Skip to Main Content
Yale School of Medicine
YSM Home

INFORMATION FOR

DownloadHi-Res Photo

Emile Boulpaep, MD

Professor Emeritus of and Senior Research Scientist in Cellular And Molecular Physiology; Director Medical Studies, Director of Graduate Studies, Cellular and Molecular Physiology

Contact Information

Emile Boulpaep, MD

Mailing Address

  • Cellular & Molecular Physiology

    PO Box 208026, 333 Cedar Street

    New Haven, CT 06520-8026

    United States

Research Summary

Polarized kidney tubule cells have proteins in the plasma membrane facing the urine that differ from those facing the blood. We are studying the electrical characteristics of these proteins-ion channels and electrogenic transporters-in the two plasma membranes of renal tubule cells. Patchclamp, and molecular biology techniques are being used.

  1. We study the physiological role and regulation of single small-conductance chloride channels, CFTR, which are activated by cAMP through phosphorylation by protein kinase A.
  2. We study the ability of CFTR to function as a molecular gating switch for the renal potassium channel ROMK by regulating the ATP sensing of ROMK.
  3. Using confocal vital microscopy and ion-sensitive fluorescent dyes, we study a model of proximal tubule cell injury induced by angiotensin II, which is accompanied by elevation of intracellular calcium and plasma membrane blebbing.

Specialized Terms: Electrical properties of membrane proteins in plasma membranes and junctions of renal tubule cells

Extensive Research Description

Polarized kidney tubule cells have proteins in the plasma membrane facing the urine that differ from those facing the blood. We are studying the electrical characteristics of these proteins-ion channels and electrogenic transporters-in the two plasma membranes of renal tubule cells. Patch-clamp, optical and molecular biology techniques are being used.

  1. We study the physiological role and regulation of single small-conductance chloride channels, which are activated by cAMP through phosphorylation by protein kinase A. Our interest is in the intracellular signal transduction pathways involved in the regulation of these renal channels and their homology with the CFTR protein, known to be deficient in cystic fibrosis.
  2. We study the physiological role and regulation of a cGMP-sensitive non-selective cation channel in the apical membrane of a kidney cell line and its homology with a cGMP-gated non-selective channel of the vertebrate photoreceptor.
  3. Using confocal vital microscopy and ion-sensitive fluorescent dyes, we study a model of proximal tubule cell injury induced by angiotensin II, which is accompanied by elevation of intracellular calcium and plasma membrane blebbing.

Coauthors

Research Interests

Kidney; Physiology

Selected Publications

Edit Profile