Apical Transporters for Neutral Amino Acids: Physiology and Pathophysiology

Physiology ◽  
2008 ◽  
Vol 23 (2) ◽  
pp. 95-103 ◽  
Author(s):  
Stefan Bröer

Absorption of amino acids in kidney and intestine involves a variety of transporters for different groups of amino acids. This is illustrated by inherited disorders of amino acid absorption, such as Hartnup disorder, cystinuria, iminoglycinuria, dicarboxylic aminoaciduria, and lysinuric protein intolerance, affecting separate groups of amino acids. Recent advances in the molecular identification of apical neutral amino acid transporters has shed a light on the molecular basis of Hartnup disorder and iminoglycinuria.

Physiology ◽  
2005 ◽  
Vol 20 (2) ◽  
pp. 112-124 ◽  
Author(s):  
Manuel Palacín ◽  
Virginia Nunes ◽  
Mariona Font-Llitjós ◽  
Maite Jiménez-Vidal ◽  
Joana Fort ◽  
...  

Heteromeric amino acid transporters (HATs) are composed of a heavy ( SLC3 family) and a light ( SLC7 family) subunit. Mutations in system b0,+ (rBAT-b0,+AT) and in system y+L (4F2hc-y+LAT1) cause the primary inherited aminoacidurias (PIAs) cystinuria and lysinuric protein intolerance, respectively. Recent developments [including the identification of the first Hartnup disorder gene (B0AT1; SLC6A19)] and knockout mouse models have begun to reveal the basis of renal and intestinal reabsorption of amino acids in mammals.


2008 ◽  
Vol 88 (1) ◽  
pp. 249-286 ◽  
Author(s):  
Stefan Bröer

The transport of amino acids in kidney and intestine is critical for the supply of amino acids to all tissues and the homeostasis of plasma amino acid levels. This is illustrated by a number of inherited disorders affecting amino acid transport in epithelial cells, such as cystinuria, lysinuric protein intolerance, Hartnup disorder, iminoglycinuria, dicarboxylic aminoaciduria, and some other less well-described disturbances of amino acid transport. The identification of most epithelial amino acid transporters over the past 15 years allows the definition of these disorders at the molecular level and provides a clear picture of the functional cooperation between transporters in the apical and basolateral membranes of mammalian epithelial cells. Transport of amino acids across the apical membrane not only makes use of sodium-dependent symporters, but also uses the proton-motive force and the gradient of other amino acids to efficiently absorb amino acids from the lumen. In the basolateral membrane, antiporters cooperate with facilitators to release amino acids without depleting cells of valuable nutrients. With very few exceptions, individual amino acids are transported by more than one transporter, providing backup capacity for absorption in the case of mutational inactivation of a transport system.


1986 ◽  
Vol 20 (11) ◽  
pp. 1117-1121 ◽  
Author(s):  
Olli Simell ◽  
Ilkka Sipilä ◽  
Jukka Rajantie ◽  
David L Valle ◽  
Saul W Brusilow

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