Calcium-induced inhibition of taurine transport in brush-border membrane vesicles from rabbit small intestine

Ysei Miyamoto, Palaniappan Kulanthaivel, Vadivel Ganapathy, Gary M. Whitford, Frederick H. Leibach

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

The influence of Ca2+ on the activity of the taurine transport system was investigated in rabbit small intestinal brush-border membrane vesicles. Preincubation of the brush-border membrane vesicles with Ca2+ prepared by the Mg2+-aggregation method markedly decreased the NaCl gradient-dependent uptake of taurine in these vesicles. Uptake of glucose and alanine, both dependent on a Na+ gradient, were also decreased by Ca2+-treatment, but their reduction was very small compared with that of taurine uptake. The inhibitory effect of Ca2+ was dose- and time-dependent. The inhibition was reduced by the presence of ethylene glycol-bis(β-amino ethyl ether)-N,N,N′-N′-tetraacetic acid during treatment of the membrane vesicles with Ca2+. Neomycin partially protected the taurine transporter activity from the Ca2+-induced inhibition, but indomethacin did not. 5-Nitro-2-(3-phenylpropylamino)benzoate, a Cl--channel blocker, did not increase taurine uptake in the Ca2+-treated membrane vesicles. It is concluded that the Ca2+-induced inhibition of taurine uptake in rabbit intestinal brush-border membrane vesicles is not due to accelerated dissipation of the ion gradient driving forces across the membrane but rather to a direct effect on the transporter, most likely mediated by the activation of the membrane-bound phospholipase C.

Original languageEnglish (US)
Pages (from-to)189-194
Number of pages6
JournalBBA - Biomembranes
Volume1030
Issue number2
DOIs
StatePublished - Dec 14 1990

Fingerprint

Taurine
Brushes
Microvilli
Small Intestine
Rabbits
Calcium
Membranes
Neomycin
Ethylene Glycol
Benzoates
Type C Phospholipases
Indomethacin
Alanine
Ether
Agglomeration
Chemical activation
Ions
Glucose
Acids

Keywords

  • (Rabbit)
  • Brush border
  • Calcium ion induced inhibition
  • Phospholipase C
  • Small intestine
  • Taurine transport

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

Cite this

Calcium-induced inhibition of taurine transport in brush-border membrane vesicles from rabbit small intestine. / Miyamoto, Ysei; Kulanthaivel, Palaniappan; Ganapathy, Vadivel; Whitford, Gary M.; Leibach, Frederick H.

In: BBA - Biomembranes, Vol. 1030, No. 2, 14.12.1990, p. 189-194.

Research output: Contribution to journalArticle

Miyamoto, Ysei ; Kulanthaivel, Palaniappan ; Ganapathy, Vadivel ; Whitford, Gary M. ; Leibach, Frederick H. / Calcium-induced inhibition of taurine transport in brush-border membrane vesicles from rabbit small intestine. In: BBA - Biomembranes. 1990 ; Vol. 1030, No. 2. pp. 189-194.
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AB - The influence of Ca2+ on the activity of the taurine transport system was investigated in rabbit small intestinal brush-border membrane vesicles. Preincubation of the brush-border membrane vesicles with Ca2+ prepared by the Mg2+-aggregation method markedly decreased the NaCl gradient-dependent uptake of taurine in these vesicles. Uptake of glucose and alanine, both dependent on a Na+ gradient, were also decreased by Ca2+-treatment, but their reduction was very small compared with that of taurine uptake. The inhibitory effect of Ca2+ was dose- and time-dependent. The inhibition was reduced by the presence of ethylene glycol-bis(β-amino ethyl ether)-N,N,N′-N′-tetraacetic acid during treatment of the membrane vesicles with Ca2+. Neomycin partially protected the taurine transporter activity from the Ca2+-induced inhibition, but indomethacin did not. 5-Nitro-2-(3-phenylpropylamino)benzoate, a Cl--channel blocker, did not increase taurine uptake in the Ca2+-treated membrane vesicles. It is concluded that the Ca2+-induced inhibition of taurine uptake in rabbit intestinal brush-border membrane vesicles is not due to accelerated dissipation of the ion gradient driving forces across the membrane but rather to a direct effect on the transporter, most likely mediated by the activation of the membrane-bound phospholipase C.

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