Heterozygous Mutations of The Gene for Kir 1.1 (ROMK) in Antenatal Bartter Syndrome Presenting with Transient Hyperkalemia, Evolving to a Benign Course.
10.3346/jkms.2003.18.1.65
- Author:
Jong Tae CHO
1
;
Lisa Marie GUAY-WOODFORD
Author Information
1. Department of Internal Medicine, Dankook University, College of Medicine, Cheonan, Korea. jtcho@dku.edu
- Publication Type:Case Reports
- Keywords:
Bartter's Disease;
Potassium Channel;
ROMK Protein;
Mutation;
Pseudohypoaldosteronism
- MeSH:
Amino Acid Substitution*;
Bartter's Disease/diagnosis;
Bartter's Disease/embryology;
Bartter's Disease/genetics*;
Codon, Nonsense*;
Diagnosis, Differential;
Exons/genetics;
Female;
Heterozygote;
Human;
Infant, Newborn;
Mutation, Missense*;
Point Mutation;
Potassium Channels/chemistry;
Potassium Channels/genetics*;
Protein Conformation;
Pseudohypoaldosteronism/diagnosis
- From:Journal of Korean Medical Science
2003;18(1):65-68
- CountryRepublic of Korea
- Language:English
-
Abstract:
Bartter-like syndrome encompasses a set of inherited renal tubular disorders associated with hypokalemic metabolic alkalosis, renal salt wasting, hyperreninemic hyperaldosteronism, and normal blood pressure. Antenatal Bartter syndrome, a subtype of Bartter-like syndrome, is characterized by polyhydramnios, premature delivery, life-threatening episodes of fever and dehydration during the early weeks of life, growth retardation, hypercalciuria, and early-onset nephrocalcinosis. Mutations in the bumetanide-sensitive Na-K-2Cl cotransporter (NKCC2) and ATP-sensitive inwardly rectifying potassium channel (ROMK) of the thick ascending limb of Henle's loop have been identified in the antenatal Bartter syndrome. We report the identification of two heterozygous mutations of the gene for Kir 1.1 (ROMK) from an antenatal Bartter syndrome patient who presented at birth with mild salt wasting and a biochemical findings that mimicked primary peudohypoaldosteronism type 1, such as hyperkalemia and hyponatremia, and evolved to a relatively benign course. We have identified amino acid exchanges Arg338Stop and Met357Thr in the gene exon 5 for ROMK by PCR and direct sequencing. Both mutations alter the C-terminus of the ROMK protein, and can affect channel function.
