PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 27509681-3 2015 It is now well established that this condition was caused by mutations in the SLC26A4 gene which codes for pendrin, a protein involved in the transport of anions (I-, Cl, HCO3-), particularly in apical iodine efflux in thyroid cells and chloride (Cl- HCO3-) at the cochlear level. Chlorides 237-245 solute carrier family 26 member 4 Homo sapiens 78-85 32923987-0 2020 Pendrin stimulates a chloride absorption pathway to increase CFTR-mediated chloride secretion from Cystic Fibrosis airway epithelia. Chlorides 21-29 solute carrier family 26 member 4 Homo sapiens 0-7 32923987-0 2020 Pendrin stimulates a chloride absorption pathway to increase CFTR-mediated chloride secretion from Cystic Fibrosis airway epithelia. Chlorides 75-83 solute carrier family 26 member 4 Homo sapiens 0-7 31281021-1 2019 Pendrin is a transmembrane chloride/anion antiporter that is strongly upregulated in the airways in rhinoviral infection, asthma, cystic fibrosis and chronic rhinosinusitis. Chlorides 27-35 solute carrier family 26 member 4 Homo sapiens 0-7 30744098-1 2019 Pendrin (SLC26A4), a Cl-/anion exchanger, is expressed at high levels in kidney, thyroid, and inner ear epithelia, where it has an essential role in bicarbonate secretion/chloride reabsorption, iodide accumulation, and endolymph ion balance, respectively. Chlorides 171-179 solute carrier family 26 member 4 Homo sapiens 0-7 30744098-1 2019 Pendrin (SLC26A4), a Cl-/anion exchanger, is expressed at high levels in kidney, thyroid, and inner ear epithelia, where it has an essential role in bicarbonate secretion/chloride reabsorption, iodide accumulation, and endolymph ion balance, respectively. Chlorides 171-179 solute carrier family 26 member 4 Homo sapiens 9-16 28648509-5 2017 Pendrin has affinity for chloride, iodide, and bicarbonate, among other anions. Chlorides 25-33 solute carrier family 26 member 4 Homo sapiens 0-7 28648509-6 2017 In the inner ear, pendrin functions as a chloride/bicarbonate exchanger that is essential for maintaining the composition and the potential of the endolymph. Chlorides 41-49 solute carrier family 26 member 4 Homo sapiens 18-25 28648509-12 2017 In the kidney, pendrin is involved in bicarbonate secretion and chloride reabsorption. Chlorides 64-72 solute carrier family 26 member 4 Homo sapiens 15-22 33182508-3 2020 In patients with excessive loss of salt in the sweat or poor salt intake, the maintenance of metabolic alkalosis is crucially modulated by the chloride-bicarbonate exchanger pendrin located on the renal tubular membrane of type B intercalated cells. Chlorides 143-151 solute carrier family 26 member 4 Homo sapiens 174-181 27509681-3 2015 It is now well established that this condition was caused by mutations in the SLC26A4 gene which codes for pendrin, a protein involved in the transport of anions (I-, Cl, HCO3-), particularly in apical iodine efflux in thyroid cells and chloride (Cl- HCO3-) at the cochlear level. Chlorides 237-245 solute carrier family 26 member 4 Homo sapiens 107-114 21358184-6 2011 SLC26A4 encodes the pendrin polypeptide, an anion exchanger that, in recombinant expression systems, transports chloride, bicarbonate, and iodide. Chlorides 112-120 solute carrier family 26 member 4 Homo sapiens 0-7 25141009-7 2014 Furthermore, HBE cells treated with short interfering RNA against Pendrin showed substantially reduced chloride-bicarbonate exchange. Chlorides 103-111 solute carrier family 26 member 4 Homo sapiens 66-73 23383138-14 2013 Pendrin is regulated by acidosis and chloride intake, whereas AE1 is enhanced by acidosis, NaCl, and the combination of DOCA and NaHCO3. Chlorides 37-45 solute carrier family 26 member 4 Homo sapiens 0-7 21551164-1 2011 INTRODUCTION: Pendred syndrome, a combination of sensorineural deafness, impaired organification of iodide in the thyroid and goitre, results from biallelic defects in pendrin (encoded by SLC26A4), which transports chloride and iodide in the inner ear and thyroid respectively. Chlorides 215-223 solute carrier family 26 member 4 Homo sapiens 168-175 21551164-1 2011 INTRODUCTION: Pendred syndrome, a combination of sensorineural deafness, impaired organification of iodide in the thyroid and goitre, results from biallelic defects in pendrin (encoded by SLC26A4), which transports chloride and iodide in the inner ear and thyroid respectively. Chlorides 215-223 solute carrier family 26 member 4 Homo sapiens 188-195 21511235-6 2011 In the kidney, pendrin functions as a chloride/bicarbonate exchanger. Chlorides 38-46 solute carrier family 26 member 4 Homo sapiens 15-22 21511235-7 2011 Elucidation of the molecular basis of Pendred syndrome and the function of pendrin has provided unexpected novel insights into the pathophysiology of the inner ear, thyroid hormone synthesis, and chloride/bicarbonate exchange in the kidney. Chlorides 196-204 solute carrier family 26 member 4 Homo sapiens 75-82 21358184-6 2011 SLC26A4 encodes the pendrin polypeptide, an anion exchanger that, in recombinant expression systems, transports chloride, bicarbonate, and iodide. Chlorides 112-120 solute carrier family 26 member 4 Homo sapiens 20-27 22116359-1 2011 BACKGROUND: Pendrin is a multifunctional anion transporter that exchanges chloride and iodide in the thyroid, as well as chloride and bicarbonate in the inner ear, kidney and airways. Chlorides 74-82 solute carrier family 26 member 4 Homo sapiens 12-19 22116371-0 2011 Pendrin overexpression affects cell volume recovery, intracellular pH and chloride concentration after hypotonicity-induced cell swelling. Chlorides 74-82 solute carrier family 26 member 4 Homo sapiens 0-7 22116353-1 2011 Pendrin (SLC26A4), a Cl(-)/anion exchanger encoded by the gene PDS, is highly expressed in the kidney, thyroid and inner ear epithelia and is essential for bicarbonate secretion/chloride reabsorption, iodide accumulation and endolymph ion balance, respectively. Chlorides 178-186 solute carrier family 26 member 4 Homo sapiens 0-7 22116353-1 2011 Pendrin (SLC26A4), a Cl(-)/anion exchanger encoded by the gene PDS, is highly expressed in the kidney, thyroid and inner ear epithelia and is essential for bicarbonate secretion/chloride reabsorption, iodide accumulation and endolymph ion balance, respectively. Chlorides 178-186 solute carrier family 26 member 4 Homo sapiens 9-16 22116353-1 2011 Pendrin (SLC26A4), a Cl(-)/anion exchanger encoded by the gene PDS, is highly expressed in the kidney, thyroid and inner ear epithelia and is essential for bicarbonate secretion/chloride reabsorption, iodide accumulation and endolymph ion balance, respectively. Chlorides 178-186 solute carrier family 26 member 4 Homo sapiens 63-66 22116359-1 2011 BACKGROUND: Pendrin is a multifunctional anion transporter that exchanges chloride and iodide in the thyroid, as well as chloride and bicarbonate in the inner ear, kidney and airways. Chlorides 121-129 solute carrier family 26 member 4 Homo sapiens 12-19 22116360-1 2011 BACKGROUND: Pendrin is a transport protein exchanging chloride for other anions, such as iodide in the thyroid gland or bicarbonate in the inner ear. Chlorides 54-62 solute carrier family 26 member 4 Homo sapiens 12-19 20298745-7 2010 In the kidney, pendrin functions as a chloride/bicarbonate exchanger. Chlorides 38-46 solute carrier family 26 member 4 Homo sapiens 15-22 20298745-9 2010 Elucidation of the function of pendrin has provided unexpected novel insights into the pathophysiology of thyroid hormone biosynthesis, chloride retention in the kidney, and composition of the endolymph. Chlorides 136-144 solute carrier family 26 member 4 Homo sapiens 31-38 19277700-7 2009 Bicarbonate secretion is achieved by non-type-A intercalated cells characterized by the luminal expression of the chloride/bicarbonate exchanger pendrin. Chlorides 114-122 solute carrier family 26 member 4 Homo sapiens 145-152 19277700-8 2009 Pendrin activity is driven by H(+)-ATPases and may serve both bicarbonate excretion and chloride reabsorption. Chlorides 88-96 solute carrier family 26 member 4 Homo sapiens 0-7 19277700-9 2009 The activity and expression of pendrin is regulated by different factors including acid-base status, chloride delivery, and angiotensin II and may play a role in NaCl retention and blood pressure regulation. Chlorides 101-109 solute carrier family 26 member 4 Homo sapiens 31-38 18692402-3 2008 Pendred syndrome is caused by biallelic mutations in the SLC26A4 gene, which encodes pendrin, a transporter of chloride, bicarbonate and iodide. Chlorides 111-119 solute carrier family 26 member 4 Homo sapiens 57-64 30290408-3 2008 SLC26A4 encodes pendrin, a sodium-independent transporter of iodide/chloride, chloride/formate and bicarbonate, that is expressed in the inner ear, thyroid gland, syncytiotrophoblast cells, endometrium and kidney. Chlorides 68-76 solute carrier family 26 member 4 Homo sapiens 0-7 30290408-3 2008 SLC26A4 encodes pendrin, a sodium-independent transporter of iodide/chloride, chloride/formate and bicarbonate, that is expressed in the inner ear, thyroid gland, syncytiotrophoblast cells, endometrium and kidney. Chlorides 68-76 solute carrier family 26 member 4 Homo sapiens 16-23 30290408-3 2008 SLC26A4 encodes pendrin, a sodium-independent transporter of iodide/chloride, chloride/formate and bicarbonate, that is expressed in the inner ear, thyroid gland, syncytiotrophoblast cells, endometrium and kidney. Chlorides 78-87 solute carrier family 26 member 4 Homo sapiens 0-7 30290408-3 2008 SLC26A4 encodes pendrin, a sodium-independent transporter of iodide/chloride, chloride/formate and bicarbonate, that is expressed in the inner ear, thyroid gland, syncytiotrophoblast cells, endometrium and kidney. Chlorides 78-87 solute carrier family 26 member 4 Homo sapiens 16-23 19050049-1 2009 CONTEXT: Pendrin is an apical protein of thyroid follicular cells, responsible for the efflux of iodide into the follicular lumen via an iodide-chloride transport mechanism. Chlorides 144-152 solute carrier family 26 member 4 Homo sapiens 9-16 18692402-3 2008 Pendred syndrome is caused by biallelic mutations in the SLC26A4 gene, which encodes pendrin, a transporter of chloride, bicarbonate and iodide. Chlorides 111-119 solute carrier family 26 member 4 Homo sapiens 85-92 17164396-0 2007 The emerging role of pendrin in renal chloride reabsorption. Chlorides 38-46 solute carrier family 26 member 4 Homo sapiens 21-28 17766716-3 2007 The encoded transmembrane protein, called pendrin, has been found to be able to transport chloride and other anions. Chlorides 90-98 solute carrier family 26 member 4 Homo sapiens 42-49 17659500-2 2007 Immunohistochemical studies have shown that pendrin is expressed at the apical surface of follicular thyroid cells, where it acts as a Cl-/I- exchanger regulating the chloride transport from the cytoplasm to the colloid space. Chlorides 167-175 solute carrier family 26 member 4 Homo sapiens 44-51 17659500-4 2007 Finally, pendrin is expressed in the kidney, where it is localized in the apical membrane of type-B intercalated cells and non-A, non-B intercalated cells of the cortical collecting ducts and connecting tubules, where it again acts as a Cl /HCO-3 exchanger regulating the acid-base status and chloride homeostasis. Chlorides 293-301 solute carrier family 26 member 4 Homo sapiens 9-16 10861298-1 2000 The PDS gene encodes a transmembrane protein, known as pendrin, which functions as a transporter of iodide and chloride. Chlorides 111-119 solute carrier family 26 member 4 Homo sapiens 4-7 16791000-3 2006 METHODS: Chloride uptake studies were made using HEK293-Phoenix cells expressing human wild type SLC26A4 (pendrin) and a mutant (SLC26A4(S28R)) we recently described in a patient with hypothyroidism, goiter and sensorineural hearing loss. Chlorides 9-17 solute carrier family 26 member 4 Homo sapiens 97-104 16791000-3 2006 METHODS: Chloride uptake studies were made using HEK293-Phoenix cells expressing human wild type SLC26A4 (pendrin) and a mutant (SLC26A4(S28R)) we recently described in a patient with hypothyroidism, goiter and sensorineural hearing loss. Chlorides 9-17 solute carrier family 26 member 4 Homo sapiens 129-136 16791000-6 2006 Furthermore, we show that the SLC26A4 induced chloride uptake in HEK293-Phoenix cells competes with iodide, and, in addition, that the chloride uptake can be blocked by NPPB and niflumic acid, whereas DIDS is ineffective. Chlorides 46-54 solute carrier family 26 member 4 Homo sapiens 30-37 16791000-6 2006 Furthermore, we show that the SLC26A4 induced chloride uptake in HEK293-Phoenix cells competes with iodide, and, in addition, that the chloride uptake can be blocked by NPPB and niflumic acid, whereas DIDS is ineffective. Chlorides 135-143 solute carrier family 26 member 4 Homo sapiens 30-37 16260428-1 2005 OBJECTIVE: The SLC26A4 protein (pendrin) seems to be involved in the exchange of chloride with other anions, therefore being responsible for iodide organification in the thyroid gland and the conditioning of the endolymphatic fluid in the inner ear. Chlorides 81-89 solute carrier family 26 member 4 Homo sapiens 15-22 16260428-1 2005 OBJECTIVE: The SLC26A4 protein (pendrin) seems to be involved in the exchange of chloride with other anions, therefore being responsible for iodide organification in the thyroid gland and the conditioning of the endolymphatic fluid in the inner ear. Chlorides 81-89 solute carrier family 26 member 4 Homo sapiens 32-39 16260428-5 2005 Recently, it has been shown that human pendrin expressed in monkey cells leads to chloride currents. Chlorides 82-90 solute carrier family 26 member 4 Homo sapiens 39-46 16260428-8 2005 CONCLUSION: Our experiments suggest that the SLC26A4-induced chloride transport is electroneutral when expressed in human cellular systems. Chlorides 61-69 solute carrier family 26 member 4 Homo sapiens 45-52 15850642-5 2005 Chloride in the medium was more effective than sulfate at inhibiting this uptake, matching the ionic specificity of pendrin. Chlorides 0-8 solute carrier family 26 member 4 Homo sapiens 116-123 11087667-3 2000 Three human transporter proteins have been functionally characterized: SLC26A2 (DTDST), SLC26A3 (CLD or DRA), and SLC26A4 (PDS) can transport with different specificities the chloride, iodine, bicarbonate, oxalate, and hydroxyl anions, whereas SLC26A5 (prestin) was suggested to act as the motor protein of the cochlear outer hair cell. Chlorides 175-183 solute carrier family 26 member 4 Homo sapiens 114-121 16914891-2 2006 It is generally assumed that SLC26A4 acts as a chloride/anion exchanger, which in the thyroid gland transports iodide, and in the inner ear contributes to the conditioning of the endolymphatic fluid. Chlorides 47-55 solute carrier family 26 member 4 Homo sapiens 29-36 16914891-4 2006 The validation of the method was done by functionally characterizing the chloride/iodide transport of SLC26A4, and a mutant, i.e. SLC26A4(S28R), which we previously described in a patient with sensorineural hearing loss, hypothyroidism and goiter. Chlorides 73-81 solute carrier family 26 member 4 Homo sapiens 102-109 16914891-5 2006 Using the fluorometric method we describe here we can continuously monitor and quantify the iodide or chloride amounts transported by the cells, and we found that the transport capability of the SLC26A4(S28R) mutant protein is markedly reduced if compared to wild-type SLC26A4. Chlorides 102-110 solute carrier family 26 member 4 Homo sapiens 195-202 12533525-8 2003 These results suggest that pendrin may play a role in thyroid hormone production as the apical porter of chloride/iodide and investigation of pendrin leads to a better understanding of functional aspects of the iodine transportation system in thyroid diseases. Chlorides 105-113 solute carrier family 26 member 4 Homo sapiens 27-34 11919333-2 2002 It codes for a transmembrane protein called pendrin, which is highly expressed at the apical surface of the thyroid cell and functions as a transporter of chloride and iodide. Chlorides 155-163 solute carrier family 26 member 4 Homo sapiens 44-51 11496064-8 2001 Functional studies indicate that pendrin can function in chloride-formate and chloride-base exchange modes. Chlorides 57-65 solute carrier family 26 member 4 Homo sapiens 33-40 11496064-11 2001 In the present review, recent studies regarding the renal distribution and membrane localization of pendrin, and its functional properties, including its roles in chloride reabsorption and base excretion, are addressed. Chlorides 163-171 solute carrier family 26 member 4 Homo sapiens 100-107 11573133-4 2001 Despite its high homology to known sulfate transporters, pendrin has been shown to transport iodide and chloride, but not sulfate. Chlorides 104-112 solute carrier family 26 member 4 Homo sapiens 57-64 10861298-1 2000 The PDS gene encodes a transmembrane protein, known as pendrin, which functions as a transporter of iodide and chloride. Chlorides 111-119 solute carrier family 26 member 4 Homo sapiens 55-62 10861298-5 2000 The mutations associated with Pendred syndrome have complete loss of pendrin-induced chloride and iodide transport, while alleles unique to people with DFNB4 are able to transport both iodide and chloride, albeit at a much lower level than wild-type pendrin. Chlorides 85-93 solute carrier family 26 member 4 Homo sapiens 69-76 10861298-5 2000 The mutations associated with Pendred syndrome have complete loss of pendrin-induced chloride and iodide transport, while alleles unique to people with DFNB4 are able to transport both iodide and chloride, albeit at a much lower level than wild-type pendrin. Chlorides 196-204 solute carrier family 26 member 4 Homo sapiens 152-157 10192399-7 1999 The rates of transport for iodide and chloride were significantly increased following the expression of pendrin in both cell systems. Chlorides 38-46 solute carrier family 26 member 4 Homo sapiens 104-111 10843192-2 2000 Its product, designated pendrin, was shown to transport chloride and iodide. Chlorides 56-64 solute carrier family 26 member 4 Homo sapiens 24-31 10644505-0 2000 An ion transporter involved in congenital deafness focus on "human pendrin expressed in Xenopus laevis oocytes mediates chloride/formate exchange". Chlorides 120-128 solute carrier family 26 member 4 Homo sapiens 67-74 10192399-8 1999 Our results demonstrate that pendrin functions as a transporter of chloride and iodide, but not sulfate, and may provide insight into thyroid physiology and the pathophysiology of Pendred syndrome. Chlorides 67-75 solute carrier family 26 member 4 Homo sapiens 29-36 35227018-4 2022 In the airways, pendrin and CFTR seems to be involved in alkalinization of the apical fluid via bicarbonate secretion, especially during inflammation, while CFTR also controls the volume of the apical fluid via a cAMP-dependent chloride secretion, which is stimulated by pendrin. Chlorides 228-236 solute carrier family 26 member 4 Homo sapiens 271-278 35227018-3 2022 While pendrin drives chloride reabsorption and bicarbonate, thiocyanate or iodide secretion within the apical compartment, CFTR represents a pathway for the apical efflux of chloride, bicarbonate, and possibly iodide. Chlorides 21-29 solute carrier family 26 member 4 Homo sapiens 6-13 35227018-4 2022 In the airways, pendrin and CFTR seems to be involved in alkalinization of the apical fluid via bicarbonate secretion, especially during inflammation, while CFTR also controls the volume of the apical fluid via a cAMP-dependent chloride secretion, which is stimulated by pendrin. Chlorides 228-236 solute carrier family 26 member 4 Homo sapiens 16-23 10571950-3 1999 The disease gene (PDS) has been mapped to chromosome 7q22-q31, and encodes a chloride-iodide transport protein. Chlorides 77-85 solute carrier family 26 member 4 Homo sapiens 18-21 33806154-5 2021 The latter mainly involves CFTR, the apical chloride/bicarbonate exchanger pendrin and paracellular transport. Chlorides 44-52 solute carrier family 26 member 4 Homo sapiens 75-82 35227018-6 2022 Bicarbonate secretion occurs via pendrin, which also drives chloride reabsorption. Chlorides 60-68 solute carrier family 26 member 4 Homo sapiens 33-40