Increased water flux induced by an aquaporin-1/carbonic anhydrase II interaction

نویسندگان

  • Gonzalo Vilas
  • Devishree Krishnan
  • Sampath Kumar Loganathan
  • Darpan Malhotra
  • Lei Liu
  • Megan Rachele Beggs
  • Patrizia Gena
  • Giuseppe Calamita
  • Martin Jung
  • Richard Zimmermann
  • Grazia Tamma
  • Joseph Roman Casey
  • Robert Todd Alexander
چکیده

Aquaporin-1 (AQP1) enables greatly enhanced water flux across plasma membranes. The cytosolic carboxy terminus of AQP1 has two acidic motifs homologous to known carbonic anhydrase II (CAII) binding sequences. CAII colocalizes with AQP1 in the renal proximal tubule. Expression of AQP1 with CAII in Xenopus oocytes or mammalian cells increased water flux relative to AQP1 expression alone. This required the amino-terminal sequence of CAII, a region that binds other transport proteins. Expression of catalytically inactive CAII failed to increase water flux through AQP1. Proximity ligation assays revealed close association of CAII and AQP1, an effect requiring the second acidic cluster of AQP1. This motif was also necessary for CAII to increase AQP1-mediated water flux. Red blood cell ghosts resealed with CAII demonstrated increased osmotic water permeability compared with ghosts resealed with albumin. Water flux across renal cortical membrane vesicles, measured by stopped-flow light scattering, was reduced in CAII-deficient mice compared with wild-type mice. These data are consistent with CAII increasing water conductance through AQP1 by a physical interaction between the two proteins.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Deficiency of Carbonic Anhydrase II Results in a Urinary Concentrating Defect

Carbonic anhydrase II (CAII) is expressed along the nephron where it interacts with a number of transport proteins augmenting their activity. Aquaporin-1 (AQP1) interacts with CAII to increase water flux through the water channel. Both CAII and aquaporin-1 are expressed in the thin descending limb (TDL); however, the physiological role of a CAII-AQP1 interaction in this nephron segment is not k...

متن کامل

Study of Glycation Process of Human Carbonic Anhydrase II and Investigation of Effect of Fasting On Enzyme Activity by Using Spectroscopic Methods

Background: Glycation is the non-enzymatic reaction between the carbonyl groups in sugar and free amino groups in proteins. this reaction leads to changes in structure and functions of proteins. Advanced glycation end products (AGEs) is the final stage in this process, which is highly oxidizing and destructive nature, causing many diabetic complications. Methods: In the present investigation, ...

متن کامل

Effect of long-term oral administration of extra thyroxine on oviductal expression of carbonic anhydrase and avidin-related protein-2 genes in broiler breeder hens

Avian sperm are stored in the sperm storage tubules (SSTs) of the hen oviduct for a prolonged period. The impact of avidin-related protein-2 (AVRP2) and carbonic anhydrase II (CA II) in sperm viability in the SSTs has been suggested. The aim of the present study was to investigate the effect of oral administration of a high dose of thyroxine on the oviductal expression of AVRP2<...

متن کامل

The functional and physical relationship between the DRA bicarbonate transporter and carbonic anhydrase II.

COOH-terminal cytoplasmic tails of chloride/bicarbonate anion exchangers (AE) bind cytosolic carbonic anhydrase II (CAII) to form a bicarbonate transport metabolon, a membrane protein complex that accelerates transmembrane bicarbonate flux. To determine whether interaction with CAII affects the downregulated in adenoma (DRA) chloride/bicarbonate exchanger, anion exchange activity of DRA-transfe...

متن کامل

Synthesis and Evaluation of Antimicrobial Activity of Metal Complexes of 4-(2'-Hydroxy Phenyl Imino) Phenyl Sulphonamide

       Keeping in view the promising potential of carbonic anhydrase inhibitor based antimicrobials and enhancement of carbonic anhydrase inhibitory activity by metal complexes of sulfonamides, with an aim to develop better antimicrobial agents we have attempted investigation of antimicrobial activity of metal complexes of 4-(2'-hydroxy phenyl imino) phenyl sulphonamide. Sulfanilamide was taken...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره 26  شماره 

صفحات  -

تاریخ انتشار 2015