scholarly journals Aboral changes in d-glucose transport by human intestinal brush-border membrane vesicles

1986 ◽  
Vol 237 (1) ◽  
pp. 229-234 ◽  
Author(s):  
M K Bluett ◽  
N N Abumrad ◽  
N Arab ◽  
F K Ghishan
Keyword(s):  
Glucose Transport ◽  
Brush Border ◽  
Terminal Ileum ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Intestinal Brush Border Membrane ◽  
Proximal Intestine ◽  
Taurocholate Transport ◽  
Colonic Transport

D-Glucose transport was investigated in isolated brush-border membrane vesicles from human small intestine. Characteristics of D-glucose transport from the jejunum were compared with that in the mid and terminal ileum. Jejunal and mid-ileal D-glucose transport was Na+-dependent and electrogenic. The transient overshoot of jejunal D-glucose transport was significantly greater than corresponding values in mid-ileum. The terminal ileum did not exhibit Na+-dependent D-glucose transport, but did exhibit Na+-dependent taurocholate transport. Na+-glucose co-transport activity as measured by tracer-exchange experiments was greatest in the jejunum, and diminished aborally. We conclude that D-glucose transport in man is Na+-dependent and electrogenic in the proximal intestine and directly related to the activity of D-glucose-Na+ transporters present in the brush-border membranes. D-Glucose transport in the terminal ileum resembles colonic transport of D-glucose.

Transport of guanidine in rabbit intestinal brush-border membrane vesicles

1988 ◽  
Vol 255 (1) ◽  
pp. G85-G92 ◽  
Author(s):  
Y. Miyamoto ◽  
V. Ganapathy ◽  
F. H. Leibach
Keyword(s):  
Brush Border ◽  
Time Course ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Extracellular Ph ◽  
Brush Border Membrane Vesicles ◽  
Intestinal Brush Border Membrane ◽  
Intestinal Brush Border ◽  
Dependent Transport ◽  
Proximal Intestine

The characteristics of guanidine uptake were studied in brush-border membrane vesicles isolated from the rabbit proximal intestine. Guanidine uptake was manyfold greater in the presence of an outward-directed H+ gradient (intracellular pH = 5.5; extracellular pH = 7.2) than in the absence of a H+ gradient (intracellular and extracellular pH = 7.2). The time course of guanidine uptake exhibited an overshoot phenomenon in the presence of the H+ gradient, indicating occurrence of uphill transport. This H+ gradient-stimulated guanidine uptake was not due to an inside-negative H+-diffusion potential because carbonyl cyanide 4-trifluoromethoxyphenylhydrazone, a protonophore, failed to have any effect on guanidine uptake. Moreover, the transient uphill transport of guanidine was observed even in voltage-clamped membrane vesicles. However, under the conditions that effectively dissipated the H+ gradient, there was no active transport of guanidine. This H+ gradient-dependent transport mechanism for guanidine is distinct from the Na+-H+ exchanger, because amiloride did not inhibit guanidine uptake even at a concentration as high as 100 microM. These data provide evidence for the presence of a guanidine-H+ antiport system in the rabbit intestinal brush-border membrane. The presence of a carrier for guanidine in these membranes is further substantiated by the trans-stimulation of the uptake of radiolabeled guanidine by unlabeled guanidine and by the inhibition of guanidine uptake by imipramine under equilibrium exchange conditions.(ABSTRACT TRUNCATED AT 250 WORDS)

Glucose transport during Ageing by human intestinal brush-border membrane vesicles

1989 ◽  
Vol 48 (1) ◽  
pp. 33-41 ◽  
Author(s):  
Maria Teresa Vicenzini ◽  
Teresa Iantomasi ◽  
Maria Stio ◽  
Fabio Favilli ◽  
Paolo Vanni ◽  
...  
Keyword(s):  
Glucose Transport ◽  
Brush Border ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Intestinal Brush Border Membrane ◽  
Intestinal Brush Border

Divalent cations and vitamin B12 uptake by intestinal brush-border membrane vesicles

1980 ◽  
Vol 239 (6) ◽  
pp. G452-G456
Author(s):  
R. C. Beesley ◽  
C. D. Bacheller
Keyword(s):  
Vitamin B12 ◽  
Brush Border ◽  
Brush Border Membrane ◽  
Divalent Cations ◽  
Intrinsic Factor ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Tetraacetic Acid ◽  
Intestinal Brush Border Membrane ◽  
Intestinal Brush Border

Brush-border membrane vesicles from hamster intestine were employed to investigate uptake (binding) of vitamin B12 (B12). Ileal vesicles took up 25 times more B12 than did jejunal vesicles. Uptake of B12 by ileal vesicles was dependent on intrinsic factor (IF) and required Ca2+. Increasing the Ca2+ concentration caused an increase in uptake of B12 reaching a maximum at approximately 8 mM Ca2+. At high Ca2+ concentrations, 6–8 mM, Mg2+ had little effect on uptake of B12. At low Ca2+ concentrations, up to 2 mM, Mg2+ stimulated B12 uptake. Mg2+, Mn2+, and, to a lesser extent, Sr2+ stimulated Ca2+-dependent B12 uptake, but Zn2+, Ba2+, Na+, K+, and La3+ did not. B12 was apparently not metabolized and was bound as IF-B12 complex, which could be removed with (ethylenedinitrilo)tetraacetic acid (EDTA). Our results suggest that two types of divalent cation reactive sites are involved in binding of IF-B12. One is Ca2+ specific. The other is less specific reacting with Mg2+, Mn2+, Sr2+, and perhaps Ca2+ itself, thereby stimulating Ca2+-dependent binding of IF-B12 to its ileal receptor.

Uphill transport of beta-alanine in intestinal brush-border membrane vesicles

1990 ◽  
Vol 259 (3) ◽  
pp. G372-G379 ◽  
Author(s):  
Y. Miyamoto ◽  
H. Nakamura ◽  
T. Hoshi ◽  
V. Ganapathy ◽  
F. H. Leibach
Keyword(s):  
Brush Border ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Beta Alanine ◽  
Intestinal Brush Border Membrane ◽  
High Affinity ◽  
Intestinal Brush Border ◽  
Proximal Small Intestine ◽  
Uptake Process

The characteristics of beta-alaline uptake were studied in brush-border membrane vesicles isolated from the proximal small intestine of rabbits and were compared with those of L-alpha-alanine uptake. The uptake of beta-alanine as well as L-alpha-alanine was significantly stimulated by imposing an inwardly directed Na+ gradient. Studies on transstimulation and substrate specificity provide evidence that the transport system serving beta-alanine is distinct from the system serving alpha-alanine. The beta-system also accepts taurine as a substrate. The Na(+)-dependent uptakes of beta-alanine and L-alpha-alanine were differentially influenced by anions. The order in which anions supported uptake was Cl- = SCN- greater than F- greater than NO3- = SO2(-4) for beta-alanine, whereas it was SCN- greater than F- = Cl- = NO3- greater than SO2(-4) for L-alpha-alanine. Cl- appeared to be the preferred anion to support the uptake of beta-alanine. beta-Alanine uptake was greater in the presence of an inwardly directed Cl- gradient than in the presence of Cl- at equal concentrations on both sides of the membrane. The uptake was maximal when a Na+ gradient and a Cl- gradient were present simultaneously. The NaCl gradient-driven beta-alanine uptake was stimulated by an inside-negative K(+)-diffusion potential induced by valinomycin, showing that the uptake process is electrogenic. Stoichiometric analyses suggest that multiple Na+ and one Cl- are associated with the uptake of one beta-alanine molecule. The kinetic study shows that the transporter for beta-alanine is a high-affinity, low-capacity system (Kt = 46 +/- 1 microM; Vmax = 30 +/- 1 pmol.mg protein-1.15 s-1).

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