The discovery of aquaporin-1 (AQP1) answered the long-standing biophysical question of
how water specifically crosses biological membranes. In the kidney, at least seven …

Despite longstanding interest by nephrologists and physiologists, the molecular identities of
membrane water channels remained elusive until recognition of CHIP, a 28-kDa channel …

Novel affinity-purified antibodies against human SGLT1 (hSGLT1) and SGLT2 (hSGLT2)
were used to localize hSGLT2 in human kidney and hSGLT1 in human kidney, small …

▪ Abstract The high water permeability characteristic of mammalian red cell membranes is
now known to be caused by the protein AQP1. This channel freely permits movement of …

Water excretion by the kidney is regulated by the peptide hormone vasopressin.
Vasopressin increases the water permeability of the renal collecting duct cells, allowing …

Aquaporin channel-forming integral protein (CHIP) is the first characterized water channel
protein (genome symbol AQP1), but the molecular structure of the aqueous pathway through …

The aquaporins transport water through membranes of numerous tissues, but the molecular
mechanisms for sensing changes in extracellular osmolality and regulating water balance in …

The existence of water-selective channels has been postulated to explain the high water
permeability of erythrocytes and certain epithelial cells. The aquaporin CHIP (channel …

Aquaporins (AQP) are integral membrane proteins that serve as channels in the transfer of
water, and in some cases, small solutes across the membrane. They are conserved in …

Two mercurial-inhibitable water-transporting proteins have been identified: CHIP28, an
erythrocyte water channel also expressed in kidney tubules and selected extrarenal …