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2-arachidonylglycerol
2-Arachidonoylglycerol (2-AG) is an endocannabinoid, an endogenous agonist of the CB1 receptor and the primary endogenous ligand for the CB2 receptor. It is an ester formed from the omega-6 fatty acid arachidonic acid and glycerol. It is present at relatively high levels in the central nervous system, with cannabinoid neuromodulatory effects. It has been found in maternal bovine and human milk. The chemical was first described in 1994-1995, although it had been discovered some time before that. The activities of phospholipase C (PLC) and diacylglycerol lipase (DAGL) mediate its formation. 2-AG is synthesized from arachidonic acid-containing diacylglycerol (DAG). Occurrence 2-AG, unlike anandamide (another endocannabinoid), is present at relatively high levels in the central nervous system; it is the most abundant molecular species of monoacylglycerol found in mouse and rat brain (~5-10 nmol/g tissue). Detection of 2-AG in brain tissue is complicated by the relative ease of its i ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
ABHD12
alpha/beta-Hydrolase domain containing 12 (ABHD12) is a serine hydrolase encoded by the ''ABHD12'' gene that participates in the breakdown of the endocannabinoid neurotransmitter 2-arachidonylglycerol (2-AG) in the central nervous system. It is responsible for about 9% of brain 2-AG hydrolysis. Together, ABHD12 along with two other enzymes, monoacylglycerol lipase (MAGL) and ABHD6, control 99% of 2-AG hydrolysis in the brain. ABHD12 also serves as a lysophospholipase and metabolizes lysophosphatidylserine (LPS). Protein structure ABHD12 is a ≈45 kDa integrated membrane glycoprotein, with an active site proposed to face into the extracellular space. Currently, the crystal structure of ABHD12 is not known. Function ABHD12 is a lysophosphatidylserine ( lysoPS) lipase responsible for regulation of immune and neurological processes, and shown to act on the endocannabinoid arachidonoylglycerol (AG) as a monoacylglycerol lipase. Endocannabinoids are associated with a range of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hebrew University Of Jerusalem
The Hebrew University of Jerusalem (HUJI; he, הַאוּנִיבֶרְסִיטָה הַעִבְרִית בִּירוּשָׁלַיִם) is a public research university based in Jerusalem, Israel. Co-founded by Albert Einstein and Dr. Chaim Weizmann in July 1918, the public university officially opened in April 1925. It is the second-oldest Israeli university, having been founded 30 years before the establishment of the State of Israel but six years after the older Technion university. The HUJI has three campuses in Jerusalem and one in Rehovot. The world's largest library for Jewish studies—the National Library of Israel—is located on its Edmond J. Safra campus in the Givat Ram neighbourhood of Jerusalem. The university has five affiliated teaching hospitals (including the Hadassah Medical Center), seven faculties, more than 100 research centers, and 315 academic departments. , one-third of all the doctoral candidates in Israel were studying at the HUJI. Among its first ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
ABHD6
alpha/beta-Hydrolase domain containing 6 (ABHD6), also known as monoacylglycerol lipase ABHD6 or 2-arachidonoylglycerol hydrolase is an enzyme that in humans is encoded by the ABHD6 gene. Function ABHD6 is a serine hydrolyzing enzyme that possesses typical α/β-hydrolase family domains. ABHD6 was first studied because of its over-expression in certain forms of tumours. ABHD6 has been linked to regulation of the endocannabinoid system as it controls the accumulation of 2-arachidonoylglycerol (2-AG) at the cannabinoid receptors. ABHD6 accounts for about 4% of 2-AG brain hydrolysis. Together, monoacylglycerol lipase (MAGL), ABHD12, and ABHD6 control about 99% of 2-AG signalling in the brain, and each enzyme exhibits a distinct subcellular distribution, suggesting that they regulate distinct pools of 2-AG in the nervous system. See also * Fatty acid amide hydrolase Fatty acid amide hydrolase or FAAH (, oleamide hydrolase, anandamide amidohydrolase) is a member of the serin ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
ABHD2
Abhydrolase domain-containing protein 2 is a serine hydrolase enzyme that is strongly expressed in human spermatozoa. It is a key controller of sperm hyperactivation, which is a necessary step in allowing sperm to fertilize an egg. It is encoded by the ''ABHD2'' gene. Function In the presence of Progesterone (or Pregnenolone Sulfate,) it cleaves 2-arachidonoylglycerol (2AG) into glycerol and arachidonic acid (AA). 2AG inhibits sperm calcium channel CatSper, and so when ABHD2 removes 2AG calcium flows into the cell through the CatSper channel, leading to hyperactivation. ABHD2 is inhibited by testosterone, (as well as hydrocortisone, and the plant triterpenoids lupeol and pristimerin) which may prevent premature hyperactivation. Structure This gene encodes a protein containing an alpha/beta hydrolase fold, which is a catalytic domain found in a very wide range of enzymes. Alternative splicing of this gene results in two transcript variants encoding the same protein. Role ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Serine Hydrolase
Serine hydrolases are one of the largest known enzyme classes comprising approximately ~200 enzymes or 1% of the genes in the human proteome. A defining characteristic of these enzymes is the presence of a particular serine at the active site, which is used for the hydrolysis of substrates. The hydrolysis of the ester or peptide bond proceeds in two steps. First, the acyl part of the substrate (the acid part of an ester or the part of a peptide ending in a carboxyl group) is transferred to the serine, making a new ester or amide bond and releasing the other part of the substrate (the alcohol of an ester or the part of the peptide ending in an amino group) is released. Later, in a slower step, the bond between the serine and the acyl group is hydrolyzed by water or hydroxide ion, regenerating free enzyme. Unlike other, non-catalytic, serines, the reactive serine of these hydrolases is typically activated by a proton relay involving a catalytic triad consisting of the serine, an acidi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Fatty Acid Amide Hydrolase
Fatty acid amide hydrolase or FAAH (, oleamide hydrolase, anandamide amidohydrolase) is a member of the serine hydrolase family of enzymes. It was first shown to break down anandamide in 1993. In humans, it is encoded by the gene ''FAAH''.; Function FAAH is an integral membrane hydrolase with a single ''N''-terminal transmembrane domain. ''In vitro'', FAAH has esterase and amidase activity. ''In vivo'', FAAH is the principal catabolic enzyme for a class of bioactive lipids called the fatty acid amides (FAAs). Members of the FAAs include: * Anandamide (''N''-arachidonoylethanolamine), an endocannabinoid * 2-arachidonoylglycerol (2-AG), an endocannabinoid. * Other ''N''-acylethanolamines, such as ''N''-oleoylethanolamine and ''N''-palmitoylethanolamine * The sleep-inducing lipid oleamide * The ''N''-acyltaurines, which are agonists of the transient receptor potential (TRP) family of calcium channels. ''FAAH'' knockout mice display highly elevated (>15-fold) levels of ''N'' ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Monoacylglycerol Lipase
Monoacylglycerol lipase (EC 3.1.1.23; systematic name glycerol-ester acylhydrolase, also known as MAG lipase, acylglycerol lipase, MAGL, MGL or MGLL) is an enzyme that, in humans, is encoded by the ''MGLL'' gene. MAGL is a 33-kDa, membrane-associated member of the serine hydrolase superfamily and contains the classical GXSXG consensus sequence common to most serine hydrolases. The catalytic triad has been identified as Ser122, His269, and Asp239. Function Monoacylglycerol lipase catalyzes a reaction that uses water molecules to break the glycerol monoesters of long-chain fatty acids: : hydrolyses glycerol monoesters of long-chain fatty acids It functions together with hormone-sensitive lipase (LIPE) to hydrolyze intracellular triglyceride stores in adipocytes and other cells to fatty acids and glycerol. MGLL may also complement lipoprotein lipase (LPL) in completing hydrolysis of monoglycerides resulting from degradation of lipoprotein triglycerides. Monoacylglycerol lipa ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Neuroblastoma
Neuroblastoma (NB) is a type of cancer that forms in certain types of nerve tissue. It most frequently starts from one of the adrenal glands but can also develop in the neck, chest, abdomen, or spine. Symptoms may include bone pain, a lump in the abdomen, neck, or chest, or a painless bluish lump under the skin. Typically, neuroblastoma occurs due to a genetic mutation occurring during early development. Rarely, it may be due to a mutation inherited from a person's parents. Environmental factors have not been found to be involved. Diagnosis is based on a tissue biopsy. Occasionally, it may be found in a baby by ultrasound during pregnancy. At diagnosis, the cancer has usually already spread. The cancer is divided into low-, intermediate-, and high-risk groups based on a child's age, cancer stage, and what the cancer looks like. Treatment and outcomes depends on the risk group a person is in. Treatments may include observation, surgery, radiation, chemotherapy, or stem cell t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
British Journal Of Pharmacology
The ''British Journal of Pharmacology'' is a biweekly peer-reviewed medical journal covering all aspects of experimental pharmacology. It is published for the British Pharmacological Society by Wiley-Blackwell. It was established in 1946 as the ''British Journal of Pharmacology and Chemotherapy''. The journal obtained its current title in 1968. The current editor-in-chief is Amrita Ahluwalia. Previous editors-in-chief include Ian McGrath, Humphrey Rang, Alan North, Phil Moore, Bill Large, and Tony Birmingham. A sister journal, also published for the British Pharmacological Society by Wiley-Blackwell is the '' British Journal of Clinical Pharmacology''. The journal publishes research papers, review articles, commentaries and correspondence in all fields of pharmacology. It also publishes themed issues, as well as supplements. ''The Concise Guide to PHARMACOLOGY'' The ''Concise Guide to PHARMACOLOGY'' is a supplement of the ''British Journal of Pharmacology'', replacing the "Guide ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Georgetown, Texas
Georgetown is a city in Texas and the county seat of Williamson County, Texas, United States. The population was 67,176 at the 2020 census. It is 30 miles (48 km) north of Austin. Founded in 1875 from four existing colleges, the oldest of which had been founded 35 years earlier, Southwestern University is the oldest university in Texas. It is in Georgetown about one-half mile from the historic square. Georgetown has a notable range of Victorian commercial and residential architecture. In 1976, a local historic ordinance was passed to recognize and protect the significance of the historic central business district. In 1977, the Williamson County Courthouse Historical District, containing some 46 contributing structures, was listed on the National Register of Historic Places. Georgetown is also known as the "Red Poppy" Capital of Texas for the red poppy ''(Papaver rhoeas)'' wildflowers planted throughout the city. Georgetown's Red Poppy Festival, which attracts tens of thou ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Springer Science+Business Media
Springer Science+Business Media, commonly known as Springer, is a German multinational publishing company of books, e-books and peer-reviewed journals in science, humanities, technical and medical (STM) publishing. Originally founded in 1842 in Berlin, it expanded internationally in the 1960s, and through mergers in the 1990s and a sale to venture capitalists it fused with Wolters Kluwer and eventually became part of Springer Nature in 2015. Springer has major offices in Berlin, Heidelberg, Dordrecht, and New York City. History Julius Springer founded Springer-Verlag in Berlin in 1842 and his son Ferdinand Springer grew it from a small firm of 4 employees into Germany's then second largest academic publisher with 65 staff in 1872.Chronology ". Springer Science+Business Media. In 1964, Springer expanded its business internationally, o ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
