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Sodium Dicarboxylate Transporter (NADC) Antibodies
The sodium-dicarboxylate cotransporters (SLC 13), which transport succinate and other Krebs cycle intermediates, fall into 2 categories based on their substrate affinity, low affinity and high affinity. Both the low- and high-affinity transporters play an important role in the handling of citrate by the kidneys. The two different Na+-coupled dicarboxylate transporters (NADC) have been identified in mammalian tissues. These are NADC1 and NADC3 (NADC2 is found in C. Elegans). NADC1 is Na+-coupled, electrogenic, and exhibits low affinity for its dicarboxylate substrates. This isoform is expressed primarily in the brush border membrane of intestinal and renal epithelial cells. The physiological function of NADC1 is to absorb the intermediates of the citric acid cycle, such as citrate, succinate, alpha-ketoglutarate, fumarate, and malate, in the intestine and kidney. NADC3 is also a Na+-coupled and electrogenic dicarboxylate transporter, but it exhibits relatively higher affinity for its substrates compared with NADC1. The NADC3 is expressed primarily in the basolateral membrane of intestinal and renal epithelial cells. However, it is also found in tissues such as liver, placenta, and brain. NADC3 in the kidney is involved in generating the driving force for the organic anion transporter OAT1 to facilitate the active entry of organic anions into the tubular cells across the basolateral membrane. In the brain, NADC3 mediates the cellular uptake of N-acetylaspartate, a process closely linked to myelination. Therefore, the physiological functions of the NADC may extend beyond the mediation of cellular entry of citric acid cycle intermediates. Recently, a third member of this family in mammals has been identified, Na+-coupled citrate transporter (NACT), mediates the cellular uptake of citrate in a Na+-coupled manner. NADC-1, (SLC13A2
gene) is involved in a sodium dicarboxylate cotransport, an electrogenic
process, coupling 3 sodium ions to the transport of each divalent anion
substrate. NADC-1 is a 586aa protein in mouse, 587aa in rat and 592aa in human
(chr 17p11.1-q11.1). Invitro translation of human NADC-1 produced an
approximately 48kD protein. The deduced aa sequence of human NADC-1 is 78%
identical to rabbit NADC-1 and 47% to rat sodium sulfate transporter. NADC-1
transporter is a low affinity, sodium dependent, and pH-insensitive transporter
of succinate, its transport of citrate is stimulated by acidic pH. NACT, is 568aa protein in human (chr 17p13.2) and 572aa in rat, NaCT is expressed in liver, testis and brain in rat and shows preference for citrate over dicarboxylates; it may play a role in cellular utilization of citrate in blood for the synthesis of fatty acids and cholesterol and for the generation of energy.
m=mouse; r=rat; h=human; b=bovine; c=chicken; d=dog; ~CT or ~NT=near C or N-terminus. EC=Extracellular; CL=Cytoplasmic loop; * Expected
antibody crossreactivity information is mostly based upon
high (>70%) sequence conservation of antigenic/control peptides in
various species. When antibody crossreactivity has actually been
experimentally confirmed in various species, it will be mentioned
in the appropriate data sheets. | |||||||||||||||||||||||||||||||||||||||||||
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© 2005 GENTAUR bvba |