Familial renal tubular acidosis

J Nephrol. 2010 Nov-Dec:23 Suppl 16:S57-76.

Abstract

The kidney maintains systemic acid-base homeostasis through proximal tubular reclamation of filtered bicarbonate, and excretion of the daily mineral acid load by collecting duct type A intercalated cells. Impairment of either process produces renal tubular acidosis (RTA). This article will provide an overview of familial forms of proximal and distal renal tubular acidosis (pRTA and dRTA). Recessive pRTA with ocular and central nervous system abnormalities is caused by loss-of-function mutations in basolateral membrane Na-HCO3- cotransporter NBCe1/ SLC4A4. Recessive dRTA with deafness is caused by loss-of-function mutations in either of 2 subunits of the vacuolar H+-ATPase (V-ATPase) of intercalated cells; the B1 subunit of the V1 cytoplasmic ATPase complex, and the a4 subunit of the V0 transmembrane pore complex. Dominant and recessive forms of dRTA are also caused by loss-of-function mutations in the basolateral membrane AE1 Cl-/HCO3- exchanger of the type A intercalated cell. The dominant AE1 dRTA mutations are accompanied by mild or asymptomatic erythroid changes, while the erythroid dyscrasias accompanying recessive AE1 dRTA mutations can be mild or severe. Recessive mixed proximal-distal RTA is caused by loss-of-function mutations of the cytoplasmic carbonic anhydrase II. Hyperkalemic RTA accompanied by hypertension (pseudohypoaldosteronism type 2 [PHA2]) is caused by dominant gain-of-function mutations in the kinases WNK1 and WNK4. Hyperkalemic RTA accompanied by volume depletion is caused by loss-of-function mutations in genes encoding the mineralocorticoid receptor or the epithelial Na+ channel (ENaC) subunits. Additional RTA genes identified in knockout mice may lead to identification of additional human RTA genes.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Acidosis, Renal Tubular / genetics*
  • Animals
  • Anion Exchange Protein 1, Erythrocyte / genetics
  • Anion Exchange Protein 1, Erythrocyte / physiology
  • Disease Models, Animal
  • Humans
  • Hypercalciuria / etiology
  • Hypokalemia / etiology
  • Mice
  • Mutation
  • Vacuolar Proton-Translocating ATPases / genetics

Substances

  • Anion Exchange Protein 1, Erythrocyte
  • SLC4A1 protein, human
  • Vacuolar Proton-Translocating ATPases