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  <cached-name>Trihexyphenidyl Action Pathway</cached-name>
  <cached-description>Trihexyphenidyl is an antispasmodic drug used as an adjunct drug in the management of parkinsonism and as a treatment for extrapyramidal symptoms caused by drugs affecting the central nervous system (CNS). Trihexyphenidyl is a non-selective muscarinic acetylcholine receptor antagonist but binds with higher affinity to the M1 subtype. In vivo studies have shown that trihexyphenidyl demonstrates higher affinity for central muscarinic receptors located in the cerebral cortex and lower affinity for those located peripherally. Other studies suggest that trihexyphenidyl may modify nicotinic acetylcholine receptor neurotransmission, leading indirectly to enhanced dopamine release in the striatum. Although the anticholinergic has proven to be useful in the treatment of symptoms associated with Parkinson’s disease or other movement disorders, its mechanism of action has yet to be fully elucidated. The precise mechanism of action of trihexyphenidyl remains inadequately comprehended; it appears to act on the parasympathetic nervous system by inhibiting efferent impulses directly. Structures innervated by the parasympathetic system, such as the salivary glands, eyes, and smooth muscles (directly and indirectly), are affected, even at smaller doses. Possible side effects of using Trihexyphenidyl may include dry mouth, constipation, nausea, and vomiting. Trihexyphenidyl is administered as an oral tablet.</cached-description>
  <cached-subject>Drug Action</cached-subject>
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          <name>Trihexyphenidyl Pathway</name>
          <description>Trihexyphenidyl is an antispasmodic drug used as an adjunct drug in the management of parkinsonism and as a treatment for extrapyramidal symptoms caused by drugs affecting the central nervous system (CNS). Trihexyphenidyl is a non-selective muscarinic acetylcholine receptor antagonist but binds with higher affinity to the M1 subtype. In vivo studies have shown that trihexyphenidyl demonstrates higher affinity for central muscarinic receptors located in the cerebral cortex and lower affinity for those located peripherally. Other studies suggest that trihexyphenidyl may modify nicotinic acetylcholine receptor neurotransmission, leading indirectly to enhanced dopamine release in the striatum. Although the anticholinergic has proven to be useful in the treatment of symptoms associated with Parkinson’s disease or other movement disorders, its mechanism of action has yet to be fully elucidated. The precise mechanism of action of trihexyphenidyl remains inadequately comprehended; it appears to act on the parasympathetic nervous system by inhibiting efferent impulses directly. Structures innervated by the parasympathetic system, such as the salivary glands, eyes, and smooth muscles (directly and indirectly), are affected, even at smaller doses. Possible side effects of using Trihexyphenidyl may include dry mouth, constipation, nausea, and vomiting. Trihexyphenidyl is administered as an oral tablet.</description>
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              <altext>Efferent Impulses</altext>
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              <pubmed-id>29126136</pubmed-id>
              <text>Wishart DS, Feunang YD, Guo AC, Lo EJ, Marcu A, Grant JR, Sajed T, Johnson D, Li C, Sayeeda Z, Assempour N, Iynkkaran I, Liu Y, Maciejewski A, Gale N, Wilson A, Chin L, Cummings R, Le D, Pon A, Knox C, Wilson M: DrugBank 5.0: a major update to the DrugBank database for 2018. Nucleic Acids Res. 2018 Jan 4;46(D1):D1074-D1082. doi: 10.1093/nar/gkx1037.</text>
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              <pubmed-id>2432979</pubmed-id>
              <text>Giachetti A, Giraldo E, Ladinsky H, Montagna E: Binding and functional profiles of the selective M1 muscarinic receptor antagonists trihexyphenidyl and dicyclomine. Br J Pharmacol. 1986 Sep;89(1):83-90. doi: 10.1111/j.1476-5381.1986.tb11123.x.</text>
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              <text>Trihexyphenidyl. </text>
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              <text>Physiology, muscarinic receptor - statpearls - NCBI bookshelf. (2022, August 8). https://www.ncbi.nlm.nih.gov/books/NBK555909/ </text>
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            <moldb-iupac>{[(2R,3S,4R,5R)-2-({[({[(3R)-3-[(2-{[2-(acetylsulfanyl)ethyl]carbamoyl}ethyl)carbamoyl]-3-hydroxy-2,2-dimethylpropoxy](hydroxy)phosphoryl}oxy)(hydroxy)phosphoryl]oxy}methyl)-5-(6-amino-9H-purin-9-yl)-4-hydroxyoxolan-3-yl]oxy}phosphonic acid</moldb-iupac>
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            <foodb-id>FDB022491</foodb-id>
            <synonyms>Ac-coa;Ac-coenzyme a;Ac-s-coa;Ac-s-coenzyme a;Acetyl coenzyme-a;Acetyl-coa;Acetyl-coenzyme a;Acetyl-s-coa;Acetyl-s-coenzyme a;Acetylcoenzyme-a;S-acetate coa;S-acetate coenzyme a;S-acetyl coenzyme a;Accoa;Acetyl coenzyme a;S-acetyl-coa;S-acetyl-coenzyme a;Acetylcoenzyme a</synonyms>
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            <short-name>Ac-CoA</short-name>
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            <name>Choline</name>
            <hmdb-id>HMDB0000097</hmdb-id>
            <description>Choline is a basic constituent of lecithin that is found in many plants and animal organs. It is important as a precursor of acetylcholine, as a methyl donor in various metabolic processes, and in lipid metabolism. Choline is now considered to be an essential vitamin. While humans can synthesize small amounts (by converting phosphatidylethanolamine to phosphatidylcholine), it must be consumed in the diet to maintain health. Required levels are between 425 mg/day (female) and 550 mg/day (male). Milk, eggs, liver, and peanuts are especially rich in choline. Most choline is found in phospholipids, namely phosphatidylcholine or lecithin. Choline can be oxidized to form betaine, which is a methyl source for many reactions (i.e. conversion of homocysteine into methionine). Lack of sufficient amounts of choline in the diet can lead to a fatty liver condition and general liver damage. This arises from the lack of VLDL, which is necessary to transport fats away from the liver. Choline deficiency also leads to elevated serum levels of alanine amino transferase and is associated with increased incidence of liver cancer.</description>
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            <kegg-id>C00114</kegg-id>
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            <moldb-iupac>(2-hydroxyethyl)trimethylazanium</moldb-iupac>
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            <foodb-id>FDB000710</foodb-id>
            <synonyms>(2-hydroxyethyl)trimethyl ammonium;(2-hydroxyethyl)trimethylammonium;(beta-hydroxyethyl)trimethylammonium;2-hydroxy-n,n,n-trimethyl-ethanaminium;2-hydroxy-n,n,n-trimethylethanaminium;Bilineurine;Biocolina;Biocoline;Choline;Choline cation;Choline ion;Cholinum;Hepacholine;Hormocline;Lipotril;N,n,n-trimethylethanol-ammonium;N,n,n-trimethylethanolammonium;Neocolina;Paresan;N-trimethylethanolamine;Trimethylethanolamine</synonyms>
            <pwc-id>PW_C000065</pwc-id>
            <short-name>Choline</short-name>
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            <name>Coenzyme A</name>
            <hmdb-id>HMDB0001423</hmdb-id>
            <description>Coenzyme A (CoA, CoASH, or HSCoA) is a coenzyme notable for its role in the synthesis and oxidization of fatty acids and the oxidation of pyruvate in the citric acid cycle. It is adapted from beta-mercaptoethylamine, panthothenate, and adenosine triphosphate. It is also a parent compound for other transformation products, including but not limited to, phenylglyoxylyl-CoA, tetracosanoyl-CoA, and 6-hydroxyhex-3-enoyl-CoA. Coenzyme A is synthesized in a five-step process from pantothenate and cysteine. In the first step pantothenate (vitamin B5) is phosphorylated to 4'-phosphopantothenate by the enzyme pantothenate kinase (PanK, CoaA, CoaX). In the second step, a cysteine is added to 4'-phosphopantothenate by the enzyme phosphopantothenoylcysteine synthetase (PPC-DC, CoaB) to form 4'-phospho-N-pantothenoylcysteine (PPC). In the third step, PPC is decarboxylated to 4'-phosphopantetheine by phosphopantothenoylcysteine decarboxylase (CoaC). In the fourth step, 4'-phosphopantetheine is adenylylated to form dephospho-CoA by the enzyme phosphopantetheine adenylyl transferase (CoaD). Finally, dephospho-CoA is phosphorylated using ATP to coenzyme A by the enzyme dephosphocoenzyme A kinase (CoaE). Since coenzyme A is, in chemical terms, a thiol, it can react with carboxylic acids to form thioesters, thus functioning as an acyl group carrier. CoA assists in transferring fatty acids from the cytoplasm to the mitochondria. A molecule of coenzyme A carrying an acetyl group is also referred to as acetyl-CoA. When it is not attached to an acyl group, it is usually referred to as 'CoASH' or 'HSCoA'. Coenzyme A is also the source of the phosphopantetheine group that is added as a prosthetic group to proteins such as acyl carrier proteins and formyltetrahydrofolate dehydrogenase. Acetyl-CoA is an important molecule itself. It is the precursor to HMG CoA which is a vital component in cholesterol and ketone synthesis. Furthermore, it contributes an acetyl group to choline to produce acetylcholine in a reaction catalysed by choline acetyltransferase. Its main task is conveying the carbon atoms within the acetyl group to the citric acid cycle to be oxidized for energy production (Wikipedia).</description>
            <cas>85-61-0</cas>
            <kegg-id>C00010</kegg-id>
            <pubchem-cid>6816</pubchem-cid>
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            <biocyc-id>CO-A</biocyc-id>
            <chemspider-id>6557</chemspider-id>
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            <moldb-smiles>CC(C)(COP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP(O)(O)=O)N1C=NC2=C1N=CN=C2N)[C@@H](O)C(=O)NCCC(=O)NCCS</moldb-smiles>
            <moldb-formula>C21H36N7O16P3S</moldb-formula>
            <moldb-inchi>InChI=1S/C21H36N7O16P3S/c1-21(2,16(31)19(32)24-4-3-12(29)23-5-6-48)8-41-47(38,39)44-46(36,37)40-7-11-15(43-45(33,34)35)14(30)20(42-11)28-10-27-13-17(22)25-9-26-18(13)28/h9-11,14-16,20,30-31,48H,3-8H2,1-2H3,(H,23,29)(H,24,32)(H,36,37)(H,38,39)(H2,22,25,26)(H2,33,34,35)/t11-,14-,15-,16+,20-/m1/s1</moldb-inchi>
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            <moldb-iupac>{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-2-({[hydroxy({hydroxy[(3R)-3-hydroxy-2,2-dimethyl-3-({2-[(2-sulfanylethyl)carbamoyl]ethyl}carbamoyl)propoxy]phosphoryl}oxy)phosphoryl]oxy}methyl)oxolan-3-yl]oxy}phosphonic acid</moldb-iupac>
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            <moldb-traditional-iupac>coenzyme A</moldb-traditional-iupac>
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            <foodb-id>FDB022614</foodb-id>
            <synonyms>Acetoacetyl coenzyme a sodium salt;Coa;Coa hydrate;Coa-sh;Coash;Coenzyme a;Coenzyme a hydrate;Coenzyme a-sh;Coenzyme ash;Coenzymes a;Depot-zeel;Propionyl coa;Propionyl coenzyme a;S-propanoate;S-propanoate coa;S-propanoate coenzyme a;S-propanoic acid;S-propionate coa;S-propionate coenzyme a;Zeel;[(2r,3s,4r,5r)-5-(6-amino-9h-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]methyl 3-hydroxy-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)-2,2-dimethyl-4-oxobutyl dihydrogen diphosphate</synonyms>
            <pwc-id>PW_C001099</pwc-id>
            <short-name>CoA</short-name>
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            <name>Acetylcholine </name>
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            <description>Acetylcholine (ACh) is a neurotransmitter. Acetylcholine in vertebrates is the major transmitter at neuromuscular junctions, autonomic ganglia, parasympathetic effector junctions, a subset of sympathetic effector junctions, and at many sites in the central nervous system. Its physiological and pharmacological effects, metabolism, release, and receptors have been well documented in several species. ACh has been considered an important excitatory neurotransmitter in the carotid body (CB). Various nicotinic and muscarinic ACh receptors are present in both afferent nerve endings and glomus cells. Therefore, ACh can depolarize or hyperpolarize the cell membrane depending on the available receptor type in the vicinity. Binding of ACh to its receptor can create a wide variety of cellular responses including opening cation channels (nicotinic ACh receptor activation), releasing Ca2+ from intracellular storage sites (via muscarinic ACh receptors), and modulating activities of K+ and Ca2+ channels. Interactions between ACh and other neurotransmitters (dopamine, adenosine, nitric oxide) have been known, and they may induce complicated responses. Cholinergic biology in the CB differs among species and even within the same species due to different genetic composition. Development and environment influence cholinergic biology. Pharmacological data clearly indicate that both muscarinic and nicotinic acetylcholine receptors have a role in the encoding of new memories. Localized lesions and antagonist infusions demonstrate the anatomical locus of these cholinergic effects, and computational modeling links the function of cholinergic modulation to specific cellular effects within these regions. Acetylcholine has been shown to increase the strength of afferent input relative to feedback, to contribute to theta rhythm oscillations, activate intrinsic mechanisms for persistent spiking, and increase the modification of synapses. These effects might enhance different types of encoding in different cortical structures. In particular, the effects in entorhinal and perirhinal cortex and hippocampus might be important for encoding new episodic memories. The role of ACh in attention has been repeatedly demonstrated in several tasks. Acetylcholine is linked to response accuracy in voluntary and reflexive attention and also to response speed in reflexive attention. It is well known that those with Attention-deficit/hyperactivity disorders tend to be inaccurate and slow to respond. (PMID: 17284361, 17011181, 15556286).</description>
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            <kegg-id>C01996</kegg-id>
            <pubchem-cid>187</pubchem-cid>
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            <drugbank-id>DB03128</drugbank-id>
            <moldb-smiles>CC(=O)OCC[N+](C)(C)C</moldb-smiles>
            <moldb-formula>C7H16NO2</moldb-formula>
            <moldb-inchi>InChI=1S/C7H16NO2/c1-7(9)10-6-5-8(2,3)4/h5-6H2,1-4H3/q+1</moldb-inchi>
            <moldb-inchikey>OIPILFWXSMYKGL-UHFFFAOYSA-N</moldb-inchikey>
            <moldb-iupac>[2-(acetyloxy)ethyl]trimethylazanium</moldb-iupac>
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            <moldb-traditional-iupac>acetylcholine</moldb-traditional-iupac>
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            <foodb-id>FDB012191</foodb-id>
            <synonyms>Ach;Acetyl choline ion;Acetylcholine cation;Acetylcholinium: acetyl-choline;Choline acetate;Choline acetate (ester);O-acetylcholine</synonyms>
            <pwc-id>PW_C000714</pwc-id>
            <short-name>ACh</short-name>
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            <name>Magnesium</name>
            <hmdb-id>HMDB0000547</hmdb-id>
            <description>Magnesium salts are essential in nutrition, being required for the activity of many enzymes, especially those concerned with oxidative phosphorylation. Physiologically, it exists as an ion in the body. It is a component of both intra- and extracellular fluids and is excreted in the urine and feces. Deficiency causes irritability of the nervous system with tetany, vasodilatation, convulsions, tremors, depression, and psychotic behavior. Magnesium ion in large amounts is an ionic laxative, and magnesium sulfate (Epsom salts) is sometimes used for this purpose. So-called "milk of magnesia" is a water suspension of one of the few insoluble magnesium compounds, magnesium hydroxide; the undissolved particles give rise to its appearance and name. Milk of magnesia is a mild base, and is commonly used as an antacid.</description>
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            <drugbank-id>DB01378</drugbank-id>
            <moldb-smiles>[Mg++]</moldb-smiles>
            <moldb-formula>Mg</moldb-formula>
            <moldb-inchi>InChI=1S/Mg/q+2</moldb-inchi>
            <moldb-inchikey>JLVVSXFLKOJNIY-UHFFFAOYSA-N</moldb-inchikey>
            <moldb-iupac>magnesium(2+) ion</moldb-iupac>
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            <moldb-mono-mass>23.985041898</moldb-mono-mass>
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            <moldb-traditional-iupac>magnesium(2+) ion</moldb-traditional-iupac>
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            <foodb-id>FDB003518</foodb-id>
            <synonyms>Magnesium;Magnesium ions;Magnesium ion;Magnesium, doubly charged positive ion;Magnesium, ion (mg(2+));Mg(2+);Mg2+</synonyms>
            <pwc-id>PW_C000423</pwc-id>
            <short-name>Mg2+</short-name>
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            <description>Acetic acid is one of the simplest carboxylic acids. It is an important chemical reagent and industrial chemical that is used in the production of plastic soft drink bottles, photographic film; and polyvinyl acetate for wood glue, as well as many synthetic fibres and fabrics. In households diluted acetic acid is often used as a cleaning agent. In the food industry acetic acid is used as an acidity regulator. The acetyl group, derived from acetic acid, is fundamental to the biochemistry of virtually all forms of life. When bound to coenzyme A it is central to the metabolism of carbohydrates and fats. However, the concentration of free acetic acid in cells is kept at a low level to avoid disrupting the control of the pH of the cell contents. Acetic acid is produced and excreted by certain bacteria, notably the Acetobacter genus and Clostridium acetobutylicum. These bacteria are found universally in foodstuffs, water, and soil, and acetic acid is produced naturally as fruits and some other foods spoil. Acetic acid is also a component of the vaginal lubrication of humans and other primates, where it appears to serve as a mild antibacterial agent.</description>
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            <synonyms>Acetate;Ethanoate;Ethanoic acid;Ethylate;Ethylic acid;Glacial acetate;Glacial acetic acid;Kyselina octova;Methanecarboxylate;Methanecarboxylic acid;Vinegar;Vinegar acid;Acide acetique;Acoh;Ch3-cooh;Ch3co2h;E 260;E-260;E260;Essigsaeure;Ethoic acid;Hoac;Ins no. 260;Meco2h;Mecooh;Ethoate</synonyms>
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            <short-name>Acoh</short-name>
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            <name>Calcium</name>
            <hmdb-id>HMDB0000464</hmdb-id>
            <description>Calcium is essential for the normal growth and maintenance of bones and teeth, and calcium requirements must be met throughout life. Requirements are greatest during periods of growth, such as childhood, during pregnancy and when breast-feeding. Long-term calcium deficiency can lead to osteoporosis, in which the bone deteriorates and there is an increased risk of fractures. Adults need between 1,000 and 1,300 mg of calcium in their daily diet. Calcium is essential for living organisms, particularly in cell physiology, and is the most common metal in many animals. Physiologically, it exists as an ion in the body. Calcium 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. Calcium is an important component of a healthy diet. A deficit can affect bone and tooth formation, while overretention can cause kidney stones. Vitamin D is needed to absorb calcium. Dairy products, such as milk and cheese, are a well-known source of calcium. However, some individuals are allergic to dairy products and even more people, particularly those of non-European descent, are lactose-intolerant, leaving them unable to consume dairy products. Fortunately, many other good sources of calcium exist. These include: seaweeds such as kelp, wakame and hijiki; nuts and seeds (like almonds and sesame); beans; amaranth; collard greens; okra; rutabaga; broccoli; kale; and fortified products such as orange juice and soy milk. Calcium has also been found to assist in the production of lymphatic fluids.</description>
            <cas>14127-61-8</cas>
            <kegg-id>C00076</kegg-id>
            <pubchem-cid>271</pubchem-cid>
            <chebi-id>29108</chebi-id>
            <biocyc-id>CA%2b2</biocyc-id>
            <chemspider-id>266</chemspider-id>
            <drugbank-id>DB01373</drugbank-id>
            <moldb-smiles>[Ca++]</moldb-smiles>
            <moldb-formula>Ca</moldb-formula>
            <moldb-inchi>InChI=1S/Ca/q+2</moldb-inchi>
            <moldb-inchikey>BHPQYMZQTOCNFJ-UHFFFAOYSA-N</moldb-inchikey>
            <moldb-iupac>calcium(2+) ion</moldb-iupac>
            <moldb-average-mass>40.078</moldb-average-mass>
            <moldb-mono-mass>39.962591155</moldb-mono-mass>
            <moldb-alogps-logs nil="true"/>
            <moldb-donor-count>0</moldb-donor-count>
            <moldb-traditional-iupac>calcium(2+) ion</moldb-traditional-iupac>
            <moldb-formal-charge type="integer">2</moldb-formal-charge>
            <moldb-physiological-charge type="integer">2</moldb-physiological-charge>
            <drugbank-metabolite-id nil="true"/>
            <foodb-id>FDB003513</foodb-id>
            <synonyms>Ca;Calcium element;Ca(2+);Ca2+;Calcium ion;Calcium, doubly charged positive ion</synonyms>
            <pwc-id>PW_C000353</pwc-id>
            <short-name>Ca2+</short-name>
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            <name>Trihexyphenidyl</name>
            <hmdb-id>HMDB0014520</hmdb-id>
            <description>Trihexyphenidyl is only found in individuals that have used or taken this drug. It is one of the centrally acting muscarinic antagonists used for treatment of parkinsonian disorders and drug-induced extrapyramidal movement disorders and as an antispasmodic. [PubChem]Trihexyphenidyl is a selective M1 muscarinic acetylcholine receptor antagonist. It is able to discriminate between the M1 (cortical or neuronal) and the peripheral muscarinic subtypes (cardiac and glandular). Trihexyphenidyl partially blocks cholinergic activity in the CNS, which is responsible for the symptoms of Parkinson's disease. It is also thought to increase the availability of dopamine, a brain chemical that is critical in the initiation and smooth control of voluntary muscle movement.</description>
            <cas>144-11-6</cas>
            <kegg-id>C07171</kegg-id>
            <pubchem-cid>5572</pubchem-cid>
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            <moldb-smiles>OC(CCN1CCCCC1)(C1CCCCC1)C1=CC=CC=C1</moldb-smiles>
            <moldb-formula>C20H31NO</moldb-formula>
            <moldb-inchi>InChI=1S/C20H31NO/c22-20(18-10-4-1-5-11-18,19-12-6-2-7-13-19)14-17-21-15-8-3-9-16-21/h1,4-5,10-11,19,22H,2-3,6-9,12-17H2</moldb-inchi>
            <moldb-inchikey>HWHLPVGTWGOCJO-UHFFFAOYSA-N</moldb-inchikey>
            <moldb-iupac>1-cyclohexyl-1-phenyl-3-(piperidin-1-yl)propan-1-ol</moldb-iupac>
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            <moldb-mono-mass>301.240564619</moldb-mono-mass>
            <moldb-alogps-logs>-4.98</moldb-alogps-logs>
            <moldb-donor-count>1</moldb-donor-count>
            <moldb-traditional-iupac>trihexyphenidyl</moldb-traditional-iupac>
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            <drugbank-metabolite-id nil="true"/>
            <foodb-id nil="true"/>
            <synonyms>Trihexifenidilo [inn-spanish];Trihexylphenidyl;Trihexylphenidyle;Trihexylphenizyl;Trihexyphenidyle;Trihexyphenidyle [inn-french];Trihexyphenidylum [inn-latin];Triphenidyl;Apo-trihex</synonyms>
            <pwc-id>PW_C008897</pwc-id>
            <short-name>AT</short-name>
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            <name>Choline O-acetyltransferase</name>
            <uniprot-id>P28329</uniprot-id>
            <description>Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses.
</description>
            <hmdbp-id>HMDBP00025</hmdbp-id>
            <gene-name>CHAT</gene-name>
            <locus>10q11.2</locus>
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                <biological-state-id type="integer">184</biological-state-id>
              </element-state>
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                <id type="integer">142580</id>
                <biological-state-id type="integer">789</biological-state-id>
              </element-state>
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                <id type="integer">142905</id>
                <biological-state-id type="integer">39</biological-state-id>
              </element-state>
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                <id type="integer">143602</id>
                <biological-state-id type="integer">1060</biological-state-id>
              </element-state>
            </element-states>
          </protein>
          <protein>
            <id type="integer">498</id>
            <name>Acetylcholinesterase</name>
            <uniprot-id>P22303</uniprot-id>
            <description>Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis.
</description>
            <hmdbp-id>HMDBP00524</hmdbp-id>
            <gene-name>ACHE</gene-name>
            <locus>7q22</locus>
            <drugbank-id nil="true"/>
            <genbank-id>CH236956</genbank-id>
            <species-id type="integer">1</species-id>
            <ec-numbers>3.1.1.7</ec-numbers>
            <synonyms nil="true"/>
            <element-states>
              <element-state>
                <id type="integer">1498</id>
                <biological-state-id type="integer">14</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">138425</id>
                <biological-state-id type="integer">211</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">142616</id>
                <biological-state-id type="integer">37</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">143603</id>
                <biological-state-id type="integer">1059</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">145583</id>
                <biological-state-id type="integer">950</biological-state-id>
              </element-state>
            </element-states>
          </protein>
          <protein>
            <id type="integer">2713</id>
            <name>Voltage-dependent N-type calcium channel subunit alpha-1B</name>
            <uniprot-id>Q00975</uniprot-id>
            <description>Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1B gives rise to N-type calcium currents. N-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by omega-conotoxin-GVIA (omega-CTx-GVIA) and by omega-agatoxin- IIIA (omega-Aga-IIIA). They are however insensitive to dihydropyridines (DHP), and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing alpha-1B subunit may play a role in directed migration of immature neurons</description>
            <hmdbp-id>HMDBP07492</hmdbp-id>
            <gene-name>CACNA1B</gene-name>
            <locus>9q34</locus>
            <drugbank-id nil="true"/>
            <genbank-id>M94173</genbank-id>
            <species-id type="integer">1</species-id>
            <ec-numbers></ec-numbers>
            <synonyms nil="true"/>
            <element-states>
              <element-state>
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                <biological-state-id type="integer">74</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">139856</id>
                <biological-state-id type="integer">204</biological-state-id>
              </element-state>
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                <id type="integer">140828</id>
                <biological-state-id type="integer">73</biological-state-id>
              </element-state>
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                <biological-state-id type="integer">787</biological-state-id>
              </element-state>
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                <biological-state-id type="integer">1058</biological-state-id>
              </element-state>
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                <biological-state-id type="integer">1033</biological-state-id>
              </element-state>
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                <biological-state-id type="integer">1071</biological-state-id>
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                <biological-state-id type="integer">901</biological-state-id>
              </element-state>
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                <id type="integer">143190</id>
                <biological-state-id type="integer">1118</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">143261</id>
                <biological-state-id type="integer">52</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">143418</id>
                <biological-state-id type="integer">308</biological-state-id>
              </element-state>
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                <biological-state-id type="integer">1409</biological-state-id>
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                <biological-state-id type="integer">1420</biological-state-id>
              </element-state>
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                <id type="integer">145543</id>
                <biological-state-id type="integer">1428</biological-state-id>
              </element-state>
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                <biological-state-id type="integer">1436</biological-state-id>
              </element-state>
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                <id type="integer">145611</id>
                <biological-state-id type="integer">1444</biological-state-id>
              </element-state>
            </element-states>
          </protein>
          <protein>
            <id type="integer">2706</id>
            <name>Voltage-dependent calcium channel subunit alpha-2/delta-2</name>
            <uniprot-id>Q9NY47</uniprot-id>
            <description>The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel. Acts as a regulatory subunit for P/Q-type calcium channel (CACNA1A), N-type (CACNA1B), L-type (CACNA1C OR CACNA1D) and possibly T-type (CACNA1G). Overexpression induces apoptosis</description>
            <hmdbp-id>HMDBP07485</hmdbp-id>
            <gene-name>CACNA2D2</gene-name>
            <locus>3p21.3</locus>
            <drugbank-id nil="true"/>
            <genbank-id>AJ251368</genbank-id>
            <species-id type="integer">1</species-id>
            <ec-numbers></ec-numbers>
            <synonyms nil="true"/>
            <element-states>
              <element-state>
                <id type="integer">940</id>
                <biological-state-id type="integer">39</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">2768</id>
                <biological-state-id type="integer">45</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">3514</id>
                <biological-state-id type="integer">14</biological-state-id>
              </element-state>
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                <biological-state-id type="integer">52</biological-state-id>
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                <biological-state-id type="integer">65</biological-state-id>
              </element-state>
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                <biological-state-id type="integer">228</biological-state-id>
              </element-state>
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                <biological-state-id type="integer">651</biological-state-id>
              </element-state>
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                <biological-state-id type="integer">51</biological-state-id>
              </element-state>
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                <id type="integer">139707</id>
                <biological-state-id type="integer">778</biological-state-id>
              </element-state>
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                <id type="integer">139809</id>
                <biological-state-id type="integer">204</biological-state-id>
              </element-state>
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                <biological-state-id type="integer">48</biological-state-id>
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                <biological-state-id type="integer">74</biological-state-id>
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                <id type="integer">140624</id>
                <biological-state-id type="integer">308</biological-state-id>
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                <id type="integer">140634</id>
                <biological-state-id type="integer">7</biological-state-id>
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                <id type="integer">140637</id>
                <biological-state-id type="integer">828</biological-state-id>
              </element-state>
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                <id type="integer">140643</id>
                <biological-state-id type="integer">787</biological-state-id>
              </element-state>
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                <biological-state-id type="integer">73</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">141687</id>
                <biological-state-id type="integer">67</biological-state-id>
              </element-state>
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                <biological-state-id type="integer">2</biological-state-id>
              </element-state>
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                <id type="integer">142395</id>
                <biological-state-id type="integer">1014</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">142871</id>
                <biological-state-id type="integer">1055</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">142911</id>
                <biological-state-id type="integer">1058</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">142955</id>
                <biological-state-id type="integer">1033</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">142980</id>
                <biological-state-id type="integer">1071</biological-state-id>
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                <biological-state-id type="integer">1118</biological-state-id>
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                <biological-state-id type="integer">1144</biological-state-id>
              </element-state>
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                <id type="integer">145487</id>
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              </element-state>
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                <id type="integer">145524</id>
                <biological-state-id type="integer">1420</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">145544</id>
                <biological-state-id type="integer">1428</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">145563</id>
                <biological-state-id type="integer">1436</biological-state-id>
              </element-state>
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                <id type="integer">145589</id>
                <biological-state-id type="integer">1367</biological-state-id>
              </element-state>
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                <id type="integer">145598</id>
                <biological-state-id type="integer">1449</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">145604</id>
                <biological-state-id type="integer">1361</biological-state-id>
              </element-state>
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                <id type="integer">145612</id>
                <biological-state-id type="integer">1444</biological-state-id>
              </element-state>
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                <id type="integer">145642</id>
                <biological-state-id type="integer">1000</biological-state-id>
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                <id type="integer">145651</id>
                <biological-state-id type="integer">1453</biological-state-id>
              </element-state>
            </element-states>
          </protein>
          <protein>
            <id type="integer">2723</id>
            <name>Voltage-dependent L-type calcium channel subunit beta-4</name>
            <uniprot-id>O00305</uniprot-id>
            <description>The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting</description>
            <hmdbp-id>HMDBP07502</hmdbp-id>
            <gene-name>CACNB4</gene-name>
            <locus>2q22-q23</locus>
            <drugbank-id nil="true"/>
            <genbank-id>U95020</genbank-id>
            <species-id type="integer">1</species-id>
            <ec-numbers></ec-numbers>
            <synonyms nil="true"/>
            <element-states>
              <element-state>
                <id type="integer">141882</id>
                <biological-state-id type="integer">787</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">142617</id>
                <biological-state-id type="integer">73</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">142956</id>
                <biological-state-id type="integer">1033</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">142981</id>
                <biological-state-id type="integer">1071</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">143289</id>
                <biological-state-id type="integer">1058</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">145488</id>
                <biological-state-id type="integer">1409</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">145525</id>
                <biological-state-id type="integer">1420</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">145545</id>
                <biological-state-id type="integer">1428</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">145564</id>
                <biological-state-id type="integer">1436</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">145613</id>
                <biological-state-id type="integer">1444</biological-state-id>
              </element-state>
            </element-states>
          </protein>
          <protein>
            <id type="integer">2720</id>
            <name>Voltage-dependent L-type calcium channel subunit beta-1</name>
            <uniprot-id>Q02641</uniprot-id>
            <description>The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting</description>
            <hmdbp-id>HMDBP07499</hmdbp-id>
            <gene-name>CACNB1</gene-name>
            <locus>17q21-q22</locus>
            <drugbank-id nil="true"/>
            <genbank-id>CH471152</genbank-id>
            <species-id type="integer">1</species-id>
            <ec-numbers></ec-numbers>
            <synonyms nil="true"/>
            <element-states>
              <element-state>
                <id type="integer">938</id>
                <biological-state-id type="integer">39</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">2769</id>
                <biological-state-id type="integer">45</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">3515</id>
                <biological-state-id type="integer">14</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">3540</id>
                <biological-state-id type="integer">52</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">5096</id>
                <biological-state-id type="integer">65</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">80753</id>
                <biological-state-id type="integer">228</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">136133</id>
                <biological-state-id type="integer">651</biological-state-id>
              </element-state>
              <element-state>
                <id type="integer">139531</id>
                <biological-state-id type="integer">51</biological-state-id>
              </element-state>
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                <id type="integer">139706</id>
                <biological-state-id type="integer">778</biological-state-id>
              </element-state>
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                <biological-state-id type="integer">204</biological-state-id>
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                <biological-state-id type="integer">48</biological-state-id>
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                <biological-state-id type="integer">308</biological-state-id>
              </element-state>
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                <biological-state-id type="integer">787</biological-state-id>
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                <biological-state-id type="integer">74</biological-state-id>
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                <biological-state-id type="integer">7</biological-state-id>
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                <id type="integer">140638</id>
                <biological-state-id type="integer">828</biological-state-id>
              </element-state>
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                <id type="integer">141001</id>
                <biological-state-id type="integer">73</biological-state-id>
              </element-state>
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                <id type="integer">141933</id>
                <biological-state-id type="integer">67</biological-state-id>
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                <biological-state-id type="integer">1014</biological-state-id>
              </element-state>
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              </element-state>
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              </element-state>
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                <biological-state-id type="integer">1033</biological-state-id>
              </element-state>
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                <biological-state-id type="integer">1071</biological-state-id>
              </element-state>
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              </element-state>
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                <biological-state-id type="integer">1138</biological-state-id>
              </element-state>
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                <biological-state-id type="integer">1367</biological-state-id>
              </element-state>
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              </element-state>
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              </element-state>
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                <biological-state-id type="integer">1428</biological-state-id>
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              </element-state>
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              </element-state>
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                <biological-state-id type="integer">1361</biological-state-id>
              </element-state>
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                <biological-state-id type="integer">1444</biological-state-id>
              </element-state>
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                <biological-state-id type="integer">1000</biological-state-id>
              </element-state>
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                <biological-state-id type="integer">1453</biological-state-id>
              </element-state>
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                <id type="integer">145873</id>
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                <biological-state-id type="integer">945</biological-state-id>
              </element-state>
            </element-states>
          </protein>
          <protein>
            <id type="integer">23817</id>
            <name>Vesicular acetylcholine transporter</name>
            <uniprot-id>Q16572</uniprot-id>
            <description>
Involved in acetylcholine transport into synaptic vesicles.
</description>
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            <gene-name>SLC18A3</gene-name>
            <locus nil="true"/>
            <drugbank-id nil="true"/>
            <genbank-id nil="true"/>
            <species-id type="integer">1</species-id>
            <ec-numbers></ec-numbers>
            <synonyms nil="true"/>
            <element-states>
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                <id type="integer">141420</id>
                <biological-state-id type="integer">932</biological-state-id>
              </element-state>
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                <id type="integer">142622</id>
                <biological-state-id type="integer">866</biological-state-id>
              </element-state>
            </element-states>
          </protein>
          <protein>
            <id type="integer">23816</id>
            <name>High affinity choline transporter 1</name>
            <uniprot-id>Q9GZV3</uniprot-id>
            <description>
Transmembrane transporter that imports choline from the extracellular space into the neuron with high affinity. Choline uptake is the rate-limiting step in acetylcholine synthesis. Sodium ion- and chloride ion-dependent.
</description>
            <hmdbp-id nil="true"/>
            <gene-name>SLC5A7</gene-name>
            <locus nil="true"/>
            <drugbank-id nil="true"/>
            <genbank-id nil="true"/>
            <species-id type="integer">1</species-id>
            <ec-numbers></ec-numbers>
            <synonyms nil="true"/>
            <element-states>
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                <biological-state-id type="integer">73</biological-state-id>
              </element-state>
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                <id type="integer">142581</id>
                <biological-state-id type="integer">787</biological-state-id>
              </element-state>
            </element-states>
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The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover.
</description>
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The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover.
</description>
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