1.
Brain-specific angiogenesis inhibitor 1
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Brain-specific angiogenesis inhibitor 1 is a protein that in humans is encoded by the BAI1 gene. It is a member of the family of receptors. Angiogenesis is controlled by a balance between stimulators and inhibitors of new vessel growth and is suppressed under normal physiologic conditions. Angiogenesis has been shown to be essential for growth and metastasis of solid tumors, BAI1 contains at least one functional p53-binding site within an intron, and its expression has been shown to be induced by wildtype p53. BAI1 is postulated to be a member of the secretin receptor family, an inhibitor of angiogenesis, brain-specific angiogenesis inhibitor 1 has been shown to interact with BAIAP3 and MAGI1. Model organisms have been used in the study of BAI1 function, a conditional knockout mouse line called Bai1tm2aWtsi was generated at the Wellcome Trust Sanger Institute. Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion, additional screens performed, - In-depth immunological phenotyping - in-depth bone and cartilage phenotyping Human ADGRB1 genome location and ADGRB1 gene details page in the UCSC Genome Browser. This article incorporates text from the United States National Library of Medicine, which is in the public domain
2.
Entrez
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The name Entrez was chosen to reflect the spirit of welcoming the public to search the content available from the NLM. Entrez Global Query is a search and retrieval system that provides access to all databases simultaneously with a single query string. Entrez can efficiently retrieve related sequences, structures, and references, the Entrez system can provide views of gene and protein sequences and chromosome maps. Some textbooks are available online through the Entrez system. The Entrez front page provides, by default, access to the global query, all databases indexed by Entrez can be searched via a single query string, supporting boolean operators and search term tags to limit parts of the search statement to particular fields. This returns a unified results page, that shows the number of hits for the search in each of the databases, Entrez also provides a similar interface for searching each particular database and for refining search results. The Limits feature allows the user to narrow a search a web forms interface, the History feature gives a numbered list of recently performed queries. Results of previous queries can be referred to by number and combined via boolean operators, search results can be saved temporarily in a Clipboard. Users with a MyNCBI account can save queries indefinitely and also choose to have updates with new search results e-mailed for saved queries of most databases and it is widely used in the field of biotechnology as a reference tool for students and professionals alike. Entrez searches the following databases, PubMed, biomedical literature citations and abstracts, including Medline - articles from journals, in addition to using the search engine forms to query the data in Entrez, NCBI provides the Entrez Programming Utilities for more direct access to query results. The eUtils are accessed by posting specially formed URLs to the NCBI server, there was also an eUtils SOAP interface which was terminated on July 2015. In 1991, entrez was introduced in CD form, in 1993, a client-server version of the software provided connectivity with the internet. In 1994, NCBI established a website, and Entrez was a part of initial release. In 2001, Entrez bookshelf was released and in 2003, the Entrez Gene database was developed, Entrez search engine form Entrez Help
3.
National Center for Biotechnology Information
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The National Center for Biotechnology Information is part of the United States National Library of Medicine, a branch of the National Institutes of Health. The NCBI is located in Bethesda, Maryland and was founded in 1988 through legislation sponsored by Senator Claude Pepper, the NCBI houses a series of databases relevant to biotechnology and biomedicine and is an important resource for bioinformatics tools and services. Major databases include GenBank for DNA sequences and PubMed, a database for the biomedical literature. Other databases include the NCBI Epigenomics database, all these databases are available online through the Entrez search engine. NCBI is directed by David Lipman, one of the authors of the BLAST sequence alignment program. He also leads a research program, including groups led by Stephen Altschul, David Landsman, Eugene Koonin, John Wilbur, Teresa Przytycka. NCBI is listed in the Registry of Research Data Repositories re3data. org, NCBI has had responsibility for making available the GenBank DNA sequence database since 1992. GenBank coordinates with individual laboratories and other databases such as those of the European Molecular Biology Laboratory. Since 1992, NCBI has grown to other databases in addition to GenBank. The NCBI assigns a unique identifier to each species of organism, the NCBI has software tools that are available by WWW browsing or by FTP. For example, BLAST is a sequence similarity searching program, BLAST can do sequence comparisons against the GenBank DNA database in less than 15 seconds. RAG2/IL2RG The NCBI Bookshelf is a collection of freely accessible, downloadable, some of the books are online versions of previously published books, while others, such as Coffee Break, are written and edited by NCBI staff. BLAST is a used for calculating sequence similarity between biological sequences such as nucleotide sequences of DNA and amino acid sequences of proteins. BLAST is a tool for finding sequences similar to the query sequence within the same organism or in different organisms. It searches the query sequence on NCBI databases and servers and post the results back to the browser in chosen format. Input sequences to the BLAST are mostly in FASTA or Genbank format while output could be delivered in variety of such as HTML, XML formatting. HTML is the output format for NCBIs web-page. Entrez is both indexing and retrieval system having data from sources for biomedical research
4.
UniProt
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UniProt is a freely accessible database of protein sequence and functional information, many entries being derived from genome sequencing projects. It contains an amount of information about the biological function of proteins derived from the research literature. The UniProt consortium comprises the European Bioinformatics Institute, the Swiss Institute of Bioinformatics, EBI, located at the Wellcome Trust Genome Campus in Hinxton, UK, hosts a large resource of bioinformatics databases and services. SIB, located in Geneva, Switzerland, maintains the ExPASy servers that are a resource for proteomics tools. In 2002, EBI, SIB, and PIR joined forces as the UniProt consortium, each consortium member is heavily involved in protein database maintenance and annotation. Until recently, EBI and SIB together produced the Swiss-Prot and TrEMBL databases and these databases coexisted with differing protein sequence coverage and annotation priorities. Swiss-Prot aimed to provide reliable protein sequences associated with a level of annotation. Recognizing that sequence data were being generated at a pace exceeding Swiss-Prots ability to keep up, meanwhile, PIR maintained the PIR-PSD and related databases, including iProClass, a database of protein sequences and curated families. The consortium members pooled their resources and expertise, and launched UniProt in December 2003. UniProt provides four core databases, UniProtKB, UniParc, UniRef, UniProt Knowledgebase is a protein database partially curated by experts, consisting of two sections, UniProtKB/Swiss-Prot and UniProtKB/TrEMBL. As of 19 March 2014, release 2014_03 of UniProtKB/Swiss-Prot contains 542,782 sequence entries, UniProtKB/Swiss-Prot is a manually annotated, non-redundant protein sequence database. It combines information extracted from literature and biocurator-evaluated computational analysis. The aim of UniProtKB/Swiss-Prot is to all known relevant information about a particular protein. Annotation is regularly reviewed to keep up with current scientific findings, the manual annotation of an entry involves detailed analysis of the protein sequence and of the scientific literature. Sequences from the gene and the same species are merged into the same database entry. Differences between sequences are identified, and their cause documented, a range of sequence analysis tools is used in the annotation of UniProtKB/Swiss-Prot entries. Computer-predictions are manually evaluated, and relevant results selected for inclusion in the entry and these predictions include post-translational modifications, transmembrane domains and topology, signal peptides, domain identification, and protein family classification. Relevant publications are identified by searching databases such as PubMed, the full text of each paper is read, and information is extracted and added to the entry
5.
Locus (genetics)
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A locus in genetics is the position on a chromosome. Each chromosome carries many genes, humans estimated haploid protein coding genes are 19, 000-20,000, a variant of the similar DNA sequence located at a given locus is called an allele. The ordered list of known for a particular genome is called a gene map. Gene mapping is the process of determining the locus for a biological trait. The chromosomal locus of a gene might be written 3p22.1, here 3 means chromosome 3, p means p-arm. And 22 refers to region 2, band 2 and this is read as two two, not as twenty-two. So the entire locus is read as three P two two point one, the cytogenetic bands are counting from the centromere out toward the telomeres. A range of loci is specified in a similar way. For example, the locus of gene OCA1 may be written 11q1. 4-q2.1, meaning it is on the arm of chromosome 11. The ends of a chromosome are labeled pter and qter, a centisome is defined as 1% of a chromosome length. Chromosomal translocation Cytogenetic notation Karyotype Null allele Michael, R. Cummings, belmont, California, Brooks/Cole Overview at ornl. gov Chromosome Banding and Nomenclature from NCBI
6.
Chromosome 8 (human)
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Chromosome 8 is one of the 23 pairs of chromosomes in humans. People normally have two copies of this chromosome, chromosome 8 spans about 145 million base pairs and represents between 4.5 and 5. 0% of the total DNA in cells. Identifying genes on each chromosome is an area of genetic research. Because researchers use different approaches to genome annotation their predictions of the number of genes on each chromosome varies, in January 2017, two estimates differed by 5%, with one estimate giving 2,152 genes, and the other estimate giving 2,047 genes. About 8% of its genes are involved in development and function. A unique feature of 8p is a region of about 15 megabases that appears to have a mutation rate. This region shows an significant divergence between human and chimpanzee, suggesting that its high rates have contributed to the evolution of the human brain. The following are some of the located on chromosome 8, AEG1, Astrocyte Elevated Gene ANK1, ankyrin 1
7.
Brain-specific angiogenesis inhibitor 2
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Brain-specific angiogenesis inhibitor 2 is a protein that in humans is encoded by the BAI2 gene. It is a member of the family of receptors. BAI1, a gene, encodes brain-specific angiogenesis inhibitor, a seven-span transmembrane protein and is thought to be a member of the secretin receptor family. Brain-specific angiogenesis proteins BAI2 and BAI3 are similar to BAI1 in structure, have similar tissue specificities, human ADGRB2 genome location and ADGRB2 gene details page in the UCSC Genome Browser. Kreienkamp HJ, Zitzer H, Gundelfinger ED, et al, the calcium-independent receptor for alpha-latrotoxin from human and rodent brains interacts with members of the ProSAP/SSTRIP/Shank family of multidomain proteins. Kee HJ, Koh JT, Kim MY, et al, expression of brain-specific angiogenesis inhibitor 2 in normal and ischemic brain, involvement of BAI2 in the ischemia-induced brain angiogenesis. Petersen HH, Hilpert J, Militz D, et al, functional interaction of megalin with the megalinbinding protein, a novel tetratrico peptide repeat-containing adaptor molecule. Adkins JN, Varnum SM, Auberry KJ, et al, toward a human blood serum proteome, analysis by multidimensional separation coupled with mass spectrometry. Chromosome 13q12 encoded Rho GTPase activating protein suppresses growth of breast carcinoma cells, ota T, Suzuki Y, Nishikawa T, et al. Complete sequencing and characterization of 21,243 full-length human cDNAs, bjarnadóttir TK, Fredriksson R, Höglund PJ, et al. The human and mouse repertoire of the family of G-protein-coupled receptors. This article incorporates text from the United States National Library of Medicine, which is in the public domain
8.
Chromosome 1 (human)
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Chromosome 1 is the designation for the largest human chromosome. Humans have two copies of chromosome 1, as they do all of the autosomes, which are the non-sex chromosomes. Chromosome 1 spans about 249 million nucleotide pairs, which are the basic units of information for DNA. It represents about 9% of the total DNA in human cells, identifying genes on each chromosome is an active area of genetic research. Because researchers use different approaches to genome annotation their predictions of the number of genes on each chromosome varies, in January 2017, two estimates differed by 12%, with one estimate giving 5,078 genes, and the other estimate giving 4,474 genes. It was the last completed chromosome, sequenced two decades after the beginning of the Human Genome Project, some of these diseases are hearing loss, Alzheimer disease, glaucoma and breast cancer. Rearrangements and mutations of chromosome 1 are prevalent in cancer and many other diseases, patterns of sequence variation reveal signals of recent selection in specific genes that may contribute to human fitness, and also in regions where no function is evident. The following diseases are some of those related to genes on chromosome 1, reuters Wed May 17,2006 Final genome chapter published BBC NEWS
9.
Chromosome 6 (human)
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Chromosome 6 is one of the 23 pairs of chromosomes in humans. People normally have two copies of this chromosome, chromosome 6 spans more than 170 million base pairs and represents between 5.5 and 6% of the total DNA in cells. It contains the Major Histocompatibility Complex, which contains over 100 genes related to the immune response, identifying genes on each chromosome is an active area of genetic research. Because researchers use different approaches to genome annotation their predictions of the number of genes on each chromosome varies, in January 2017, two estimates differed by 16%, with one estimate giving 3,000 genes, and the other estimate giving 2,516 genes. In 2003, the entirety of chromosome 6 was manually annotated for proteins, resulting in the identification of 1,557 genes, the human leukocyte antigen lies on chromosome 6, and encodes cell-surface antigen-presenting proteins among other functions
10.
PubMed Identifier
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PubMed is a free search engine accessing primarily the MEDLINE database of references and abstracts on life sciences and biomedical topics. The United States National Library of Medicine at the National Institutes of Health maintains the database as part of the Entrez system of information retrieval, from 1971 to 1997, MEDLINE online access to the MEDLARS Online computerized database primarily had been through institutional facilities, such as university libraries. PubMed, first released in January 1996, ushered in the era of private, free, home-, the PubMed system was offered free to the public in June 1997, when MEDLINE searches via the Web were demonstrated, in a ceremony, by Vice President Al Gore. Information about the journals indexed in MEDLINE, and available through PubMed, is found in the NLM Catalog. As of 5 January 2017, PubMed has more than 26.8 million records going back to 1966, selectively to the year 1865, and very selectively to 1809, about 500,000 new records are added each year. As of the date,13.1 million of PubMeds records are listed with their abstracts. In 2016, NLM changed the system so that publishers will be able to directly correct typos. Simple searches on PubMed can be carried out by entering key aspects of a subject into PubMeds search window, when a journal article is indexed, numerous article parameters are extracted and stored as structured information. Such parameters are, Article Type, Secondary identifiers, Language, publication type parameter enables many special features. As these clinical girish can generate small sets of robust studies with considerable precision, since July 2005, the MEDLINE article indexing process extracts important identifiers from the article abstract and puts those in a field called Secondary Identifier. The secondary identifier field is to store numbers to various databases of molecular sequence data, gene expression or chemical compounds. For clinical trials, PubMed extracts trial IDs for the two largest trial registries, ClinicalTrials. gov and the International Standard Randomized Controlled Trial Number Register, a reference which is judged particularly relevant can be marked and related articles can be identified. If relevant, several studies can be selected and related articles to all of them can be generated using the Find related data option, the related articles are then listed in order of relatedness. To create these lists of related articles, PubMed compares words from the title and abstract of each citation, as well as the MeSH headings assigned, using a powerful word-weighted algorithm. The related articles function has been judged to be so precise that some researchers suggest it can be used instead of a full search, a strong feature of PubMed is its ability to automatically link to MeSH terms and subheadings. Examples would be, bad breath links to halitosis, heart attack to myocardial infarction, where appropriate, these MeSH terms are automatically expanded, that is, include more specific terms. Terms like nursing are automatically linked to Nursing or Nursing and this important feature makes PubMed searches automatically more sensitive and avoids false-negative hits by compensating for the diversity of medical terminology. The My NCBI area can be accessed from any computer with web-access, an earlier version of My NCBI was called PubMed Cubby
11.
Cell surface receptor
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Cell surface receptors are receptors that are embedded in the membranes of cells. They act in signaling by receiving extracellular molecules. They are specialized integral membrane proteins that allow communication between the cell and the extracellular space, in the process of signal transduction, ligand binding affects a cascading chemical change through the cell membrane. Transmembrane receptors are classified based on their tertiary structure. But, if the structure is yet undiscovered, then they can be classified based on experimentally verifiable membrane topology. The simplest polypeptide chains are found to cross the lipid bilayer once, while others, such as the G-protein coupled receptors, there are various kinds, such as glycoprotein and lipoprotein. Hundreds of different receptors are known and many more have yet to be studied, many membrane receptors include transmembrane proteins. Each cell membrane can have several kinds of receptor, in varying surface distribution. A specific receptor may also be distributed on different membrane surfaces, depending on the membrane sort. Since receptors usually cluster on the surface, the placement of every receptor on each membrane surface is heterogeneous. Two current models have been proposed to explain transmembrane receptors mechanism, dimerization, This dimerization model suggests that prior to ligand binding, receptors exist in a monomeric form. When contact occurs with a ligand, receptors bind together to form a dimer, prior to ligand binding, the extracellular protein loses flexibility while the intracellular portion gains it. Like any integral membrane protein, a receptor may be divided into three domains. The extracellular domain juts externally from the cell or organelle, if the polypeptide chain crosses the bilayer several times, the external domain comprises loops entwined through the membrane. By definition, a main function is to recognize and respond to a type of ligand. For example, a neurotransmitter, hormone, or atomic ions may bind to the extracellular domain as a ligand coupled to receptor. Klotho is an enzyme which effects a receptor to recognize the ligand, in the majority of receptors with known structures, transmembrane alpha helices constitute most of the transmembrane component. In certain receptors, such as the nicotinic receptor, the transmembrane domain forms a protein pore through the membrane
12.
Rhodopsin-like receptors
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Rhodopsin-like receptors are a family of proteins that comprise the largest group of G protein-coupled receptors. G-protein-coupled receptors, GPCRs, constitute a vast protein family that encompasses a range of functions. They show considerable diversity at the level, on the basis of which they can be separated into distinct groups. There is a database for GPCRs. Rhodopsin-like GPCRs have been classified into the following 19 subgroups based on a phylogenetic analysis
13.
Rhodopsin
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Rhodopsin is a light-sensitive receptor protein involved in visual phototransduction. It is named after ancient Greek ῥόδον for “rose”, due to its pinkish color, Rhodopsin is a biological pigment found in the rods of the retina and is a G-protein-coupled receptor. Rhodopsin is extremely sensitive to light, and thus enables vision in low-light conditions, when rhodopsin is exposed to light, it immediately photobleaches. In humans, it is regenerated fully in about 30 minutes, Rhodopsin was discovered by Franz Christian Boll in 1876. Rhodopsin consists of a protein moiety also called scotopsin, which binds covalently a cofactor called retinal, opsins are G protein coupled receptors and have seven transmembrane domains. The seven transmembrane domains form a pocket, where the retinal binds to a residue in the seventh transmembrane domain. The retinal lies horizontally to the cell membrane, and the cell membrane lipid bilayer embeds half of the rhodopsin. Thousands of rhodopsin molecules are found in outer segment disc of the host rod cell. Retinol is produced in the retina from Vitamin A, from dietary beta-carotene, Rhodopsin of the rods most strongly absorbs green-blue light and, therefore, appears reddish-purple, which is why it is also called visual purple. It is responsible for vision in the dark. Several closely related opsins exist that only in a few amino acids. Humans have eight different other opsins besides rhodopsin, as well as cryptochrome, the photopsins are found in the different types of the cone cells of the retina and are the basis of color vision. They have absorption maxima for yellowish-green, green, and bluish-violet light, the remaining opsin is found in photosensitive ganglion cells and absorbs blue light most strongly. In rhodopsin, the group of retinal is covalently linked to the amino group of a lysine residue on the protein in a protonated Schiff base. The intermediates formed during this process were first investigated in the laboratory of George Wald, the photoisomerization dynamics has been subsequently investigated with time-resolved IR spectroscopy and UV/Vis spectroscopy. A first photoproduct called photorhodopsin forms within 200 femtoseconds after irradiation and this intermediate can be trapped and studied at cryogenic temperatures, and was initially referred to as prelumirhodopsin. In subsequent intermediates lumirhodopsin and metarhodopsin I, the Schiffs base linkage to all-trans retinal remains protonated, the structure of rhodopsin has been studied in detail via x-ray crystallography on rhodopsin crystals. Several models attempt to explain how the group can change its conformation without clashing with the enveloping rhodopsin protein pocket
14.
Neurotransmitter receptor
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A neurotransmitter receptor is a membrane receptor protein that is activated by a neurotransmitter. A membrane protein interacts with the bilayer that encloses the cell and a membrane receptor protein interacts with a chemical in the cells external environment. Membrane receptor proteins, in neuronal and glial cells, allow cells to communicate with one another through chemical signals, in postsynaptic cells, neurotransmitter receptors receive signals that trigger an electrical signal, by regulating the activity of ion channels. The influx of ions through ion channels opened due to the binding of neurotransmitters to specific receptors can change the potential of a neuron. This can result in a signal that runs along the axon and is passed along at a synapse to another neuron, on presynaptic cells, there can be receptor sites specific to the neurotransmitters released by that cell, which provide feedback and mediate excessive neurotransmitter release from it. There are two types of receptors, ligand-gated receptors or ionotropic receptors and G protein-coupled receptors or metabotropic receptors. Ligand-gated receptors can be excited by neurotransmitters like glutamate and aspartate and these receptors can also be inhibited by neurotransmitters like GABA and glycine. Conversely, G protein-coupled receptors are neither excitatory nor inhibitory, rather, they modulate the actions of excitatory and inhibitory neurotransmitters. Most neurotransmitters receptors are G-protein coupled, ligand-gated ion channels are one type of ionotropic receptor or channel-linked receptor. They are a group of ion channels that are opened or closed in response to the binding of a chemical messenger. The binding site of endogenous ligands on LGICs protein complexes are located on a different portion of the protein compared to where the ion conduction pore is located. LGICs are also different from voltage-gated ion channels, and stretch-activated ion channels, G protein-coupled receptors are found only in eukaryotes, including yeast, choanoflagellates, and animals. G protein-coupled receptors are involved in diseases, and are also the target of approximately 30% of all modern medicinal drugs. There are two principal signal transduction pathways involving the G protein-coupled receptors, the signal pathway and the phosphatidylinositol signal pathway. When a ligand binds to the GPCR it causes a change in the GPCR. The GPCR can then activate an associated G-protein by exchanging its bound GDP for a GTP, Neurotransmitter receptors are subject to ligand-induced desensitization, That is, they can become unresponsive upon prolonged exposure to their neurotransmitter. In addition to being found in cells, neurotransmitter receptors are also found in various immune. Many neurotransmitter receptors are categorized as a receptor or G protein-coupled receptor because they span the cell membrane not once
15.
Adrenergic receptor
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The adrenergic receptors are a class of G protein-coupled receptors that are targets of the catecholamines, especially norepinephrine and epinephrine. Many cells possess these receptors, and the binding of a catecholamine to the receptor will generally stimulate the nervous system. By the turn of the 19th century, it was agreed that the stimulation of sympathetic nerves could cause different effects on body tissues, the second hypothesis found support from 1906 to 1913, when Henry Dale explored the effects of adrenaline, injected into animals, on blood pressure. Usually, adrenaline would increase the pressure of these animals. Although, if the animal had been exposed to ergotoxine, the pressure decreased. This mixed response, with the same compound causing either contraction or relaxation, was conceived of as the response of different types of junctions to the same compound and this again supported the argument that the muscles had two different mechanisms by which they could respond to the same compound. In June of that year, Raymond Ahlquist, Professor of Pharmacology at Medical College of Georgia, in it, he explicitly named the different responses as due to what he called α receptors and β receptors, and that the only sympathetic transmitter was adrenaline. While the latter conclusion was subsequently shown to be incorrect, his receptor nomenclature, there are two main groups of adrenergic receptors, α and β, with several subtypes. α receptors have the subtypes α1 and α2, phenylephrine is a selective agonist of the α receptor. β receptors have the subtypes β1, β2 and β3, all three are linked to Gs proteins, which in turn are linked to adenylate cyclase. Agonist binding thus causes a rise in the concentration of the second messenger cAMP. Downstream effectors of cAMP include cAMP-dependent protein kinase, which some of the intracellular events following hormone binding. Epinephrine reacts with both α- and β-adrenoreceptors, causing vasoconstriction and vasodilation, respectively, the result is that high levels of circulating epinephrine cause vasoconstriction. At lower levels of circulating epinephrine, β-adrenoreceptor stimulation dominates, producing vasodilation followed by decrease of peripheral vascular resistance, Smooth muscle behavior is variable depending on anatomical location. Smooth muscle contraction/relaxation is generalized below, one important note is the differential effects of increased cAMP in smooth muscle compared to cardiac muscle. Increased cAMP will promote relaxation in smooth muscle, while promoting increased contractility, at one time, there was a subtype known as C, but was found to be identical to one of the previously discovered subtypes. To avoid confusion, naming was continued with the letter D. α receptors have several functions in common, common effects include, Vasoconstriction of veins Decrease motility of smooth muscle in gastrointestinal tract α1-adrenergic receptors are members of the Gq protein-coupled receptor superfamily. Upon activation, a heterotrimeric G protein, Gq, activates phospholipase C, the PLC cleaves phosphatidylinositol 4, 5-bisphosphate, which in turn causes an increase in inositol triphosphate and diacylglycerol
16.
Alpha-1A adrenergic receptor
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The alpha-1A adrenergic receptor, also known as ADRA1A, formerly known also as the alpha-1C adrenergic receptor, is an alpha-1 adrenergic receptor, and also denotes the human gene encoding it. There is no longer a subtype α1C receptor, at one time, there was a subtype known as α1C, but it was found to be identical to the previously discovered α1A receptor subtype. To avoid confusion, the convention was continued with the letter D. There are 3 alpha-1 adrenergic receptor subtypes, alpha-1A, -1B and -1D, different subtypes show different patterns of activation. The majority of receptors are directed toward the function of epinephrine. This gene encodes the alpha-1A-adrenergic receptor, alternative splicing of this gene generates four transcript variants, which encode four different isoforms with distinct C-termini but having similar ligand binding properties. IUPHAR Database of Receptors and Ion Channels, international Union of Basic and Clinical Pharmacology. Human ADRA1A genome location and ADRA1A gene details page in the UCSC Genome Browser
17.
Alpha-1B adrenergic receptor
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The alpha-1B adrenergic receptor, also known as ADRA1B, is an alpha-1 adrenergic receptor, and also denotes the human gene encoding it. There are 3 alpha-1 adrenergic receptor subtypes, alpha-1A, -1B and -1D, all of which signal through the Gq/11 family of G-proteins and they activate mitogenic responses and regulate growth and proliferation of many cells. This gene encodes alpha-1B-adrenergic receptor, which induces neoplastic transformation when transfected into NIH 3T3 fibroblasts, thus, this normal cellular gene is identified as a protooncogene. This gene comprises 2 exons and a large intron of at least 20 kb that interrupts the coding region. Antagonists L-765,314 Risperidone Alpha-1B adrenergic receptor has shown to interact with AP2M1. A role in regulation of dopaminergic neurotransmission has also been suggested, adrenergic receptor Human ADRA1B genome location and ADRA1B gene details page in the UCSC Genome Browser
18.
Alpha-1D adrenergic receptor
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The alpha-1D adrenergic receptor, also known as ADRA1D, is an alpha-1 adrenergic receptor, and also denotes the human gene encoding it. There are 3 alpha-1 adrenergic receptor subtypes, alpha-1A, -1B and -1D, all of which signal through the Gq/11 family of G-proteins and they activate mitogenic responses and regulate growth and proliferation of many cells. Similar to alpha-1B-adrenergic receptor gene, this gene comprises 2 exons, antagonists A-315456 BMY7378 Adrenergic receptor Human ADRA1A genome location and ADRA1A gene details page in the UCSC Genome Browser. Human ADRA1D genome location and ADRA1D gene details page in the UCSC Genome Browser
19.
Alpha-2A adrenergic receptor
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The alpha-2A adrenergic receptor, also known as ADRA2A, is an α2 adrenergic receptor, and also denotes the human gene encoding it. α2 adrenergic receptors include 3 highly homologous subtypes, α2A, α2B and these receptors have a critical role in regulating neurotransmitter release from sympathetic nerves and from adrenergic neurons in the central nervous system. This gene encodes α2A subtype and it contains no introns in either its coding or untranslated sequences, many post-synaptic α2A receptors have important effects on brain function, for example, α2A receptors are localized on prefrontal cortical neurons where they regulate higher cognitive function. Clonidine Lofexidine Dexmedetomidine Guanfacine Asenapine BRL-44408 Clozapine Lurasidone Mianserin Mirtazapine Paliperidone Risperidone Yohimbine Adrenergic receptor α2A-adrenoceptor, IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology, human ADRA2A genome location and ADRA2A gene details page in the UCSC Genome Browser. Human ZNF32 genome location and ZNF32 gene details page in the UCSC Genome Browser
20.
Beta-1 adrenergic receptor
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The beta-1 adrenergic receptor, also known as ADRB1, is a beta-adrenergic receptor, and also denotes the human gene encoding it. It is a G-protein coupled receptor associated with the Gs heterotrimeric G-protein and is expressed predominantly in cardiac tissue, increases contractility and automaticity of ventricular cardiac muscle. Increases conduction and automaticity of atrioventricular node Renin release from juxtaglomerular cells, relaxation of the urinary bladder wall Receptor also present in cerebral cortex. Isoprenaline has higher affinity for β1 than adrenaline, which, in turn, specific polymorphisms in the ADRB1 gene have been shown to affect the resting heart rate and can be involved in heart failure. Beta-1 adrenergic receptor has shown to interact with DLG4 and GIPC1. Interaction between testosterone and β-1 ARs have been shown in anxiolytic behaviors in the basolateral amygdala, IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology
21.
Beta-2 adrenergic receptor
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Unlike other adrenergic receptors, norepinephrine does not produce β2 receptor stimulation. The official symbol for the gene encoding the β2 adrenoreceptor is ADRB2. Different polymorphic forms, point mutations, and/or downregulation of gene are associated with nocturnal asthma, obesity. An alternative method, involving production of a protein with an agonist. This receptor is associated with one of its ultimate effectors. Protein kinase A then goes on to phosphorylate myosin light chain kinase, the assembly of the signaling complex provides a mechanism that ensures specific and rapid signaling. A two-state biophysical and molecular model has been proposed to account for the pH and REDOX sensitivity of this, beta-2 Adrenergic Receptors have also been found to couple with Gs, possibly providing a mechanism by which response to ligand is highly localized within cells. In contrast, Beta-1 Adrenergic Receptors are coupled only to Gs and this appears to be mediated by cAMP induced PKA phosphorylation of the receptor. Actions of the β2 receptor include, Heart muscle contraction Increases cardiac output, Increases heart rate in sinoatrial node. Increases contractility and automaticity of ventricular cardiac muscle, in glaucoma, drainage is reduced or blocked completely. In such cases, beta-2 stimulation with its consequent increase in production is highly contra-indicated, and conversely. Glycogenolysis and lactate release in skeletal muscle, insulin secretion from pancreas Inhibit histamine-release from mast cells. Increase protein content of secretions from lacrimal glands, bronchiole dilation Involved in brain - immune - communication butoxamine* First generation β-blockers ICI-118,551 * denotes selective agonists to the receptor. IUPHAR Database of Receptors and Ion Channels, international Union of Basic and Clinical Pharmacology. Human ADRB2 genome location and ADRB2 gene details page in the UCSC Genome Browser
22.
Beta-3 adrenergic receptor
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The beta-3 adrenergic receptor, also known as ADRB3, is a beta-adrenergic receptor, and also denotes the human gene encoding it. Actions of the β3 receptor include Enhancement of lipolysis in adipose tissue, thermogenesis in skeletal muscle It is located mainly in adipose tissue and is involved in the regulation of lipolysis and thermogenesis. Some β3 agonists have demonstrated antistress effects in studies, suggesting it also has a role in the central nervous system. β3 receptors are found in the gallbladder, urinary bladder, and their role in gallbladder physiology is unknown, but they are thought to play a role in lipolysis and thermogenesis in brown fat. In the urinary bladder it is thought to cause relaxation of the bladder, Beta adrenergic receptors are involved in the epinephrine- and norepinephrine-induced activation of adenylate cyclase through the action of the G proteins of the type Gs. Amibegron CL-316,243 L-742,791 L-796,568 LY-368,842 Mirabegron, approved for treatment of overactive bladder in Japan, United States, UK, Canada, China and India. Ro40-2148 Solabegron Vibegron L-748,328 L-748,337 SR 59230A was thought to be a selective β3 antagonist, beta-3 adrenergic receptor has been shown to interact with Src. Other adrenergic receptors Alpha-1 adrenergic receptor Alpha-2 adrenergic receptor Beta-1 adrenergic receptor Beta-2 adrenergic receptor Beta Blocker β3-adrenoceptor, IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology, human ADRB3 genome location and ADRB3 gene details page in the UCSC Genome Browser
23.
Purinergic receptor
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Purinergic receptors, also known as purinoceptors, are a family of plasma membrane molecules that are found in almost all mammalian tissues. Within the field of purinergic signalling, these receptors have been implicated in learning and memory, locomotor and feeding behavior, more specifically, they are involved in several cellular functions, including proliferation and migration of neural stem cells, vascular reactivity, apoptosis and cytokine secretion. These functions have not been characterized and the effect of the extracellular microenvironment on their function is also poorly understood. P2 receptors have further divided into five subclasses, P2X, P2Y, P2Z, P2U. To distinguish P2 receptors further, the subclasses have been divided into families of metabotropic and ionotropic receptors, in 2014, the first purinergic receptor in plants, DORN1, was discovered. There are three distinct classes of purinergic receptors, known as P1, P2X, and P2Y receptors. P2X receptors are ligand-gated ion channels, whereas the P1 and P2Y receptors are G protein-coupled receptors and these ligand-gated ion channels are nonselective cation channels responsible for mediating excitatory postsynaptic responses, similar to nicotinic and ionotropic glutamate receptors. These receptors are greatly distributed in neurons and glial cells throughout the central and peripheral nervous systems, P2X receptors mediate a large variety of responses including fast transmission at central synapses, contraction of smooth muscle cells, platelet aggregation, macrophage activation, and apoptosis. Both of these receptors are distinguished by their reactivity to specific activators. P1 receptors are activated by adenosine and P2Y receptors are preferentially more activated by ATP. P1 and P2Y receptors are known to be distributed in the brain, heart, kidneys. Xanthines specifically block adenosine receptors, and are known to induce an effect to ones behavior. Inhibitors of purinergic receptors include clopidogrel, prasugrel and ticlopidine, as well as ticagrelor, all of these are antiplatelet agents that block P2Y12 receptors. Data obtained from using P2 receptor-selective antagonists has produced evidence supporting ATPs ability to initiate and this recent knowledge of purinergic receptors effects on chronic pain provide promise in discovering a drug that specifically targets individual P2 receptor subtypes. While some P2 receptor-selective compounds have proven useful in preclinical trials, recent research has identified a role for microglial P2X receptors in neuropathic pain and inflammatory pain, especially the P2X4 and P2X7 receptors. Purinergic receptors have been suggested to play a role in the treatment of cytotoxic edema, further pharmacological evidence has suggested that 2MeSADP protection is controlled by enhanced astrocyte mitochondrial metabolism through increased inositol triphosphate-dependent calcium release. There is evidence suggesting a relationship between the levels of ATP and cytotoxic edema, where low ATP levels are associated with a prevalence of cytotoxic edema. It is believed that play an essential role in the metabolism of astrocyte energy within the penumbra of ischemic lesions
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Adenosine receptor
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The adenosine receptors are a class of purinergic G protein-coupled receptors with adenosine as endogenous ligand. In humans, there are four types of adenosine receptors, each is encoded by a separate gene and has different functions, although with some overlap. The adenosine A1 receptor has been found to be throughout the entire body. This receptor has a function on most of the tissues in which it is expressed. In the brain, it slows metabolic activity by a combination of actions, presynaptically, it reduces synaptic vesicle release while post synaptically it has been found to stabilize the magnesium on the NMDA receptor. Specific A1 antagonists include 8-Cyclopentyl-1, 3-dipropylxanthine, and Cyclopentyltheophylline or 8-cyclopentyl-1, 3-dipropylxanthine, tecadenoson is an effective A1 adenosine agonist, as is selodenoson. The A1, together with A2A receptors of endogenous adenosine play a role in regulating myocardial oxygen consumption, stimulation of the A1 receptor has a myocardial depressant effect by decreasing the conduction of electrical impulses and suppressing pacemaker cell function, resulting in a decrease in heart rate. This makes adenosine a useful medication for treating and diagnosing tachyarrhythmias and this effect on the A1 receptor also explains why there is a brief moment of cardiac standstill when adenosine is administered as a rapid IV push during cardiac resuscitation. The rapid infusion causes a momentary myocardial stunning effect, in normal physiological states, this serves as a protective mechanism. Theophylline and caffeine are nonselective adenosine antagonists that are used to stimulate respiration in premature infants, adenosine receptors play a key role in the homeostasis of bone. The A1 receptor has shown to stimulate osteoclast differentiation and function. Studies have found that blockade of the A1 Receptor suppresses the osteoclast function, as with the A1, the A2A receptors are believed to play a role in regulating myocardial oxygen consumption and coronary blood flow. The activity of A2A adenosine receptor, a G-protein coupled receptor family member, is mediated by G proteins that activate adenylyl cyclase and it is abundant in basal ganglia, vasculature and platelets and it is a major target of caffeine. The A2A receptor is responsible for regulating blood flow by vasodilating the coronary arteries, which increases blood flow to the myocardium. Just as in A1 receptors, this serves as a protective mechanism. Specific antagonists include istradefylline and SCH-58261, while specific agonists include CGS-21680, the role of A2A receptor opposes that of A1 in that it inhibits osteoclast differentiation and activates osteoblasts. Studies have shown it to be effective in decreasing inflammatory osteolysis in inflamed bone and this role could potentiate new therapeutic treatment in aid of bone regeneration and increasing bone volume. This integral membrane protein stimulates adenylate cyclase activity in the presence of adenosine and this protein also interacts with netrin-1, which is involved in axon elongation
25.
Adenosine A1 receptor
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The adenosine A1 receptor is one member of the adenosine receptor group of G protein-coupled receptors with adenosine as endogenous ligand. A1 receptors are implicated in sleep promotion by inhibiting wake-promoting cholinergic neurons in the basal forebrain, A1 receptors are also present in smooth muscle throughout the vascular system. The adenosine A1 receptor has been found to be throughout the entire body. Activation of the adenosine A1 receptor by an agonist causes binding of Gi1/2/3 or Go protein, binding of Gi1/2/3 causes an inhibition of adenylate cyclase and, therefore, a decrease in the cAMP concentration. Several types of channels are activated but N-, P-. This receptor has a function on most of the tissues in which it rests. In the brain, it slows metabolic activity by a combination of actions, at the neurons synapse, it reduces synaptic vesicle release. Caffeine, as well as theophylline, has found to antagonize both A1 and A2A receptors in the brain. N6-Cyclopentyladenosine N-cyclohexyladenosine Tecadenoson is an effective A1 adenosine agonist, as is selodenoson, stimulation of the A1 receptor has a myocardial depressant effect by decreasing the conduction of electrical impulses and suppressing pacemaker cell function, resulting in a decrease in heart rate. This makes adenosine a useful medication for treating and diagnosing tachyarrhythmias and this effect on the A1 receptor also explains why there is a brief moment of cardiac standstill when adenosine is administered as a rapid IV push during cardiac resuscitation. The rapid infusion causes a momentary myocardial stunning effect, in normal physiological states, this serves as protective mechanisms. Theophylline and caffeine are nonselective adenosine antagonists that are used to stimulate respiration in premature infants, however, we are unaware of clinical studies that have examined the incidence of periventricular leukomalacia as related to neonatal caffeine use. Caffeine may reduce blood flow in premature infants, it is presumed by blocking vascular A2 ARs. Thus, it may prove advantageous to use selective A1 antagonists to help reduce adenosine-induced brain injury. IUPHAR Database of Receptors and Ion Channels, international Union of Basic and Clinical Pharmacology. Adenosine A1 Receptor at the US National Library of Medicine Medical Subject Headings Human ADORA1 genome location and ADORA1 gene details page in the UCSC Genome Browser
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Adenosine A2A receptor
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The adenosine A2A receptor, also known as ADORA2A, is an adenosine receptor, and also denotes the human gene encoding it. This protein is a member of the G protein-coupled receptor family which possess seven transmembrane alpha helices, the crystallographic structure of the adenosine A2A receptor reveals a ligand binding pocket distinct from that of other structurally determined GPCRs. The receptors role in immunomodulation in the context of cancer has suggested that it is an important immune checkpoint molecule, the gene encodes a protein which is one of several receptor subtypes for adenosine. The activity of the protein, a G protein-coupled receptor family member, is mediated by G proteins which activate adenylyl cyclase. The encoded protein is abundant in basal ganglia, vasculature, T lymphocytes, and platelets and it is a target of caffeine. As with the A1, the A2A receptors are believed to play a role in regulating myocardial oxygen consumption, in addition, A2A receptor can negatively regulate overreactive immune cells, thereby protecting tissues from collateral inflammatory damage. The A2A receptor is responsible for regulating blood flow by vasodilating the coronary arteries, which increases blood flow to the myocardium. Just as in A1 receptors, this serves as a protective mechanism. A number of selective A2A ligands have been developed, with possible therapeutic applications. Adenosine A2A receptor has shown to interact with Dopamine receptor D2. As a result, Adenosine receptor A2A decreases activity in the Dopamine D2 receptors, human ADORA2A genome location and ADORA2A gene details page in the UCSC Genome Browser
27.
Adenosine A2B receptor
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The adenosine A2B receptor, also known as ADORA2B, is a G-protein coupled adenosine receptor, and also denotes the human adenosine A2b receptor gene which encodes it. This integral membrane protein stimulates adenylate cyclase activity in the presence of adenosine and this protein also interacts with netrin-1, which is involved in axon elongation. The gene is located near the Smith-Magenis syndrome region on chromosome 17, IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology, human ADORA2B genome location and ADORA2B gene details page in the UCSC Genome Browser
28.
Adenosine A3 receptor
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The adenosine A3 receptor, also known as ADORA3, is an adenosine receptor, but also denotes the human gene encoding it. Adenosine A3 receptors are G protein-coupled receptors that couple to Gi/Gq and are involved in a variety of signaling pathways. Recent publications demonstrate that adenosine A3 receptor antagonists could have potential in bronchial asthma. Multiple transcript variants encoding different isoforms have been found for this gene, an adenosine A3 receptor agonist is in clinical trials for the treatment of rheumatoid arthritis. In a mouse model of infarction the A3 selective agonist CP-532,903 protected against myocardial ischemia, a number of selective A3 ligands are available. IUPHAR Database of Receptors and Ion Channels, international Union of Basic and Clinical Pharmacology. Human ADORA3 genome location and ADORA3 gene details page in the UCSC Genome Browser
29.
P2Y receptor
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P2Y receptors are a family of purinergic G protein-coupled receptors, stimulated by nucleotides such as ATP, ADP, UTP, UDP and UDP-glucose. To date,8 P2Y receptors have been cloned in humans, P2Y1, P2Y2, P2Y4, P2Y6, P2Y11, P2Y12, P2Y13, P2Y receptors are present in almost all human tissues where they exert various biological functions based on their G-protein coupling. The biological effects of P2Y receptor activation depends on how they couple to downstream signalling pathways, either via Gi, P2Y2 is a potential drug target for treating cystic fibrosis. P2Y12 is the target of the anti-platelet drug clopidogrel and other thienopyridines, ivar von Kügelgen, Pharmacology of mammalian P2X- and P2Y-receptors, BIOTREND Reviews No. 03, September 2008, ©2008 BIOTREND Chemicals AG P2Y Receptors, IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology, purinergic P2 receptors at the US National Library of Medicine Medical Subject Headings
30.
P2RY1
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P2Y purinoceptor 1 is a protein that in humans is encoded by the P2RY1 gene. The product of gene, P2Y1 belongs to the family of G-protein coupled receptors. This family has several subtypes with different pharmacological selectivity, which overlaps in some cases. This receptor functions as a receptor for extracellular ATP and ADP, in platelets binding to ADP leads to mobilization of intracellular calcium ions via activation of phospholipase C, a change in platelet shape, and probably to platelet aggregation. IUPHAR Database of Receptors and Ion Channels, international Union of Basic and Clinical Pharmacology. This article incorporates text from the United States National Library of Medicine, which is in the public domain
31.
P2RY2
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P2Y purinoceptor 2 is a protein that in humans is encoded by the P2RY2 gene. The product of gene, P2Y2 belongs to the family of G-protein coupled receptors. This family has several subtypes with different pharmacological selectivity, which overlaps in some cases. This receptor is responsive to both adenosine and uridine nucleotides and it may participate in control of the cell cycle of endometrial carcinoma cells. Three transcript variants encoding the protein have been identified for this gene. P2Y receptor Denufosol, a P2Y2 agonist P2Y Receptors, P2Y2, IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology and this article incorporates text from the United States National Library of Medicine, which is in the public domain
32.
P2RY4
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P2Y purinoceptor 4 is a protein that in humans is encoded by the P2RY4 gene. The product of gene, P2Y4, belongs to the family of G-protein coupled receptors. This family has several subtypes with different pharmacological selectivity, which overlaps in some cases. This receptor is responsive to uridine nucleotides, partially responsive to ATP, IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology and this article incorporates text from the United States National Library of Medicine, which is in the public domain
33.
LPAR6
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Lysophosphatidic acid receptor 6 also known as LPA6, P2RY5, and GPR87, is a protein that in humans is encoded by the LPAR6 gene. LPA6 is a G protein-coupled receptor that binds the lipid signaling molecule lysophosphatidic acid, the protein encoded by this gene belongs to the family of G-protein coupled receptors, that are preferentially activated by adenosine and uridine nucleotides. This gene aligns with an internal intron of the retinoblastoma susceptibility gene in the reverse orientation, in February 2008 researchers at the University of Bonn announced they have found the genetic basis of two distinct forms of inherited hair loss, opening a broad path to treatments for baldness. They found that mutations in the gene P2RY5 causes a rare and it is the first receptor in humans known to play a role in hair growth. Lysophospholipid receptor P2Y receptor LPAR6 human gene location in the UCSC Genome Browser, LPAR6 human gene details in the UCSC Genome Browser. This article incorporates text from the United States National Library of Medicine, which is in the public domain
34.
P2RY6
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P2Y purinoceptor 6 is a protein that in humans is encoded by the P2RY6 gene. The product of gene, P2Y6, belongs to the family of G-protein coupled receptors. This family has several subtypes with different pharmacological selectivity, which overlaps in some cases. This receptor is responsive to UDP, partially responsive to UTP and ADP, four transcript variants encoding the same isoform have been identified for this gene. IUPHAR Database of Receptors and Ion Channels, international Union of Basic and Clinical Pharmacology. This article incorporates text from the United States National Library of Medicine, which is in the public domain
35.
P2RY8
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P2Y purinoceptor 8 is a protein that in humans is encoded by the P2RY8 gene. The protein encoded by this gene belongs to the family of G-protein coupled receptors and this gene is moderately expressed in undifferentiated HL60 cells, and is located on both chromosomes X and Y. Recurrent mutations in this gene have been associated to cases of diffuse large B-cell lymphoma, p2Y receptor This article incorporates text from the United States National Library of Medicine, which is in the public domain
36.
P2RY11
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P2Y purinoceptor 11 is a protein that in humans is encoded by the P2RY11 gene. The product of gene, P2Y11, belongs to the family of G-protein coupled receptors. This family has several subtypes with different pharmacological selectivity, which overlaps in some cases. This receptor is coupled to the stimulation of the phosphoinositide and adenylyl cyclase pathways, naturally occurring read-through transcripts, resulting from intergenic splicing between this gene and an immediately upstream gene, have been found. The PPAN-P2RY11 read-through mRNA is ubiquitously expressed and encodes a protein that shares identity with each individual gene product. IUPHAR Database of Receptors and Ion Channels, international Union of Basic and Clinical Pharmacology. This article incorporates text from the United States National Library of Medicine, which is in the public domain
37.
P2Y12
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In the field of purinergic signaling, the P2Y12 protein is found mainly but not exclusively on the surface of blood platelets, and is an important regulator in blood clotting. P2Y12 belongs to the Gi class of a group of G protein-coupled purinergic receptors and is a chemoreceptor for adenosine diphosphate and this P2Y receptor family has several receptor subtypes with different pharmacological selectivity, which overlaps in some cases, for various adenosine and uridine nucleotides. The P2Y12 receptor is involved in platelet aggregation and is thus a target for the treatment of thromboembolisms. Two transcript variants encoding the same isoform have been identified for this gene, the drugs clopidogrel, prasugrel, ticagrelor, and cangrelor bind to this receptor and are marketed as antiplatelet agents. P2Y12 inhibitors do not change the risk of death given as a pretreatment prior to routine percutaneous coronary intervention in people who have had a non-ST-elevation myocardial infarction. Though, a P2Y12 inhibitor in addition to aspirin should be administered for up to 12 months to most patients with acute coronary syndrome. They do however increase the risk of bleeding and decrease the risk of cardiovascular problems. Thus their routine use in context is of questionable value. In patients undergoing primary PCI for an ST-segment elevation myocardial infarction, the use of clopidogrel in particular has been shown to improve morbidity and mortality endpoints including cardiovascular death, recurrent MI, and stroke at 30 days after PCI. IUPHAR Database of Receptors and Ion Channels, international Union of Basic and Clinical Pharmacology. Purinoceptor P2Y12 at the US National Library of Medicine Medical Subject Headings This article incorporates text from the United States National Library of Medicine, which is in the public domain
