the neck region (cervical) and is formed by the fusion of several smaller ganglia.

This ganglion is responsible for providing innervation to various structures in the head and neck, including the eyes, scalp, face muscles, meninges (membranes surrounding the brain and spinal cord), and certain glands such as the salivary and sweat glands. It does this through the postganglionic fibers that branch off from the ganglion and synapse with target organs or tissues.

The superior cervical ganglion is an essential component of the autonomic nervous system, which controls involuntary physiological functions such as heart rate, blood pressure, digestion, and respiration.

Ryanodine is not a medical condition or term, but it is a chemical compound that interacts with ryanodine receptors (RyRs), which are calcium release channels found in the sarcoplasmic reticulum of muscle cells. Ryanodine receptors play a crucial role in excitation-contraction coupling, which is the process by which electrical signals trigger muscle contractions.

Ryanodine itself is a plant alkaloid that was initially isolated from the South American shrub Ryania speciosa. It can bind to and inhibit ryanodine receptors, altering calcium signaling in muscle cells. This ability of ryanodine to modulate calcium release has made it a valuable tool in researching excitation-contraction coupling and related processes.

In some cases, the term "ryanodine" may be used in a medical context to refer to the effects of ryanodine or ryanodine receptor modulation on muscle function, particularly in relation to diseases associated with calcium handling abnormalities. However, it is not a medical condition per se.

The Ryanodine Receptor (RyR) is a calcium release channel located on the sarcoplasmic reticulum (SR), a type of endoplasmic reticulum found in muscle cells. It plays a crucial role in excitation-contraction coupling, which is the process by which electrical signals are converted into mechanical responses in muscle fibers.

In more detail, when an action potential reaches the muscle fiber's surface membrane, it triggers the opening of voltage-gated L-type calcium channels (Dihydropyridine Receptors or DHPRs) in the sarcolemma (the cell membrane of muscle fibers). This influx of calcium ions into the cytoplasm causes a conformational change in the RyR, leading to its own opening and the release of stored calcium from the SR into the cytoplasm. The increased cytoplasmic calcium concentration then initiates muscle contraction through interaction with contractile proteins like actin and myosin.

There are three isoforms of RyR: RyR1, RyR2, and RyR3. RyR1 is primarily found in skeletal muscle, while RyR2 is predominantly expressed in cardiac muscle. Both RyR1 and RyR2 are large homotetrameric proteins with a molecular weight of approximately 2.2 million Daltons. They contain multiple domains including an ion channel pore, regulatory domains, and a foot structure that interacts with DHPRs. RyR3 is more widely distributed, being found in various tissues such as the brain, smooth muscle, and some types of neurons.

Dysfunction of these channels has been implicated in several diseases including malignant hyperthermia, central core disease, catecholaminergic polymorphic ventricular tachycardia (CPVT), and certain forms of heart failure.

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.

Poly(ADP-ribose) (PAR) is not strictly referred to as "Poly Adenosine Diphosphate Ribose" in the medical or biochemical context, although the term ADP-ribose is a component of it. Poly(ADP-ribose) is a polymer of ADP-ribose units that are synthesized by enzymes called poly(ADP-ribose) polymerases (PARPs).

Poly(ADP-ribosyl)ation, the process of adding PAR polymers to target proteins, plays a crucial role in various cellular processes such as DNA repair, genomic stability, and cell death. In medical research, alterations in PAR metabolism have been implicated in several diseases, including cancer and neurodegenerative disorders. Therefore, understanding the function and regulation of poly(ADP-ribose) is of significant interest in biomedical sciences.

NAD (Nicotinamide Adenine Dinucleotide) is a coenzyme found in all living cells. It plays an essential role in cellular metabolism, particularly in redox reactions, where it acts as an electron carrier. NAD exists in two forms: NAD+, which accepts electrons and becomes reduced to NADH. This pairing of NAD+/NADH is involved in many fundamental biological processes such as generating energy in the form of ATP during cellular respiration, and serving as a critical cofactor for various enzymes that regulate cellular functions like DNA repair, gene expression, and cell death.

Maintaining optimal levels of NAD+/NADH is crucial for overall health and longevity, as it declines with age and in certain disease states. Therefore, strategies to boost NAD+ levels are being actively researched for their potential therapeutic benefits in various conditions such as aging, neurodegenerative disorders, and metabolic diseases.

Ribose monophosphates are organic compounds that play a crucial role in the metabolism of cells, particularly in energy transfer and nucleic acid synthesis. A ribose monophosphate is formed by the attachment of a phosphate group to a ribose molecule, which is a type of sugar known as a pentose.

In biochemistry, there are two important ribose monophosphates:

1. Alpha-D-Ribose 5-Phosphate (ADP-Ribose): This compound serves as an essential substrate in various cellular processes, including DNA repair, chromatin remodeling, and protein modification. The enzyme that catalyzes the formation of ADP-ribose is known as poly(ADP-ribose) polymerase (PARP).
2. Ribulose 5-Phosphate: This compound is a key intermediate in the Calvin cycle, which is the process by which plants and some bacteria convert carbon dioxide into glucose during photosynthesis. Ribulose 5-phosphate is formed from ribose 5-phosphate through a series of enzymatic reactions.

Ribose monophosphates are essential for the proper functioning of cells and have implications in various physiological processes, as well as in certain disease states.

Apoptosis is a programmed and controlled cell death process that occurs in multicellular organisms. It is a natural process that helps maintain tissue homeostasis by eliminating damaged, infected, or unwanted cells. During apoptosis, the cell undergoes a series of morphological changes, including cell shrinkage, chromatin condensation, and fragmentation into membrane-bound vesicles called apoptotic bodies. These bodies are then recognized and engulfed by neighboring cells or phagocytic cells, preventing an inflammatory response. Apoptosis is regulated by a complex network of intracellular signaling pathways that involve proteins such as caspases, Bcl-2 family members, and inhibitors of apoptosis (IAPs).

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.

Caspases are a family of protease enzymes that play essential roles in programmed cell death, also known as apoptosis. These enzymes are produced as inactive precursors and are activated when cells receive signals to undergo apoptosis. Once activated, caspases cleave specific protein substrates, leading to the characteristic morphological changes and DNA fragmentation associated with apoptotic cell death. Caspases also play roles in other cellular processes, including inflammation and differentiation. There are two types of caspases: initiator caspases (caspase-2, -8, -9, and -10) and effector caspases (caspase-3, -6, and -7). Initiator caspases are activated in response to various apoptotic signals and then activate the effector caspases, which carry out the proteolytic cleavage of cellular proteins. Dysregulation of caspase activity has been implicated in a variety of diseases, including neurodegenerative disorders, ischemic injury, and cancer.

Caspase-3 is a type of protease enzyme that plays a central role in the execution-phase of cell apoptosis, or programmed cell death. It's also known as CPP32 (CPP for ced-3 protease precursor) or apopain. Caspase-3 is produced as an inactive protein that is activated when cleaved by other caspases during the early stages of apoptosis. Once activated, it cleaves a variety of cellular proteins, including structural proteins, enzymes, and signal transduction proteins, leading to the characteristic morphological and biochemical changes associated with apoptotic cell death. Caspase-3 is often referred to as the "death protease" because of its crucial role in executing the cell death program.

I'm sorry for any confusion, but "hybrid cells" is not a standard medical term with a widely accepted or specific definition in the field of medicine. The term "hybrid" is used in various scientific and medical contexts to describe combinations or mixtures of different elements, such as hybridoma cells (a type of fusion cell used in research, created by combining a B cell and a tumor cell) or hybridization (in genetics, the process of combining DNA from two different sources).

Without more specific context, it's difficult to provide an accurate medical definition for "hybrid cells." If you could provide more information about the context in which this term was used, I would be happy to help you further!

Enzyme inhibitors are substances that bind to an enzyme and decrease its activity, preventing it from catalyzing a chemical reaction in the body. They can work by several mechanisms, including blocking the active site where the substrate binds, or binding to another site on the enzyme to change its shape and prevent substrate binding. Enzyme inhibitors are often used as drugs to treat various medical conditions, such as high blood pressure, abnormal heart rhythms, and bacterial infections. They can also be found naturally in some foods and plants, and can be used in research to understand enzyme function and regulation.

Pentose phosphates are monosaccharides that contain five carbon atoms and one phosphate group. They play a crucial role in various metabolic pathways, including the pentose phosphate pathway (PPP), which is a major source of NADPH and ribose-5-phosphate for the synthesis of nucleotides.

The pentose phosphate pathway involves two main phases: the oxidative phase and the non-oxidative phase. In the oxidative phase, glucose-6-phosphate is converted to ribulose-5-phosphate, producing NADPH and CO2 as byproducts. Ribulose-5-phosphate can then be further metabolized in the non-oxidative phase to produce other pentose phosphates or converted back to glucose-6-phosphate through a series of reactions.

Pentose phosphates are also important intermediates in the synthesis of nucleotides, coenzymes, and other metabolites. Abnormalities in pentose phosphate pathway enzymes can lead to various metabolic disorders, such as defects in erythrocyte function and increased susceptibility to oxidative stress.

Mitochondrial ADP/ATP translocases, also known as adenine nucleotide translocators (ANT), are a group of proteins located in the inner mitochondrial membrane that play a crucial role in cellular energy production. These translocases facilitate the exchange of adenosine diphosphate (ADP) and adenosine triphosphate (ATP) across the mitochondrial membrane, which is essential for oxidative phosphorylation and thus, energy homeostasis in the cell.

In more detail, during oxidative phosphorylation, ATP is produced within the mitochondria as a result of the electron transport chain's activity. This ATP must be exported to the cytosol for use by the cell's various processes. Simultaneously, the mitochondria need a continuous supply of ADP to sustain the production of ATP. The mitochondrial ADP/ATP translocases facilitate this exchange, allowing for the import of ADP into the mitochondria and the export of ATP to the cytosol.

There are multiple isoforms of the ADP/ATP translocase in humans (ANT1, ANT2, ANT3, and ANT4), encoded by different genes, with varying tissue distributions and functions. Dysfunction of these translocases has been implicated in several pathological conditions, including neurodegenerative diseases, ischemia-reperfusion injury, and cancer.

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.

A cell line that is derived from tumor cells and has been adapted to grow in culture. These cell lines are often used in research to study the characteristics of cancer cells, including their growth patterns, genetic changes, and responses to various treatments. They can be established from many different types of tumors, such as carcinomas, sarcomas, and leukemias. Once established, these cell lines can be grown and maintained indefinitely in the laboratory, allowing researchers to conduct experiments and studies that would not be feasible using primary tumor cells. It is important to note that tumor cell lines may not always accurately represent the behavior of the original tumor, as they can undergo genetic changes during their time in culture.

ADP Ribose Transferases are a group of enzymes that catalyze the transfer of ADP-ribose groups from donor molecules, such as NAD+ (nicotinamide adenine dinucleotide), to specific acceptor molecules. This transfer process plays a crucial role in various cellular processes, including DNA repair, gene expression regulation, and modulation of protein function.

The reaction catalyzed by ADP Ribose Transferases can be represented as follows:

Donor (NAD+ or NADP+) + Acceptor → Product (NR + ADP-ribosylated acceptor)

There are two main types of ADP Ribose Transferases based on their function and the type of modification they perform:

1. Poly(ADP-ribose) polymerases (PARPs): These enzymes add multiple ADP-ribose units to a single acceptor protein, forming long, linear, or branched chains known as poly(ADP-ribose) (PAR). PARylation is involved in DNA repair, genomic stability, and cell death pathways.
2. Monomeric ADP-ribosyltransferases: These enzymes transfer a single ADP-ribose unit to an acceptor protein, which is called mono(ADP-ribosyl)ation. This modification can regulate protein function, localization, and stability in various cellular processes, such as signal transduction, inflammation, and stress response.

Dysregulation of ADP Ribose Transferases has been implicated in several diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases. Therefore, understanding the function and regulation of these enzymes is essential for developing novel therapeutic strategies to target these conditions.

A pentose is a monosaccharide (simple sugar) that contains five carbon atoms. The name "pentose" comes from the Greek word "pente," meaning five, and "ose," meaning sugar. Pentoses play important roles in various biological processes, such as serving as building blocks for nucleic acids (DNA and RNA) and other biomolecules.

Some common pentoses include:

1. D-Ribose - A naturally occurring pentose found in ribonucleic acid (RNA), certain coenzymes, and energy-carrying molecules like adenosine triphosphate (ATP).
2. D-Deoxyribose - A pentose that lacks a hydroxyl (-OH) group on the 2' carbon atom, making it a key component of deoxyribonucleic acid (DNA).
3. Xylose - A naturally occurring pentose found in various plants and woody materials; it is used as a sweetener and food additive.
4. Arabinose - Another plant-derived pentose, arabinose can be found in various fruits, vegetables, and grains. It has potential applications in the production of biofuels and other bioproducts.
5. Lyxose - A less common pentose that can be found in some polysaccharides and glycoproteins.

Pentoses are typically less sweet than hexoses (six-carbon sugars) like glucose or fructose, but they still contribute to the overall sweetness of many foods and beverages.

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.

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