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Pendrin

April 12, 2024

Pendrin is an anion exchange protein that in humans is encoded by the SLC26A4 gene (solute carrier family 26, member 4).[1][2] Pendrin was initially identified as a sodium-independent chloride-iodide exchanger[3] with subsequent studies showing that it also accepts formate and bicarbonate as substrates.[4][5] Pendrin is similar to the Band 3 transport protein found in red blood cells. Pendrin is the protein which is mutated in Pendred syndrome, which is an autosomal recessive disorder characterized by sensorineural hearing loss, goiter and a partial organification problem detectable by a positive perchlorate test.[6]

Pendrin
Identifiers
AliasesIPR030285SLC26A4
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Pendrin is responsible for mediating the electroneutral exchange of chloride (Cl−) for bicarbonate (HCO3−) across a plasma membrane in the chloride cells of freshwater fish.

By phylogenetic analysis, pendrin has been found to be a close relative of prestin present on the hair cells or organ of corti in the inner ear. Prestin is primarily an electromechanical transducer but pendrin is an ion transporter.

Function edit

Pendrin is an ion exchanger found in many types of cells in the body. High levels of pendrin expression have been identified in the inner ear and thyroid. In the thyroid, pendrin mediates a component of the efflux of iodide across the apical membrane of the thyrocyte, which is critical for the formation of thyroid hormone.[7] The exact function of pendrin in the inner ear remains unclear; however, pendrin may play a role in acid-base balance as a chloride-bicarbonate exchanger, regulate volume homeostasis through its ability to function as a chloride-formate exchanger[8][9] or indirectly modulate the calcium concentration of the endolymph.[10] Pendrin is also expressed in the kidney, and has been localized to the apical membrane of a population of intercalated cells in the cortical collecting duct where it is involved in bicarbonate secretion.[11][12]

 
Thyroid hormone synthesis, with Pendrin seen at center between the follicular colloid and the follicular cell.

Clinical significance edit

Mutations in this gene are associated with Pendred syndrome, the most common form of syndromic deafness, an autosomal-recessive disease. Pendred syndrome is characterized by thyroid goiter and enlargement of the vestibular aqueduct resulting in deafness; however, despite being expressed in the kidney, individuals with Pendred syndrome do not show any kidney-related acid-base, or volume abnormalities under basal conditions. This is probably the result of other bicarbonate or chloride transporters in the kidney compensating for any loss of pendrin function. Only under extreme situations of salt depletion or metabolic alkalosis, or with inactivation of the sodium-chloride cotransporter, are fluid and electrolyte disorders manifested in these patients.[13] SLC26A4 is highly homologous to the SLC26A3 gene; they have similar genomic structures and this gene is located 3' of the SLC26A3 gene. The encoded protein has homology to sulfate transporters.[1]

Another little-understood role of pendrin is in airway hyperreactivity and inflammation, as during asthma attacks and allergic reactions. Expression of pendrin in the lung increases in response to allergens and high concentrations of IL-13,[14][15] and overexpression of pendrin results in airway inflammation, hyperreactivity, and increased mucus production.[16][17] These symptoms could result from pendrin's effects on ion concentration in the airway surface liquid, possibly causing the liquid to be less hydrated.[18]

References edit

  1. ^ a b "Entrez Gene: SLC26A4 solute carrier family 26, member 4".
  2. ^ Everett LA, Glaser B, Beck JC, Idol JR, Buchs A, Heyman M, Adawi F, Hazani E, Nassir E, Baxevanis AD, Sheffield VC, Green ED (December 1997). "Pendred syndrome is caused by mutations in a putative sulphate transporter gene (PDS)". Nature Genetics. 17 (4): 411–22. doi:10.1038/ng1297-411. PMID 9398842. S2CID 39359838.
  3. ^ Scott DA, Wang R, Kreman TM, Sheffield VC, Karniski LP (April 1999). "The Pendred syndrome gene encodes a chloride-iodide transport protein". Nature Genetics. 21 (4): 440–3. doi:10.1038/7783. PMID 10192399. S2CID 23717390.
  4. ^ Scott DA, Karniski LP (January 2000). "Human pendrin expressed in Xenopus laevis oocytes mediates chloride/formate exchange". American Journal of Physiology. Cell Physiology. 278 (1): C207-11. doi:10.1152/ajpcell.2000.278.1.c207. PMID 10644529. S2CID 18841371.
  5. ^ Soleimani M, Greeley T, Petrovic S, Wang Z, Amlal H, Kopp P, Burnham CE (February 2001). "Pendrin: an apical Cl-/OH-/HCO3- exchanger in the kidney cortex". American Journal of Physiology. Renal Physiology. 280 (2): F356-64. doi:10.1152/ajprenal.2001.280.2.f356. PMID 11208611.
  6. ^ Patterson C, Runge MS (2006). Principles of molecular medicine. Totowa, NJ: Humana Press. p. 957. ISBN 1-58829-202-9.
  7. ^ Bizhanova A, Kopp P (2011-01-01). "Controversies concerning the role of pendrin as an apical iodide transporter in thyroid follicular cells". Cellular Physiology and Biochemistry. 28 (3): 485–90. doi:10.1159/000335103. PMID 22116361.
  8. ^ Karniski LP, Aronson PS (September 1985). "Chloride/formate exchange with formic acid recycling: a mechanism of active chloride transport across epithelial membranes". Proceedings of the National Academy of Sciences of the United States of America. 82 (18): 6362–5. Bibcode:1985PNAS...82.6362K. doi:10.1073/pnas.82.18.6362. PMC 391054. PMID 3862136.
  9. ^ Kim HM, Wangemann P (November 2010). "Failure of fluid absorption in the endolymphatic sac initiates cochlear enlargement that leads to deafness in mice lacking pendrin expression". PLOS ONE. 5 (11): e14041. Bibcode:2010PLoSO...514041K. doi:10.1371/journal.pone.0014041. PMC 2984494. PMID 21103348.
  10. ^ Wangemann P, Nakaya K, Wu T, Maganti RJ, Itza EM, Sanneman JD, Harbidge DG, Billings S, Marcus DC (May 2007). "Loss of cochlear HCO3- secretion causes deafness via endolymphatic acidification and inhibition of Ca2+ reabsorption in a Pendred syndrome mouse model". American Journal of Physiology. Renal Physiology. 292 (5): F1345-53. doi:10.1152/ajprenal.00487.2006. PMC 2020516. PMID 17299139.
  11. ^ Wall SM (2006). "The renal physiology of pendrin (SLC26A4) and its role in hypertension". Novartis Foundation Symposium. Novartis Foundation Symposia. 273: 231–9, discussion 239–43, 261–4. doi:10.1002/0470029579.ch15. ISBN 978-0-470-02957-2. PMID 17120771.
  12. ^ Royaux IE, Wall SM, Karniski LP, Everett LA, Suzuki K, Knepper MA, Green ED (March 2001). "Pendrin, encoded by the Pendred syndrome gene, resides in the apical region of renal intercalated cells and mediates bicarbonate secretion". Proceedings of the National Academy of Sciences of the United States of America. 98 (7): 4221–6. Bibcode:2001PNAS...98.4221R. doi:10.1073/pnas.071516798. PMC 31206. PMID 11274445.
  13. ^ Pela I, Bigozzi M, Bianchi B (June 2008). "Profound hypokalemia and hypochloremic metabolic alkalosis during thiazide therapy in a child with Pendred syndrome". Clinical Nephrology. 69 (6): 450–3. doi:10.5414/cnp69450. PMID 18538122.
  14. ^ Kuperman DA, Lewis CC, Woodruff PG, Rodriguez MW, Yang YH, Dolganov GM, Fahy JV, Erle DJ (August 2005). "Dissecting asthma using focused transgenic modeling and functional genomics". The Journal of Allergy and Clinical Immunology. 116 (2): 305–11. doi:10.1016/j.jaci.2005.03.024. PMID 16083784.
  15. ^ Zhen G, Park SW, Nguyenvu LT, Rodriguez MW, Barbeau R, Paquet AC, Erle DJ (February 2007). "IL-13 and epidermal growth factor receptor have critical but distinct roles in epithelial cell mucin production". American Journal of Respiratory Cell and Molecular Biology. 36 (2): 244–53. doi:10.1165/rcmb.2006-0180OC. PMC 1899314. PMID 16980555.
  16. ^ Pedemonte N, Caci E, Sondo E, Caputo A, Rhoden K, Pfeffer U, Di Candia M, Bandettini R, Ravazzolo R, Zegarra-Moran O, Galietta LJ (April 2007). "Thiocyanate transport in resting and IL-4-stimulated human bronchial epithelial cells: role of pendrin and anion channels". Journal of Immunology. 178 (8): 5144–53. doi:10.4049/jimmunol.178.8.5144. PMID 17404297.
  17. ^ Nakao I, Kanaji S, Ohta S, Matsushita H, Arima K, Yuyama N, Yamaya M, Nakayama K, Kubo H, Watanabe M, Sagara H, Sugiyama K, Tanaka H, Toda S, Hayashi H, Inoue H, Hoshino T, Shiraki A, Inoue M, Suzuki K, Aizawa H, Okinami S, Nagai H, Hasegawa M, Fukuda T, Green ED, Izuhara K (May 2008). "Identification of pendrin as a common mediator for mucus production in bronchial asthma and chronic obstructive pulmonary disease". Journal of Immunology. 180 (9): 6262–9. doi:10.4049/jimmunol.180.9.6262. PMID 18424749.
  18. ^ Nakagami Y, Favoreto S, Zhen G, Park SW, Nguyenvu LT, Kuperman DA, Dolganov GM, Huang X, Boushey HA, Avila PC, Erle DJ (August 2008). "The epithelial anion transporter pendrin is induced by allergy and rhinovirus infection, regulates airway surface liquid, and increases airway reactivity and inflammation in an asthma model". Journal of Immunology. 181 (3): 2203–10. doi:10.4049/jimmunol.181.3.2203. PMC 2491716. PMID 18641360.

Further reading edit

  • Markovich D (October 2001). "Physiological roles and regulation of mammalian sulfate transporters". Physiological Reviews. 81 (4): 1499–533. doi:10.1152/physrev.2001.81.4.1499. PMID 11581495. S2CID 30942862.
  • Baldwin CT, Weiss S, Farrer LA, De Stefano AL, Adair R, Franklyn B, Kidd KK, Korostishevsky M, Bonné-Tamir B (September 1995). "Linkage of congenital, recessive deafness (DFNB4) to chromosome 7q31 and evidence for genetic heterogeneity in the Middle Eastern Druze population". Human Molecular Genetics. 4 (9): 1637–42. doi:10.1093/hmg/4.9.1637. PMID 8541853.
  • Coyle B, Coffey R, Armour JA, Gausden E, Hochberg Z, Grossman A, Britton K, Pembrey M, Reardon W, Trembath R (April 1996). "Pendred syndrome (goitre and sensorineural hearing loss) maps to chromosome 7 in the region containing the nonsyndromic deafness gene DFNB4". Nature Genetics. 12 (4): 421–3. doi:10.1038/ng0496-421. PMID 8630497. S2CID 7166946.
  • Sheffield VC, Kraiem Z, Beck JC, Nishimura D, Stone EM, Salameh M, Sadeh O, Glaser B (April 1996). "Pendred syndrome maps to chromosome 7q21-34 and is caused by an intrinsic defect in thyroid iodine organification". Nature Genetics. 12 (4): 424–6. doi:10.1038/ng0496-424. PMID 8630498. S2CID 25888014.
  • Gausden E, Armour JA, Coyle B, Coffey R, Hochberg Z, Pembrey M, Britton KE, Grossman A, Reardon W, Trembath R (April 1996). "Thyroid peroxidase: evidence for disease gene exclusion in Pendred's syndrome". Clinical Endocrinology. 44 (4): 441–6. doi:10.1046/j.1365-2265.1996.714536.x. PMID 8706311. S2CID 21410631.
  • Coucke P, Van Camp G, Demirhan O, Kabakkaya Y, Balemans W, Van Hauwe P, Van Agtmael T, Smith RJ, Parving A, Bolder CH, Cremers CW, Willems PJ (February 1997). "The gene for Pendred syndrome is located between D7S501 and D7S692 in a 1.7-cM region on chromosome 7q". Genomics. 40 (1): 48–54. doi:10.1006/geno.1996.4541. hdl:2066/25039. PMID 9070918.
  • Li XC, Everett LA, Lalwani AK, Desmukh D, Friedman TB, Green ED, Wilcox ER (March 1998). "A mutation in PDS causes non-syndromic recessive deafness". Nature Genetics. 18 (3): 215–7. doi:10.1038/ng0398-215. PMID 9500541. S2CID 40830620.
  • Van Hauwe P, Everett LA, Coucke P, Scott DA, Kraft ML, Ris-Stalpers C, Bolder C, Otten B, de Vijlder JJ, Dietrich NL, Ramesh A, Srisailapathy SC, Parving A, Cremers CW, Willems PJ, Smith RJ, Green ED, Van Camp G (July 1998). "Two frequent missense mutations in Pendred syndrome". Human Molecular Genetics. 7 (7): 1099–104. doi:10.1093/hmg/7.7.1099. PMID 9618166.
  • Coyle B, Reardon W, Herbrick JA, Tsui LC, Gausden E, Lee J, Coffey R, Grueters A, Grossman A, Phelps PD, Luxon L, Kendall-Taylor P, Scherer SW, Trembath RC (July 1998). "Molecular analysis of the PDS gene in Pendred syndrome". Human Molecular Genetics. 7 (7): 1105–12. doi:10.1093/hmg/7.7.1105. PMID 9618167.
  • Usami S, Abe S, Weston MD, Shinkawa H, Van Camp G, Kimberling WJ (February 1999). "Non-syndromic hearing loss associated with enlarged vestibular aqueduct is caused by PDS mutations". Human Genetics. 104 (2): 188–92. doi:10.1007/s004390050933. PMID 10190331. S2CID 3116063.
  • Masmoudi S, Charfedine I, Hmani M, Grati M, Ghorbel AM, Elgaied-Boulila A, Drira M, Hardelin JP, Ayadi H (January 2000). "Pendred syndrome: phenotypic variability in two families carrying the same PDS missense mutation". American Journal of Medical Genetics. 90 (1): 38–44. doi:10.1002/(SICI)1096-8628(20000103)90:1<38::AID-AJMG8>3.0.CO;2-R. PMID 10602116.
  • Reardon W, OMahoney CF, Trembath R, Jan H, Phelps PD (February 2000). "Enlarged vestibular aqueduct: a radiological marker of pendred syndrome, and mutation of the PDS gene". QJM. 93 (2): 99–104. doi:10.1093/qjmed/93.2.99. PMID 10700480.
  • Bogazzi F, Raggi F, Ultimieri F, Campomori A, Cosci C, Berrettini S, Neri E, La Rocca R, Ronca G, Martino E, Bartalena L (March 2000). "A novel mutation in the pendrin gene associated with Pendred's syndrome". Clinical Endocrinology. 52 (3): 279–85. doi:10.1046/j.1365-2265.2000.00930.x. PMID 10718825. S2CID 40121366.
  • Bidart JM, Mian C, Lazar V, Russo D, Filetti S, Caillou B, Schlumberger M (May 2000). "Expression of pendrin and the Pendred syndrome (PDS) gene in human thyroid tissues". The Journal of Clinical Endocrinology and Metabolism. 85 (5): 2028–33. doi:10.1210/jcem.85.5.6519. PMID 10843192.
  • Adato A, Raskin L, Petit C, Bonne-Tamir B (June 2000). "Deafness heterogeneity in a Druze isolate from the Middle East: novel OTOF and PDS mutations, low prevalence of GJB2 35delG mutation and indication for a new DFNB locus". European Journal of Human Genetics. 8 (6): 437–42. doi:10.1038/sj.ejhg.5200489. PMID 10878664.
  • Lohi H, Kujala M, Kerkelä E, Saarialho-Kere U, Kestilä M, Kere J (November 2000). "Mapping of five new putative anion transporter genes in human and characterization of SLC26A6, a candidate gene for pancreatic anion exchanger". Genomics. 70 (1): 102–12. doi:10.1006/geno.2000.6355. PMID 11087667.
  • Campbell C, Cucci RA, Prasad S, Green GE, Edeal JB, Galer CE, Karniski LP, Sheffield VC, Smith RJ (May 2001). "Pendred syndrome, DFNB4, and PDS/SLC26A4 identification of eight novel mutations and possible genotype-phenotype correlations". Human Mutation. 17 (5): 403–11. doi:10.1002/humu.1116. PMID 11317356. S2CID 36643824.

External links edit

  • GeneReviews/NCBI/NIH/UW entry on Pendred Syndrome/DFNB4
  • Description at oto.wustl.edu
  • SLC26A4+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

April 12, 2024
pendrin, anion, exchange, protein, that, humans, encoded, slc26a4, gene, solute, carrier, family, member, initially, identified, sodium, independent, chloride, iodide, exchanger, with, subsequent, studies, showing, that, also, accepts, formate, bicarbonate, su. Pendrin is an anion exchange protein that in humans is encoded by the SLC26A4 gene solute carrier family 26 member 4 1 2 Pendrin was initially identified as a sodium independent chloride iodide exchanger 3 with subsequent studies showing that it also accepts formate and bicarbonate as substrates 4 5 Pendrin is similar to the Band 3 transport protein found in red blood cells Pendrin is the protein which is mutated in Pendred syndrome which is an autosomal recessive disorder characterized by sensorineural hearing loss goiter and a partial organification problem detectable by a positive perchlorate test 6 PendrinIdentifiersAliasesIPR030285SLC26A4External IDsGeneCards 1 OrthologsSpeciesHumanMouseEntrezn an aEnsembln an aUniProtnan aRefSeq mRNA n an aRefSeq protein n an aLocation UCSC n an aPubMed searchn an aWikidataView Edit HumanPendrin is responsible for mediating the electroneutral exchange of chloride Cl for bicarbonate HCO3 across a plasma membrane in the chloride cells of freshwater fish By phylogenetic analysis pendrin has been found to be a close relative of prestin present on the hair cells or organ of corti in the inner ear Prestin is primarily an electromechanical transducer but pendrin is an ion transporter Contents 1 Function 2 Clinical significance 3 References 4 Further reading 5 External linksFunction editPendrin is an ion exchanger found in many types of cells in the body High levels of pendrin expression have been identified in the inner ear and thyroid In the thyroid pendrin mediates a component of the efflux of iodide across the apical membrane of the thyrocyte which is critical for the formation of thyroid hormone 7 The exact function of pendrin in the inner ear remains unclear however pendrin may play a role in acid base balance as a chloride bicarbonate exchanger regulate volume homeostasis through its ability to function as a chloride formate exchanger 8 9 or indirectly modulate the calcium concentration of the endolymph 10 Pendrin is also expressed in the kidney and has been localized to the apical membrane of a population of intercalated cells in the cortical collecting duct where it is involved in bicarbonate secretion 11 12 nbsp Thyroid hormone synthesis with Pendrin seen at center between the follicular colloid and the follicular cell Clinical significance editMutations in this gene are associated with Pendred syndrome the most common form of syndromic deafness an autosomal recessive disease Pendred syndrome is characterized by thyroid goiter and enlargement of the vestibular aqueduct resulting in deafness however despite being expressed in the kidney individuals with Pendred syndrome do not show any kidney related acid base or volume abnormalities under basal conditions This is probably the result of other bicarbonate or chloride transporters in the kidney compensating for any loss of pendrin function Only under extreme situations of salt depletion or metabolic alkalosis or with inactivation of the sodium chloride cotransporter are fluid and electrolyte disorders manifested in these patients 13 SLC26A4 is highly homologous to the SLC26A3 gene they have similar genomic structures and this gene is located 3 of the SLC26A3 gene The encoded protein has homology to sulfate transporters 1 Another little understood role of pendrin is in airway hyperreactivity and inflammation as during asthma attacks and allergic reactions Expression of pendrin in the lung increases in response to allergens and high concentrations of IL 13 14 15 and overexpression of pendrin results in airway inflammation hyperreactivity and increased mucus production 16 17 These symptoms could result from pendrin s effects on ion concentration in the airway surface liquid possibly causing the liquid to be less hydrated 18 References edit a b Entrez Gene SLC26A4 solute carrier family 26 member 4 Everett LA Glaser B Beck JC Idol JR Buchs A Heyman M Adawi F Hazani E Nassir E Baxevanis AD Sheffield VC Green ED December 1997 Pendred syndrome is caused by mutations in a putative sulphate transporter gene PDS Nature Genetics 17 4 411 22 doi 10 1038 ng1297 411 PMID 9398842 S2CID 39359838 Scott DA Wang R Kreman TM Sheffield VC Karniski LP April 1999 The Pendred syndrome gene encodes a chloride iodide transport protein Nature Genetics 21 4 440 3 doi 10 1038 7783 PMID 10192399 S2CID 23717390 Scott DA Karniski LP January 2000 Human pendrin expressed in Xenopus laevis oocytes mediates chloride formate exchange American Journal of Physiology Cell Physiology 278 1 C207 11 doi 10 1152 ajpcell 2000 278 1 c207 PMID 10644529 S2CID 18841371 Soleimani M Greeley T Petrovic S Wang Z Amlal H Kopp P Burnham CE February 2001 Pendrin an apical Cl OH HCO3 exchanger in the kidney cortex American Journal of Physiology Renal Physiology 280 2 F356 64 doi 10 1152 ajprenal 2001 280 2 f356 PMID 11208611 Patterson C Runge MS 2006 Principles of molecular medicine Totowa NJ Humana Press p 957 ISBN 1 58829 202 9 Bizhanova A Kopp P 2011 01 01 Controversies concerning the role of pendrin as an apical iodide transporter in thyroid follicular cells Cellular Physiology and Biochemistry 28 3 485 90 doi 10 1159 000335103 PMID 22116361 Karniski LP Aronson PS September 1985 Chloride formate exchange with formic acid recycling a mechanism of active chloride transport across epithelial membranes Proceedings of the National Academy of Sciences of the United States of America 82 18 6362 5 Bibcode 1985PNAS 82 6362K doi 10 1073 pnas 82 18 6362 PMC 391054 PMID 3862136 Kim HM Wangemann P November 2010 Failure of fluid absorption in the endolymphatic sac initiates cochlear enlargement that leads to deafness in mice lacking pendrin expression PLOS ONE 5 11 e14041 Bibcode 2010PLoSO 514041K doi 10 1371 journal pone 0014041 PMC 2984494 PMID 21103348 Wangemann P Nakaya K Wu T Maganti RJ Itza EM Sanneman JD Harbidge DG Billings S Marcus DC May 2007 Loss of cochlear HCO3 secretion causes deafness via endolymphatic acidification and inhibition of Ca2 reabsorption in a Pendred syndrome mouse model American Journal of Physiology Renal Physiology 292 5 F1345 53 doi 10 1152 ajprenal 00487 2006 PMC 2020516 PMID 17299139 Wall SM 2006 The renal physiology of pendrin SLC26A4 and its role in hypertension Novartis Foundation Symposium Novartis Foundation Symposia 273 231 9 discussion 239 43 261 4 doi 10 1002 0470029579 ch15 ISBN 978 0 470 02957 2 PMID 17120771 Royaux IE Wall SM Karniski LP Everett LA Suzuki K Knepper MA Green ED March 2001 Pendrin encoded by the Pendred syndrome gene resides in the apical region of renal intercalated cells and mediates bicarbonate secretion Proceedings of the National Academy of Sciences of the United States of America 98 7 4221 6 Bibcode 2001PNAS 98 4221R doi 10 1073 pnas 071516798 PMC 31206 PMID 11274445 Pela I Bigozzi M Bianchi B June 2008 Profound hypokalemia and hypochloremic metabolic alkalosis during thiazide therapy in a child with Pendred syndrome Clinical Nephrology 69 6 450 3 doi 10 5414 cnp69450 PMID 18538122 Kuperman DA Lewis CC Woodruff PG Rodriguez MW Yang YH Dolganov GM Fahy JV Erle DJ August 2005 Dissecting asthma using focused transgenic modeling and functional genomics The Journal of Allergy and Clinical Immunology 116 2 305 11 doi 10 1016 j jaci 2005 03 024 PMID 16083784 Zhen G Park SW Nguyenvu LT Rodriguez MW Barbeau R Paquet AC Erle DJ February 2007 IL 13 and epidermal growth factor receptor have critical but distinct roles in epithelial cell mucin production American Journal of Respiratory Cell and Molecular Biology 36 2 244 53 doi 10 1165 rcmb 2006 0180OC PMC 1899314 PMID 16980555 Pedemonte N Caci E Sondo E Caputo A Rhoden K Pfeffer U Di Candia M Bandettini R Ravazzolo R Zegarra Moran O Galietta LJ April 2007 Thiocyanate transport in resting and IL 4 stimulated human bronchial epithelial cells role of pendrin and anion channels Journal of Immunology 178 8 5144 53 doi 10 4049 jimmunol 178 8 5144 PMID 17404297 Nakao I Kanaji S Ohta S Matsushita H Arima K Yuyama N Yamaya M Nakayama K Kubo H Watanabe M Sagara H Sugiyama K Tanaka H Toda S Hayashi H Inoue H Hoshino T Shiraki A Inoue M Suzuki K Aizawa H Okinami S Nagai H Hasegawa M Fukuda T Green ED Izuhara K May 2008 Identification of pendrin as a common mediator for mucus production in bronchial asthma and chronic obstructive pulmonary disease Journal of Immunology 180 9 6262 9 doi 10 4049 jimmunol 180 9 6262 PMID 18424749 Nakagami Y Favoreto S Zhen G Park SW Nguyenvu LT Kuperman DA Dolganov GM Huang X Boushey HA Avila PC Erle DJ August 2008 The epithelial anion transporter pendrin is induced by allergy and rhinovirus infection regulates airway surface liquid and increases airway reactivity and inflammation in an asthma model Journal of Immunology 181 3 2203 10 doi 10 4049 jimmunol 181 3 2203 PMC 2491716 PMID 18641360 Further reading editMarkovich D October 2001 Physiological roles and regulation of mammalian sulfate transporters Physiological Reviews 81 4 1499 533 doi 10 1152 physrev 2001 81 4 1499 PMID 11581495 S2CID 30942862 Baldwin CT Weiss S Farrer LA De Stefano AL Adair R Franklyn B Kidd KK Korostishevsky M Bonne Tamir B September 1995 Linkage of congenital recessive deafness DFNB4 to chromosome 7q31 and evidence for genetic heterogeneity in the Middle Eastern Druze population Human Molecular Genetics 4 9 1637 42 doi 10 1093 hmg 4 9 1637 PMID 8541853 Coyle B Coffey R Armour JA Gausden E Hochberg Z Grossman A Britton K Pembrey M Reardon W Trembath R April 1996 Pendred syndrome goitre and sensorineural hearing loss maps to chromosome 7 in the region containing the nonsyndromic deafness gene DFNB4 Nature Genetics 12 4 421 3 doi 10 1038 ng0496 421 PMID 8630497 S2CID 7166946 Sheffield VC Kraiem Z Beck JC Nishimura D Stone EM Salameh M Sadeh O Glaser B April 1996 Pendred syndrome maps to chromosome 7q21 34 and is caused by an intrinsic defect in thyroid iodine organification Nature Genetics 12 4 424 6 doi 10 1038 ng0496 424 PMID 8630498 S2CID 25888014 Gausden E Armour JA Coyle B Coffey R Hochberg Z Pembrey M Britton KE Grossman A Reardon W Trembath R April 1996 Thyroid peroxidase evidence for disease gene exclusion in Pendred s syndrome Clinical Endocrinology 44 4 441 6 doi 10 1046 j 1365 2265 1996 714536 x PMID 8706311 S2CID 21410631 Coucke P Van Camp G Demirhan O Kabakkaya Y Balemans W Van Hauwe P Van Agtmael T Smith RJ Parving A Bolder CH Cremers CW Willems PJ February 1997 The gene for Pendred syndrome is located between D7S501 and D7S692 in a 1 7 cM region on chromosome 7q Genomics 40 1 48 54 doi 10 1006 geno 1996 4541 hdl 2066 25039 PMID 9070918 Li XC Everett LA Lalwani AK Desmukh D Friedman TB Green ED Wilcox ER March 1998 A mutation in PDS causes non syndromic recessive deafness Nature Genetics 18 3 215 7 doi 10 1038 ng0398 215 PMID 9500541 S2CID 40830620 Van Hauwe P Everett LA Coucke P Scott DA Kraft ML Ris Stalpers C Bolder C Otten B de Vijlder JJ Dietrich NL Ramesh A Srisailapathy SC Parving A Cremers CW Willems PJ Smith RJ Green ED Van Camp G July 1998 Two frequent missense mutations in Pendred syndrome Human Molecular Genetics 7 7 1099 104 doi 10 1093 hmg 7 7 1099 PMID 9618166 Coyle B Reardon W Herbrick JA Tsui LC Gausden E Lee J Coffey R Grueters A Grossman A Phelps PD Luxon L Kendall Taylor P Scherer SW Trembath RC July 1998 Molecular analysis of the PDS gene in Pendred syndrome Human Molecular Genetics 7 7 1105 12 doi 10 1093 hmg 7 7 1105 PMID 9618167 Usami S Abe S Weston MD Shinkawa H Van Camp G Kimberling WJ February 1999 Non syndromic hearing loss associated with enlarged vestibular aqueduct is caused by PDS mutations Human Genetics 104 2 188 92 doi 10 1007 s004390050933 PMID 10190331 S2CID 3116063 Masmoudi S Charfedine I Hmani M Grati M Ghorbel AM Elgaied Boulila A Drira M Hardelin JP Ayadi H January 2000 Pendred syndrome phenotypic variability in two families carrying the same PDS missense mutation American Journal of Medical Genetics 90 1 38 44 doi 10 1002 SICI 1096 8628 20000103 90 1 lt 38 AID AJMG8 gt 3 0 CO 2 R PMID 10602116 Reardon W OMahoney CF Trembath R Jan H Phelps PD February 2000 Enlarged vestibular aqueduct a radiological marker of pendred syndrome and mutation of the PDS gene QJM 93 2 99 104 doi 10 1093 qjmed 93 2 99 PMID 10700480 Bogazzi F Raggi F Ultimieri F Campomori A Cosci C Berrettini S Neri E La Rocca R Ronca G Martino E Bartalena L March 2000 A novel mutation in the pendrin gene associated with Pendred s syndrome Clinical Endocrinology 52 3 279 85 doi 10 1046 j 1365 2265 2000 00930 x PMID 10718825 S2CID 40121366 Bidart JM Mian C Lazar V Russo D Filetti S Caillou B Schlumberger M May 2000 Expression of pendrin and the Pendred syndrome PDS gene in human thyroid tissues The Journal of Clinical Endocrinology and Metabolism 85 5 2028 33 doi 10 1210 jcem 85 5 6519 PMID 10843192 Adato A Raskin L Petit C Bonne Tamir B June 2000 Deafness heterogeneity in a Druze isolate from the Middle East novel OTOF and PDS mutations low prevalence of GJB2 35delG mutation and indication for a new DFNB locus European Journal of Human Genetics 8 6 437 42 doi 10 1038 sj ejhg 5200489 PMID 10878664 Lohi H Kujala M Kerkela E Saarialho Kere U Kestila M Kere J November 2000 Mapping of five new putative anion transporter genes in human and characterization of SLC26A6 a candidate gene for pancreatic anion exchanger Genomics 70 1 102 12 doi 10 1006 geno 2000 6355 PMID 11087667 Campbell C Cucci RA Prasad S Green GE Edeal JB Galer CE Karniski LP Sheffield VC Smith RJ May 2001 Pendred syndrome DFNB4 and PDS SLC26A4 identification of eight novel mutations and possible genotype phenotype correlations Human Mutation 17 5 403 11 doi 10 1002 humu 1116 PMID 11317356 S2CID 36643824 External links editGeneReviews NCBI NIH UW entry on Pendred Syndrome DFNB4 Description at oto wustl edu SLC26A4 protein human at the U S National Library of Medicine Medical Subject Headings MeSH Retrieved from https en wikipedia org w index php title Pendrin amp oldid 1136207834, wikipedia, wiki, 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