References
- Everett LA, Glaser B, Beck JC, et al. Pendred syndrome is caused by mutations in a putative sulphate transporter gene (PDS). Nat Genet 1997;17:411–22
- Royaux IE, Suzuki K, Mori A, et al. Pendrin, the protein encoded by the Pendred syndrome gene (PDS), is an apical porter of iodide in the thyroid and is regulated by thyroglobulin in FRTL-5 cells. Endocrinology 2000;141:839–45
- Royaux IE, Wall SM, Karniski LP, et al. Pendrin, encoded by the Pendred syndrome gene, resides in the apical region of renal intercalated cells and mediates bicarbonate secretion. Proc Natl Acad Sci USA 2001;98:4221–6
- Bidart JM, Lacroix L, Evain-Brion D, et al. Expression of Na/I_Symporter and Pendred syndrome genes in trophoblast cells. J Clin Endocrinol Metab 2000;85:4367–72
- Suzuki K, Royaux IE, Everett LA, et al. Expression of PDS/Pds, the Pendred syndrome gene, in endometrium. J Clin Endocrinol Metab 2002;87:938--41
- Scott DA, Wang R, Kreman TM, et al. The Pendred syndrome gene encodes a chloride-iodide transport protein. Nat Genet 1999;21:440–3
- Soleimani M, Greeley T, Petrovic S, et al. Pendrin an apical Cl-/OH-/HCO3 – exchanger in the kidney cortex. Am J Physiol Renal Physiol 2001;280:F356–64
- Pedemonte N, Caci E, Sondo E, et al. Thiocyanate transport in resting and IL-4-stimulated human bronchial epithelial cells: role of pendrin and anion channels. J Immunol 2007;178:5144–53
- Manley SW, Li H, Mortimer RH. The BeWo choriocarcinoma cell line as a model of iodide transport by placenta. Placenta 2005;26:380–6
- Wall SM, Pech V. Pendrin and sodium channels: relevance to hypertension. J Nephrol 2010;16:S118–23
- Hadchouel J, Buesst C, Procino G, et al. Regulation of extracellular fluid volume and blood pressure by pendrin. Cell Physiol Biochem 2011;28:505–12
- Eladari D, Chambrey R, Frische S, et al. Pendrin as a regulator of ECF and blood pressure. Curr Opin Nephrol Hypertens 2009;18:356–62
- ACOG Committee on Practice Bulletins–Obstetrics. ACOG practice bulletin: diagnosis and management of preeclampsia and eclampsia. Number 33. Obstet Gynecol 2002;99:159–67
- Skubis-Zegadło J, Nikodemska A, Przytuła E, et al. Expression of pendrin in benign and malignant human thyroid tissues. Br J Cancer 2005;93:144–51
- Amlal H, Petrovic S, Xu J, et al. Deletion of the anion exchanger Slc26a4 (pendrin) decreases apical Cl-/HCO3 – exchanger activity and impairs bicarbonate secretion in kidney collecting duct. Am J Physiol Cell Physiol 2010;299:C33–41
- Rodighiero S, Botta G, Bazzini C, Meyer G. Pendrin overexpression affects cell volume recovery, intracellular pH and chloride concentration after hypotonicity-induced cells welling. Cell Physiol Biochem 2011;28:559–70
- Wagner CA, Mohebbi N, Capasso G, Geibel JP. The anion Exchange pendrin (SLC26A4) andrenal-acid-basehomeostasis. Cell Physiol Biochem 2011;28:497–504
- Eladari D, Chambrey R, Frische S, et al. Pendrin as a regulator of ECF and blood pressure. Curr Opin Nephrol Hypertens 2009;18:356–62
- Wagner SJ, Craici IM, Grande JP, Garovic VD. From placenta to podocyte: vascular and podocyte pathophysiology in preeclampsia. Clin Nephrol 2012;78:241–9
- Alexander JM, Wilson KL. Hypertensive emergencies of pregnancy. Obstet Gynecol Clin North Am 2013;40:89–101
- Lo JO, Mission JF, Caughey AB. Hypertensive disease of pregnancy and maternal mortality. Curr Opin Obstet Gynecol 2013;25:124–32
- Turner MA, Sides MK, Sibley CP, Greenwood SL. Anion efflux from cytotrophoblast cells derived from normal term human placenta is stimulated by hyposmotic challenge and extracellular A23187 but not by membrane soluble cAMP. Exp Physiol 1999;84:27–40