Back to Search Start Over

Aquaporin CHIP: the archetypal molecular water channel

Authors :
Agre, Peter
Preston, Gregory M.
Smith, Barbara L.
Jin Sup Jung
Raina, Surabhi
Moon, Chulso
Guggino, William B.
Nielsen, Soren
Source :
The American Journal of Physiology. Oct, 1993, Vol. 265 Issue 4, pF463, 14 p.
Publication Year :
1993

Abstract

Human red blood cells, CHIP28, yields CHIP, a 28-kDa channel-forming integral membrane protein, which is identified to determine the molecular properties of membrane water channels. Osmosis, seen in CHIP, causes water-selective pore movement. Enhancement in osmotic water permeability is seen in Xenopus oocytes due to CHIP expression. Transmembrane movement of ions or other minute molecules is not permitted by CHIP. Permeability of unit water is determined by the recreation of distilled CHIP into proteoliposomes.

Details

ISSN :
00029513
Volume :
265
Issue :
4
Database :
Gale General OneFile
Journal :
The American Journal of Physiology
Publication Type :
Academic Journal
Accession number :
edsgcl.14640368