Effects of acetaldehyde and/or ethanol on neutral amino acid transport systems in microvillous brush border membrane vesicles prepared from human placenta

1985 ◽  
Vol 41 (12) ◽  
pp. 1566-1568 ◽  
Author(s):  
M. Asai ◽  
O. Narita ◽  
S. Kashiwamata
Keyword(s):  
Amino Acid ◽  
Human Placenta ◽  
Brush Border ◽  
Amino Acid Transport ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Neutral Amino Acid ◽  
Transport Systems ◽  
Acid Transport

scholarly journals Studies of Amino Acid Transport into Brush Border Membrane Vesicles Isolated from Rat Small Intestine

1993 ◽  
Vol 64 (7) ◽  
pp. 700-708
Author(s):  
Kiyoshi TAJIMA ◽  
Ryozo TAKADA ◽  
Toru MORI ◽  
Hisao ITABASHI ◽  
Kei-ichiro SUGIMURA
Keyword(s):  
Small Intestine ◽  
Amino Acid ◽  
Brush Border ◽  
Amino Acid Transport ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Rat Small Intestine ◽  
Acid Transport

scholarly journals Reconstitution and identification of the major Na+-dependent neutral amino acid-transport protein from bovine renal brush-border membrane vesicles

1992 ◽  
Vol 281 (1) ◽  
pp. 95-102 ◽  
Author(s):  
F A Doyle ◽  
J D McGivan
Keyword(s):  
Amino Acid ◽  
Brush Border ◽  
Amino Acid Transport ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Acid Transport ◽  
Transport Activity ◽  
Renal Brush Border Membrane ◽  
Renal Brush Border

Amino acid transport activity from bovine renal brush-border membrane vesicles (BBMV) was reconstituted into phospholipid vesicles composed of phosphatidylcholine/5% stearylamine. Reconstitutable transport activity was enhanced in protein fractions binding to various lectins. When solubilized BBMV were fractionated on peanut lectin, a single protein band of average molecular mass 132 kDa was obtained. When this protein fraction was reconstituted into phospholipid membrane vesicles, amino acid transport activity was obtained with properties similar to those in native BBMV with regard to amino acid specificity, although the cation specificity was different. A monoclonal antibody which reacted with the same protein removed reconstitutable amino acid transport activity from solubilized BBMV. These findings may provide the first identification of a renal amino acid-transporting protein, although confirmation of this identification by other approaches will be required.

AMINO ACID TRANSPORT SYSTEMS IN BRUSH-BORDER MEMBRANE VESICLES FROM LEPIDOPTERAN ENTEROCYTES

1989 ◽  
Vol 143 (1) ◽  
pp. 87-100
Author(s):  
GIORGIO M. HANOZET ◽  
BARBARA GIORDANA ◽  
V. FRANCA SACCHI ◽  
PAOLO PARENTI
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Glutamic Acid ◽  
Brush Border ◽  
Amino Acid Transport ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Transport Systems ◽  
Acid Transport ◽  
Luminal Membrane

The presence of different potassium-dependent amino acid transport systems in the luminal membrane of the larval midgut of Philosamia cynthia Drury (Saturnidae, Lepidoptera) was investigated by means of countertransport experiments performed with brush-border membrane vesicles. The vesicles were preloaded with 14 different unlabelled amino acids, whose ability to elicit an intravesicular accumulation over the equilibrium value of six labelled amino acids (L-alanine, L-leucine, L-phenylalanine, L-glutamic acid, L-lysine and L-histidine) was tested. For histidine, the results were compared with those obtained from inhibition experiments, in which the same 14 amino acids were used as inhibitors on the cis side of the brush-border membrane. The data demonstrate the presence in the lepidopteran luminal membrane of distinct transport pathways for lysine and glutamic acid. The transport of most neutral amino acids, with the exclusionof glycine and proline, seems to occur through a system that may be similar to the neutral brush-border system (NBB) found in mammalian intestinal membranes. This system is also able to handle histidine.

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