RENAL AMINO-ACID-TRANSPORT - CELLULAR AND MOLECULAR EVENTS FROM CLEARANCE STUDIES TO FROG EGGS

Citation
Rw. Chesney et al., RENAL AMINO-ACID-TRANSPORT - CELLULAR AND MOLECULAR EVENTS FROM CLEARANCE STUDIES TO FROG EGGS, Pediatric nephrology, 7(5), 1993, pp. 574-584
Citations number
NO
Categorie Soggetti
Pediatrics,"Urology & Nephrology
Journal title
Pediatric nephrology
ISSN journal
0931041X → ACNP
Volume
7
Issue
5
Year of publication
1993
Pages
574 - 584
Database
ISI
SICI code
0931-041X(1993)7:5<574:RA-CAM>2.0.ZU;2-H
Abstract
This article reviews recent advances in the mechanisms of renal amino acid transport. Renal amino acid transport is necessary to efficiently reclaim approximately 450 mmol amino acids from the glomerular ultraf iltrate each day in man. In general, individual amino acids are transp orted across the epithelial membrane of the proximal tubule by a sodiu m (Na+) dependent mechanism. This cotransport process utilizes the ene rgy of the Na+ gradient to enter the cell. The amino acid then exits t he basolateral surface and Na+ is pumped out by the Na+-K+-ATPase loca ted in the basolateral membrane. In addition to the cellular accumulat ion of amino acids across the luminal membrane, these compounds may be taken up by the cell from the basolateral surface. Most amino acids a re transported both individually and in a series of seven group specif ic processes. Human disorders of amino acid transport have been descri bed for six of the seven transport systems. The process of ontogeny of amino acid accumulation by the proximal tubule is a complex one and w ill be further discussed in this review. A number of factors including pH, ion dependency, electrogenicity of transport process, as well as a variety of hormonal factors, may contribute to the regulation of ami no acid transport. Gene expression of several amino acid transporters has been successfully performed using the oocyte of the frog Xenopus l aevis. Using this system, a number of transporters have been cloned. S uch a strategy will permit the cloning of virtually all transporter mo lecules, and thus we can anticipate the elucidation of the structure o f the transporters. However, for a comprehensive understanding of cyto skeletal interactions protein phosphorylation and phospholipid domains and their linkage to the primary structure of the transporter need to be studied. The future for research in this area is indeed a bright o ne.