Human SLC26A1 Gene Variants: A Pilot Study
Kidney stones are a global health problem, incurring massive health costs annually. Why stones recur in many patients remains unknown but likely involves environmental, physiological, and genetic factors. The solute linked carrier (SLC) 26A1 gene has previously been linked to kidney stones in mice....
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| Format: | Article |
| Language: | English |
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Wiley
2013-01-01
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| Series: | The Scientific World Journal |
| Online Access: | http://dx.doi.org/10.1155/2013/541710 |
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| author | Paul A. Dawson Pearl Sim David W. Mudge David Cowley |
| author_facet | Paul A. Dawson Pearl Sim David W. Mudge David Cowley |
| author_sort | Paul A. Dawson |
| collection | DOAJ |
| description | Kidney stones are a global health problem, incurring massive health costs annually. Why stones recur in many patients remains unknown but likely involves environmental, physiological, and genetic factors. The solute linked carrier (SLC) 26A1 gene has previously been linked to kidney stones in mice. SLC26A1 encodes the sulfate anion transporter 1 (SAT1) protein, and its loss in mice leads to hyperoxaluria and calcium oxalate renal stones. To investigate the possible involvement of SAT1 in human urolithiasis, we screened the SLC26A1 gene in a cohort of 13 individuals with recurrent calcium oxalate urolithiasis, which is the commonest type. DNA sequence analyses showed missense mutations in seven patients: one individual was heterozygous R372H; 4 individuals were heterozygous Q556R; one patient was homozygous Q556R; and one patient with severe nephrocalcinosis (requiring nephrectomy) was homozygous Q556R and heterozygous M132T. The M132 amino acid in human SAT1 is conserved with 15 other species and is located within the third transmembrane domain of the predicted SAT1 protein structure, suggesting that this amino acid may be important for SAT1 function. These initial findings demonstrate genetic variants in SLC26A1 of recurrent stone formers and warrant wider independent studies of SLC26A1 in humans with recurrent calcium oxalate stones. |
| format | Article |
| id | doaj-art-4137cbec85f24a85822278aa3337f705 |
| institution | Kabale University |
| issn | 1537-744X |
| language | English |
| publishDate | 2013-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | The Scientific World Journal |
| spelling | doaj-art-4137cbec85f24a85822278aa3337f7052025-02-03T01:11:43ZengWileyThe Scientific World Journal1537-744X2013-01-01201310.1155/2013/541710541710Human SLC26A1 Gene Variants: A Pilot StudyPaul A. Dawson0Pearl Sim1David W. Mudge2David Cowley3Mater Research, Translational Research Institute, Woolloongabba, QLD 4102, AustraliaMater Research, Translational Research Institute, Woolloongabba, QLD 4102, AustraliaDepartment of Nephrology, University of Queensland at Princess Alexandra Hospital, Brisbane, QLD 4102, AustraliaPathology Department, Mater Misercordiae Hospital, South Brisbane, QLD 4101, AustraliaKidney stones are a global health problem, incurring massive health costs annually. Why stones recur in many patients remains unknown but likely involves environmental, physiological, and genetic factors. The solute linked carrier (SLC) 26A1 gene has previously been linked to kidney stones in mice. SLC26A1 encodes the sulfate anion transporter 1 (SAT1) protein, and its loss in mice leads to hyperoxaluria and calcium oxalate renal stones. To investigate the possible involvement of SAT1 in human urolithiasis, we screened the SLC26A1 gene in a cohort of 13 individuals with recurrent calcium oxalate urolithiasis, which is the commonest type. DNA sequence analyses showed missense mutations in seven patients: one individual was heterozygous R372H; 4 individuals were heterozygous Q556R; one patient was homozygous Q556R; and one patient with severe nephrocalcinosis (requiring nephrectomy) was homozygous Q556R and heterozygous M132T. The M132 amino acid in human SAT1 is conserved with 15 other species and is located within the third transmembrane domain of the predicted SAT1 protein structure, suggesting that this amino acid may be important for SAT1 function. These initial findings demonstrate genetic variants in SLC26A1 of recurrent stone formers and warrant wider independent studies of SLC26A1 in humans with recurrent calcium oxalate stones.http://dx.doi.org/10.1155/2013/541710 |
| spellingShingle | Paul A. Dawson Pearl Sim David W. Mudge David Cowley Human SLC26A1 Gene Variants: A Pilot Study The Scientific World Journal |
| title | Human SLC26A1 Gene Variants: A Pilot Study |
| title_full | Human SLC26A1 Gene Variants: A Pilot Study |
| title_fullStr | Human SLC26A1 Gene Variants: A Pilot Study |
| title_full_unstemmed | Human SLC26A1 Gene Variants: A Pilot Study |
| title_short | Human SLC26A1 Gene Variants: A Pilot Study |
| title_sort | human slc26a1 gene variants a pilot study |
| url | http://dx.doi.org/10.1155/2013/541710 |
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