The Human GeneSLC25A29, of Solute Carrier Family 25, Encodes a Mitochondrial Transporter of Basic Amino Acids

Maternally derived amino acids (AA) are essential for early conceptus development, and specific transporters enhance histotrophic AA content during early ruminant pregnancy. In the present study we investigated AA transporter expression in early equine conceptuses and endometrium, during normal pregnancy and after induction of embryo–uterus asynchrony. ‘Normal’ conceptuses and endometrium were recovered on Days 7, 14, 21 and 28 after ovulation. To investigate asynchrony, Day 8 embryos were transferred to recipient mares on Day 8 or Day 3, and conceptuses were recovered 6 or 11 days later. Endometrial expression of AA transporters solute carrier family 38 member 2 (SLC38A2), solute carrier family 1 members 4 and 5 (SLC1A4 and SLC1A5) increased during early pregnancy, whereas solute carrier family 7 member 8 (SLC7A8), solute carrier family 43 member 2 (SLC43A2) and solute carrier family 7 member 1 (SLC7A1) SLC7A8, SLC43A2 and SLC7A1 expression decreased and the expression of solute carrier family 1 member 1(SLC1A1) and solute carrier family 7 member 2 (SLC7A2) was unaffected. In conceptus membranes, most transporters studied were upregulated, either after Day 14 (solute carrier family 7 member 5 – SLC7A5, SLC38A2, SLC1A4, SLC1A5 and SLC7A1) or Day 21 (SLC43A2 and SLC7A2). Asynchronous ET indicated that endometrial SLC1A5, SLC1A1 and SLC7A8 are primarily regulated by conceptus factors and/or longer exposure to progesterone. In conclusion, AA transporters are expressed in early equine conceptus membranes and endometrium in specific spatiotemporal patterns. Because conceptuses express a wider range of transporters than the endometrium, we speculate that the equine yolk sac has recruited AA transporters to ensure adequate nutrient provision during an unusually long preimplantation period.

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Identification of a mitochondrial transporter for basic amino acids in Arabidopsis thaliana by functional reconstitution into liposomes and complementation in yeast

The Plant Journal ◽

10.1046/j.1365-313x.2003.01685.x ◽

2003 ◽

Vol 33 (6) ◽

pp. 1027-1035 ◽

Cited By ~ 68

Author(s):

Mary Elizabeth Hoyos ◽

Luigi Palmieri ◽

Timothy Wertin ◽

Roberto Arrigoni ◽

Joseph C. Polacco ◽

...

Keyword(s):

Amino Acids ◽

Arabidopsis Thaliana ◽

Basic Amino Acids ◽

Mitochondrial Transporter

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SLC6 neurotransmitter transporter family (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database

IUPHAR/BPS Guide to Pharmacology CITE ◽

10.2218/gtopdb/f144/2019.4 ◽

2019 ◽

Vol 2019 (4) ◽

Author(s):

Stefan Bröer ◽

Gary Rudnick

Keyword(s):

Amino Acids ◽

Plasma Membrane ◽

Amino Acid ◽

Crystal Structures ◽

Structural Motif ◽

Solute Carrier Family ◽

Neurotransmitter Transporter ◽

Transporter Family ◽

Bacterial Homolog ◽

Solute Carrier

Members of the solute carrier family 6 (SLC6) of sodium- and (sometimes chloride-) dependent neurotransmitter transporters [29, 22, 70] are primarily plasma membrane located and may be divided into four subfamilies that transport monoamines, GABA, glycine and neutral amino acids, plus the related bacterial NSS transporters [99]. The members of this superfamily share a structural motif of 10 TM segments that has been observed in crystal structures of the NSS bacterial homolog LeuTAa, a Na+-dependent amino acid transporter from Aquiflex aeolicus [126] and in several other transporter families structurally related to LeuT [45].

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Fine mapping* of the bovine solute carrier family 25, member 4 (SLC25A4) gene to BTA27q14-q15 by fluorescence in situ hybridization and radiation hybrid mapping

Animal Genetics ◽

10.1046/j.1365-2052.2002.t01-15-00886.x ◽

2002 ◽

Vol 33 (4) ◽

pp. 318-320

Author(s):

C. Drogemuller ◽

H. Kuiper ◽

G. Hauke ◽

J. L. Williams ◽

O. Distl

Keyword(s):

In Situ Hybridization ◽

Fluorescence In Situ Hybridization ◽

Fine Mapping ◽

Radiation Hybrid ◽

Radiation Hybrid Mapping ◽

Solute Carrier Family ◽

Hybrid Mapping ◽

Solute Carrier

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Does the polyamine carrier system absorb basic amino acids?

Gastroenterology ◽

10.1016/s0016-5085(01)80702-2 ◽

2001 ◽

Vol 120 (5) ◽

pp. A142-A142

Author(s):

J GASKEY ◽

E SEIDEL

Keyword(s):

Amino Acids ◽

Carrier System ◽

Basic Amino Acids

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Faculty Opinions recommendation of Deorphanization of GPRC6A: a promiscuous L-alpha-amino acid receptor with preference for basic amino acids.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1024356.287883 ◽

2005 ◽

Author(s):

Joseph Heitman

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Acid Receptor ◽

Basic Amino Acids ◽

Alpha Amino Acid

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Atypical amino acids inhibit histidine, valine, or lysine transport into rat brain

AJP Regulatory Integrative and Comparative Physiology ◽

10.1152/ajpregu.1983.245.4.r556 ◽

1983 ◽

Vol 245 (4) ◽

pp. R556-R563 ◽

Cited By ~ 1

Author(s):

J. K. Tews ◽

A. E. Harper

Keyword(s):

Amino Acids ◽

Rat Brain ◽

Blood Brain Barrier ◽

Brain Slices ◽

Aromatic Amino Acids ◽

Brain Barrier ◽

Basic Amino Acids ◽

Large Neutral Amino Acids ◽

Neutral Amino Acids ◽

Single Meal

Transport of histidine, valine, or lysine into rat brain slices and across the blood-brain barrier (BBB) was determined in the presence of atypical nonprotein amino acids. Competitors of histidine and valine transport in slices were large neutral amino acids including norleucine, norvaline, alpha-aminooctanoate, beta-methylphenylalanine, and alpha-aminophenylacetate. Less effective were aromatic amino acids with ring substituents; ineffective were basic amino acids and omega-amino isomers of norleucine and aminooctanoate. Lysine transport was moderately depressed by homoarginine or ornithine plus arginine; large neutral amino acids were also similarly inhibitory. Histidine or valine transport across the BBB was also strongly inhibited by large neutral amino acids that were the most effective competitors in the slices (norvaline, norleucine, alpha-aminooctanoate, and alpha-aminophenylacetate); homoarginine and 8-aminooctanoate were ineffective. Homoarginine, ornithine, and arginine almost completely blocked lysine transport, but the large neutral amino acids were barely inhibitory. When rats were fed a single meal containing individual atypical large neutral amino acids or homoarginine, brain pools of certain large neutral amino acids or of arginine and lysine, respectively, were depleted.

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Autosomal recessive congenital hereditary corneal dystrophy associated with a novel SLC4A11 mutation in two consanguineous Tunisian families

British Journal of Ophthalmology ◽

10.1136/bjophthalmol-2020-318204 ◽

2021 ◽

pp. bjophthalmol-2020-318204

Author(s):

Zohra Chibani ◽

Imen Zone Abid ◽

Peter Söderkvist ◽

Jamel Feki ◽

Mounira Hmani Aifa

Keyword(s):

Autosomal Recessive ◽

Corneal Transplantation ◽

Gene Mutations ◽

In Silico Analysis ◽

Corneal Dystrophy ◽

Solute Carrier Family ◽

Transporter Protein ◽

Bicarbonate Transporter ◽

Corneal Clouding ◽

Solute Carrier

BackgroundAutosomal recessive congenital hereditary corneal dystrophy (CHED) is a rare isolated developmental anomaly of the eye characterised by diffuse bilateral corneal clouding that may lead to visual impairment requiring corneal transplantation. CHED is known to be caused by mutations in the solute carrier family 4 member 11 (SLC4A11) gene which encodes a membrane transporter protein (sodium bicarbonate transporter-like solute carrier family 4 member 11).MethodsTo identify SLC4A11 gene mutations associated with CHED (OMIM: #217700), genomic DNA was extracted from whole blood and sequenced for all exons and intron-exon boundaries in two large Tunisian families.ResultsA novel deletion SLC4A11 mutation (p. Leu479del; c.1434_1436del) is responsible for CHED in both analysed families. This non-frameshift mutation was found in a homozygous state in affected members and heterozygous in non-affected members. In silico analysis largely support the pathogenicity of this alteration that may leads to stromal oedema by disrupting the osmolarity balance. Being localised to a region of alpha-helical secondary structure, Leu479 deletion may induce protein-compromising structural rearrangements.ConclusionTo the best of our knowledge, this is the first clinical and genetic study exploring CHED in Tunisia. The present work also expands the list of pathogenic genotypes in SLC4A11 gene and its associated clinical diagnosis giving more insights into genotype–phenotype correlations.

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