Rapamycin-induced phosphaturia

Nephrol Dial Transplant. 2010 Sep;25(9):2938-44. doi: 10.1093/ndt/gfq172. Epub 2010 Apr 5.

Abstract

Background: The mammalian target of rapamycin (mTOR) is known to stimulate a variety of transport mechanisms including the intestinal phosphate transporter NaPi-IIb. The present study was performed to elucidate whether mTOR similarly regulates the major renal tubular phosphate transporter NaPi-IIa.

Methods: To this end, NaPi-IIa was expressed in Xenopus oocytes with or without mTOR and phosphate transport estimated from phosphate-induced (1 mM) current (I(pi)).

Results: As a result, I(pi) was observed in NaPi-IIa-expressing but not in H(2)O-injected Xenopus oocytes. Co-expression of mTOR significantly enhanced I(pi) in NaPi-IIa-expressing Xenopus oocytes, an effect abrogated by treatment with rapamycin (50 nM for the last 24 h of incubation). In a second series of experiments, the effect of rapamycin was analysed in mice. The in vivo administration of rapamycin (3 microg/g body weight/day) for 3 days resulted in phosphaturia in mice despite a tendency of plasma phosphate concentration to decrease.

Conclusions: mTOR contributes to the regulation of renal phosphate transport, and rapamycin thus influences phosphate balance.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Biological Transport
  • Female
  • Hypophosphatemia, Familial / chemically induced*
  • Hypophosphatemia, Familial / metabolism
  • Immunoenzyme Techniques
  • Immunosuppressive Agents / toxicity*
  • Kidney / drug effects*
  • Kidney / metabolism
  • Male
  • Mice
  • Oocytes / cytology
  • Oocytes / drug effects*
  • Oocytes / metabolism
  • Phosphates / urine*
  • Rats
  • Sirolimus / toxicity*
  • Sodium-Phosphate Cotransporter Proteins, Type IIa / metabolism
  • TOR Serine-Threonine Kinases / genetics
  • TOR Serine-Threonine Kinases / metabolism*
  • Xenopus laevis

Substances

  • Immunosuppressive Agents
  • Phosphates
  • Sodium-Phosphate Cotransporter Proteins, Type IIa
  • mTOR protein, rat
  • TOR Serine-Threonine Kinases
  • Sirolimus