[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/all2en\/wiki32\/presstine-proashin-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/all2en\/wiki32\/presstine-proashin-wikipedia\/","headline":"PRESSTINE (PROashin) \u2014 Wikipedia","name":"PRESSTINE (PROashin) \u2014 Wikipedia","description":"before-content-x4 A wikipedia article, free l’encyclop\u00e9i. after-content-x4 The prestine is a protein that is encoded in humans by the gene","datePublished":"2019-09-27","dateModified":"2019-09-27","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/all2en\/wiki32\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/all2en\/wiki32\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/44a4cee54c4c053e967fe3e7d054edd4?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/44a4cee54c4c053e967fe3e7d054edd4?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/fr.wikipedia.org\/wiki\/Special:CentralAutoLogin\/start?type=1x1","url":"https:\/\/fr.wikipedia.org\/wiki\/Special:CentralAutoLogin\/start?type=1x1","height":"1","width":"1"},"url":"https:\/\/wiki.edu.vn\/all2en\/wiki32\/presstine-proashin-wikipedia\/","wordCount":4416,"articleBody":"     (adsbygoogle = window.adsbygoogle || []).push({});before-content-x4A wikipedia article, free l’encyclop\u00e9i.        (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4The prestine is a protein that is encoded in humans by the gene SLC26A5 (solute carrier family 26, member 5) [ first ] , [ 2 ] , located on chromosome 7 [ 3 ] . Different variants of this protein are known in the animal world, all involved in hearing or echolocation. PRESTINE is a motor molecule sensitive to tension. It is notably expressed in external ciliated cells (CCE) of the cochlea and seems essentially to be used for the processing of hearing information. These cells actively modify their length in response to changes in the electrical potential of the membrane. This electromotility (mediated by the membrane prestine) is considered responsible for the cochlear amplification.        (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4It is also (in humans at least) under the control of the thyroid [ 4 ] . They are found in the ovary of mammals [ 5 ] .   PRESTINE seems to play several roles, all more or less necessary for auditory amplification, allowed by one of the two types of hearing receptors (external ciliated cells) of the Corti organ: It is the motor protein that animates the eyelashes of the cochlea in mammals [ first ] . It is strongly expressed in mobile external ciliated cells, and is not in the internal (motionless) hair cells. L’immunolocalisation [ 6 ] shows that prestine is expressed in the lateral plasma membrane of external ciliated cells, the region where electromotility is produced. It is believed that intracellular anions act as Extrinsic tension sensors ; By binding to the prestine, they trigger the necessary conformation changes for quick changes in the length length [ 2 ] . The removal of these anions blocks the dependent motility of rapid voltage differences, and load changes (with non-linear characteristics) can produce “blocking currents” resulting in underlying structural rearrangements of the protein [ 7 ] . In several species gifted with echolocation competence by emission and reception of ultrasound, in water or in air; Cetaceans (Odontoc\u00e8tes in Sonar, excluding Cachalot) and bat, the Prestine is involved in echolocation. The gene that codes for bats and dolphins has undergone the same changes (evolutionary convergence) [ 8 ] . According to the amino acid sequence, the perception of sounds differs. It’s the pygmy sperm whale ( Kogia breviceps ) which would perceive the ultrasound emitted in the highest frequencies. This seems to be linked to the conformations that the external ciliated cell can take in response to electrical or mechanical stimuli (sound wave effect in air or in water). The phylogenetic tree of the Odontoc\u00e8tes reconstituted according to the prestine sequence, suggests that this protein has transferred into 2 phases of evolution fast (a few million years for each phase); In the ancestor common to all the tooth whales about thirty million years ago (the first cetaceans who notably gave the shales to Pams (mystical) were therefore probably not endowed with echolocation). A second phase led to dolphins and beales that we know. These mutations seem to have allowed protein conformations allowing greater contractions and elongations of external hair cells, necessary for the perception of high sound frequencies. PRESTINE (Mol. WT. 80 KDA) is one of the family of anion transporter proteins, SLC26. The members of this family are structurally stable and, through plasma membranes of mammal cells, they can contribute to electroneural exchanges of chlorides and carbonates, two anions which are essential to the motility of the vibratile eyelashes of the inner ear. Unlike the classic organic engine (under enzymatic control), the operation of this new type of biological engine is based on a conversion of electrical potential difference (measurable in volts). It acts at a speed of a few microseconds, a very higher speed (of several orders of magnitude) to that characterizing other known proteins as Cellular motors . The gene inhibition techniques have shown that prestine is an essential link in the mechanical-electric transduction chain of the inner ear. The absence of prestine divides by 100 hearing sensitivity (loss of 40 to 60 dB) [ 9 ] .        (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4The available data confirm the model according to which anions act as extrinsic tension sensors, bind to the prestine molecule and thus trigger the conformational changes necessary for the motility of the CCEs [ 7 ] . The ciliated cells are killed by certain so -called antibiotics ototoxiques And genetically modified mice that are not producing prestine. They made it possible to study the functions of the Prestine, as well as the young gerbilles who are naturally deaf in the week following their birth [ ten ] . The discovery of the prestine was published in the year 2000 by a team led by Peter Dallos [ first ] and named after musical notation Soon . The prestine molecule, although not invented or created by man, was patented by his discoverers in 2003 [ 11 ] . Apart from the mutations of the SLC26A5 gene found in cetaceans and bats, the other changes are candidates to explain neurosensory deafness. Several transcription isoforms coding different variants have been found for this gene [ 2 ] . PRESTINE is a transmembrane protein and an incomplete anion transporter; It does not allow anions to cross the cell membrane, but it rather undergoes a change in conformation in response to changes in the intracellular rate of chlorine, which results in a change in length of the cell. The electromotility functions of the mammalian prestine are blocked by an anion amphiphile (salicylate), at millimolar concentrations, in a dose-dependent, and reversible manner [ 7 ] . \u2191 A B and C Zheng J, Shen W, He DZ, Long KB, Madison LD, Dallos P, \u00ab\u00a0 Prestin is the motor protein of cochlear outer hair cells \u00bb, Nature , vol. 405, n O 6783, June 2000 , p. 149-55 (PMID\u00a0 10821263 , DOI\u00a0 10.1038\/35012009 , r\u00e9sum\u00e9 )  \u2191 A B and C Entrez Gene: SLC26A5 solute carrier family 26, member 5 (prestin)  \u2191 Hillier LW, Fulton RS, Fulton LA, et al. \u00ab The DNA sequence of human chromosome 7 \u00bb, Nature , vol. 424, n O 6945, 2003 , p. 157\u201364 (PMID\u00a0 12853948 , DOI\u00a0 10.1038\/nature01782 )  \u2191 Weber T, Zimmermann U, Winter H, et al. \u00ab Thyroid hormone is a critical determinant for the regulation of the cochlear motor protein prestin \u00bb, PNAS , vol. 99, n O 5, 2002 , p. 2901\u20136 (PMID\u00a0 11867734 , DOI\u00a0 10.1073\/pnas.052609899 , read online )  \u2191 Koji Iida, Kazuaki Konno, Takesi Oshima, Kouhii TSUMOTO, Katsuhisa Ikeda, Izumi Kumagai, Toshimitsu Kobayashi et Hiroshi Wada Stable Expression of the Motor Protein Prestin in Chinese Hamster Ovary Cells \u00bb, We are the International Journal , vol. 46C, n O 4, 2003 , p. 1266-74  \u2191 Illustration (Oxford Journal), consulted 2010 12 28  \u2191 A B and C Dominik Oliver, David Z.Z. He, Nikolai Kl\u00f6cker, Jost Ludwig, Uwe Schulte, Siegfried Waldegger, J.P. Ruppersberg, Peter Dallos, Bernd Fakler, \u00ab Intracellular Anions as the Voltage Sensor of Prestin, the Outer Hair Cell Motor Protein \u00bb, Science , vol. 292, n O 5525, 2001 , p. 2340-3 ( r\u00e9sum\u00e9 )  \u2191 Li G, Wang J, Rossiter SJ, Jones G, Cotton Judge, Zhang S, ” The hearing gene Prestin reunites echolocating bats \u00bb, PNAS , vol. 105, n O 37, September 2008 , p. 13959-64 (PMID\u00a0 18776049 , PMCID\u00a0 2544561 , DOI\u00a0 10.1073\/pnas.0802097105 , read online ) ( \/ taken up by BBC News )  \u2191 Liberman MC, Gao J, He DZ, Wu X, Jia S, Zuo J, \u00ab\u00a0 Prestin is required for electromotility of the outer hair cell and for the cochlear amplifier \u00bb, Nature , vol. 419, n O 6904, September 2002 , p. 300\u20134 (PMID\u00a0 12239568 , DOI\u00a0 10.1038\/nature01059 , r\u00e9sum\u00e9 )  \u2191 Presentation of the work of the “Northwestern Search School of Communication” on the Prestine , consulted 2010\/12\/28  \u2191 US patent n \u00b0 6602992, entitled Mammalian Prestin Polynucleotides, published 2003-08-05, by Dallos P, Zheng J, Madison LD  Related articles [ modifier | Modifier and code ] Bibliography [ modifier | Modifier and code ] (in) Dallos P, Fakler B, ‘ Prestin, a new type of motor protein \u00bb , Nature, Rev. Mol. Cell Biol , vol. 3, n O 2, 2002 , p. 104-11. (PMID\u00a0 11836512 , DOI\u00a0 10.1038\/nrm730 ) (in) Dallos P, Zheng J, Cheatham today, ‘ Prestin and the cochlear amplifier \u00bb , J. Physiol. (Lond.) , vol. 576, n O \u00a0Pt 1,\u200e 2006 , p. 37\u201342. (PMID\u00a0 16873410 , DOI\u00a0 10.1113\/jphysiol.2006.114652 ) Toward a complete human genome sequence ., Jurnal=Genome Res. ;volume=8 ;issue= 11 ;pages= 1097\u2013108; 1999; PMID 9847074 (in) Salmon H, Kujala M, Kerkel\u00e4 E, et al. , ‘ Mapping of five new putative anion transporter genes in human and characterization of SLC26A6, a candidate gene for pancreatic anion exchanger \u00bb , Genomics , vol. 70, n O 1, 2001 , p. 102-12. (PMID\u00a0 11087667 , DOI\u00a0 10.1006\/geno.2000.6355 ) Oliver D, He DZ, Kl\u00f6cker N, et al.  Intracellular anions as the voltage sensor of prestin, the outer hair cell motor protein . Journal=Science, volume=292\u00a0; issue= 5525\u00a0; pages= 2340\u20133\u00a0; 2001\u00a0; PMID 11423665 \u00a0; doi:10.1126\/science.1060939 Liberman MC, Gao J, He DZ, et al. \u00a0; Prestin is required for electromotility of the outer hair cell and for the cochlear amplifier.\u00a0; Nature, volume 419\u00a0; issue= 6904; pages= 300\u20134\u00a0; 2002; PMID 12239568 ; doi:10.1038\/nature01059} Strausberg RL, Feingold EA, Grouse LH, et al.  Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Journal\u00a0: Proc. Natl. Acad. Sci. U.S.A.\u00a0; volume=99\u00a0; issue= 26\u00a0; pages= 16899\u2013903\u00a0; 2003; PMID 12477932 ; doi:10.1073\/pnas.242603899 Liu xz, uyang xm, xia xj, et al. ; Prestin, a cochlear motor protein, is defective in non-syndromic hearing loss .\u00a0; Journal=Hum. Mol. Genet.\u00a0; volume=12\u00a0; issue= 10\u00a0; pages= 1155\u201362\u00a0; 2004\u00a0; PMID 12719379 \u00a0; doi:10.1093\/hmg\/ddg127 {Dong xx, iwasa kh; Tension sensitivity of prestin\u00a0: comparison with the membrane motor in outer hair cells \u00a0; Journal=Biophys. J.\u00a0; volume=86\u00a0; issue= 2\u00a0; pages= 1201\u20138\u00a0; 2004; PMID 4747354 ; two: 10.1016\/s0006-3495 (04) 74194-6 Matsuda k, zheng j, du gg, et al. ; N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function .\u00a0; Journal=J. Neurochem.\u00a0; volume=89\u00a0; issue= 4\u00a0; pages= 928\u201338\u00a0; 2004\u00a0; PMID 15140192 ; DOI: 10.1111\/J.1471-4159.2004.02377.x Chambard JM, Ashmore JF\u00a0; Regulation of the voltage-gated potassium channel KCNQ4 in the auditory pathway. \u00a0; journal=Pflugers Arch.\u00a0; volume=450\u00a0; issue= 1\u00a0; pages= 34\u201344\u00a0; 2005\u00a0; PMID 15660259 \u00a0; doi:10.1007\/s00424-004-1366-2 Rajagopalan L, Patel N, Madabushi S, et al. \u00a0; Essential helix interactions in the anion transporter domain of prestin revealed by evolutionary trace analysis.\u00a0; journal=J. Neurosci.\u00a0; volume=26\u00a0; issue= 49\u00a0; pages= 12727\u201334\u00a0; year= 2006\u00a0; PMID 17151276 ; two: 10.1523\/jneurosci.2734-06.2006 Toth t, deak l, fazakas f, et al.  A new mutation in the human pres gene and its effect on prestin function .\u00a0; journal=Int. J. Mol. Med.\u00a0; volume=20\u00a0; issue= 4\u00a0; pages= 545\u201350\u00a0; 2007\u00a0; PMID 17786286 Koji Iida, Kouhii TSUMOTO, Katsuhisa IKEDA, Izumi Kumagai, Toshimitsu Kobayashi And Hiroshi Wada. Contraction of An Expression System for T He Motor Protein Prestin in Kinese Hamster Ovary Cells Hearing Research, 205, (2005), 262-270       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4"},{"@context":"http:\/\/schema.org\/","@type":"BreadcrumbList","itemListElement":[{"@type":"ListItem","position":1,"item":{"@id":"https:\/\/wiki.edu.vn\/all2en\/wiki32\/#breadcrumbitem","name":"Enzyklop\u00e4die"}},{"@type":"ListItem","position":2,"item":{"@id":"https:\/\/wiki.edu.vn\/all2en\/wiki32\/presstine-proashin-wikipedia\/#breadcrumbitem","name":"PRESSTINE (PROashin) \u2014 Wikipedia"}}]}]