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Titolo:
A NEW FAMILY OF PROTEINS (RBAT AND 4F2HC) INVOLVED IN CATIONIC AND ZWITTERIONIC AMINO-ACID-TRANSPORT - A TALE OF 2 PROTEINS IN SEARCH OF A TRANSPORT FUNCTION
Autore:
PALACIN M;
Indirizzi:
UNIV BARCELONA,FAC BIOL,DEPT BIOQUIM & FISIOL,AVE DIAGONAL 645 E-08028 BARCELONA SPAIN
Titolo Testata:
Journal of Experimental Biology
, volume: 196, anno: 1994,
pagine: 123 - 137
SICI:
0022-0949(1994)196:<123:ANFOP(>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
XENOPUS-LAEVIS OOCYTES; PROXIMAL STRAIGHT TUBULES; BORDER MEMBRANE-VESICLES; MONOCLONAL-ANTIBODY 4F2; RABBIT KIDNEY CORTEX; HEAVY-CHAIN; MESSENGER-RNA; RAT-KIDNEY; L-CYSTINE; EXPRESSION CLONING;
Keywords:
RBAT; 4F2HC; SYSTEM B(O,+); SYSTEM Y(+)L; AMINO ACID TRANSPORT; CYSTINURIA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
53
Recensione:
Indirizzi per estratti:
Citazione:
M. Palacin, "A NEW FAMILY OF PROTEINS (RBAT AND 4F2HC) INVOLVED IN CATIONIC AND ZWITTERIONIC AMINO-ACID-TRANSPORT - A TALE OF 2 PROTEINS IN SEARCH OF A TRANSPORT FUNCTION", Journal of Experimental Biology, 196, 1994, pp. 123-137

Abstract

The currently identified cDNA clones of mammalian amino acid transporters can be grouped into five different families. One family is composed of the proteins rBAT and the heavy chain (hc) of the cell surface antigen 4F2. RNAs encoding these two proteins induce a system b(0,+)-like (rBAT) and a system y(+)L-like (4F2hc) activity in Xenopus oocytes. Surprisingly, rBAT and 4F2hc do not seem to be pore-forming proteins. This finding supports the hypothesis that rBAT and 4F2hc are subunitsor modulators of the corresponding amino acid transport systems. Expression of rBAT in oocytes induces high-affinity transport of cystine, which is shared with transport of cationic and zwitterionic amino acids. The rBAT gene is expressed mainly in kidney and small intestine. The rBAT protein is localized to the microvilli of proximal straight tubules of the kidney and mucosa from the small intestine. This finding is consistent with the involvement of rBAT in a high-affinity resorption system for cystine in the proximal straight tubule of the nephron. All of these characteristics suggest that rBAT is a good candidate for a cystinuria gene. Cystinuria is an inheritable defect in high-affmitytransport of cystine, shared with cationic amino acids, through epithelial cells of the renal tubule and intestinal tract. Very recently, point missense mutations have been found in the rBAT gene of cystinuriapatients. The most frequent rBAT mutation, M467T (threonine substitution of methionine at residue 467) nearly abolished the amino acid transport activity elicited by rBAT in oocytes. This result offers convincing evidence that rBAT is a cystinuria gene. Biochemical, cytological and genetic approaches are now needed to delineate the mechanism of action of rBAT and 4F2hc in the transport of amino acids

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Documento generato il 28/01/21 alle ore 06:43:15