Document Detail


Molecular characterization of the first aromatic nutrient transporter from the sodium neurotransmitter symporter family.
MedLine Citation:
PMID:  16888066     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Nutrient amino acid transporters (NATs, subfamily of sodium neurotransmitter symporter family SNF, a.k.a. SLC6) represent a set of phylogenetically and functionally related transport proteins, which perform intracellular absorption of neutral, predominantly essential amino acids. Functions of NATs appear to be critical for the development and survival in organisms. However, mechanisms of specific and synergetic action of various NAT members in the amino acid transport network are virtually unexplored. A new transporter, agNAT8, was cloned from the malaria vector mosquito Anopheles gambiae (SS). Upon heterologous expression in Xenopus oocytes it performs high-capacity, sodium-coupled (2:1) uptake of nutrients with a strong preference for aromatic catechol-branched substrates, especially phenylalanine and its derivatives tyrosine and L-DOPA, but not catecholamines. It represents a previously unknown SNF phenotype, and also appears to be the first sodium-dependent B(0) type transporter with a narrow selectivity for essential precursors of catecholamine synthesis pathways. It is strongly and specifically transcribed in absorptive and secretory parts of the larval alimentary canal and specific populations of central and peripheral neurons of visual-, chemo- and mechano-sensory afferents. We have identified a new SNF transporter with previously unknown phenotype and showed its important role in the accumulation and redistribution of aromatic substrates. Our results strongly suggest that agNAT8 is an important, if not the major, provider of an essential catechol group in the synthesis of catecholamines for neurochemical signaling as well as ecdysozoan melanization and sclerotization pathways, which may include cuticle hardening/coloring, wound curing, oogenesis, immune responses and melanization of pathogens.
Authors:
Ella A Meleshkevitch; Poincyane Assis-Nascimento; Lyudmila B Popova; Melissa M Miller; Andrea B Kohn; Elizabeth N Phung; Anita Mandal; William R Harvey; Dmitri Y Boudko
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  The Journal of experimental biology     Volume:  209     ISSN:  0022-0949     ISO Abbreviation:  J. Exp. Biol.     Publication Date:  2006 Aug 
Date Detail:
Created Date:  2006-08-04     Completed Date:  2006-11-02     Revised Date:  2014-09-10    
Medline Journal Info:
Nlm Unique ID:  0243705     Medline TA:  J Exp Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  3183-98     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Amino Acid Transport Systems / chemistry,  genetics,  physiology*
Amino Acids, Aromatic / metabolism*
Animals
Anopheles gambiae / anatomy & histology,  genetics,  metabolism*
Catecholamines / biosynthesis
Catechols / metabolism
Cloning, Molecular
Electric Conductivity
Insect Proteins / chemistry,  genetics,  physiology*
Molecular Sequence Data
Phylogeny
Plasma Membrane Neurotransmitter Transport Proteins / genetics
Protein Structure, Tertiary
RNA, Messenger / metabolism
Sequence Alignment
Signal Transduction / genetics
Xenopus
Grant Support
ID/Acronym/Agency:
R01 5R01 AI030464/AI/NIAID NIH HHS; R01 AI030464/AI/NIAID NIH HHS; R01 AI030464-14/AI/NIAID NIH HHS; R01 AI030464-15/AI/NIAID NIH HHS; R01 AI030464-16/AI/NIAID NIH HHS; R01 AI030464-17/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Amino Acid Transport Systems; 0/Amino Acids, Aromatic; 0/Catecholamines; 0/Catechols; 0/Insect Proteins; 0/Plasma Membrane Neurotransmitter Transport Proteins; 0/RNA, Messenger; LF3AJ089DQ/catechol

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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