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Pinches SA, Gribble SM, Beechey RB, et al. Preparation and characterization of basolateral membrane vesicles from pig and human colonocytes: the mechanism of glucose transport. Biochem J. 1993;294:529-34doi: 10.1042/bj2940529.
Pinches, S. A., Gribble, S. M., Beechey, R. B., Ellis, A., Shaw, J. M., & Shirazi-Beechey, S. P. (1993). Preparation and characterization of basolateral membrane vesicles from pig and human colonocytes: the mechanism of glucose transport. The Biochemical journal, 294529-34. https://doi.org/10.1042/bj2940529
Pinches, S A, et al. "Preparation and characterization of basolateral membrane vesicles from pig and human colonocytes: the mechanism of glucose transport." The Biochemical journal vol. 294 (1993): 529-34. doi: https://doi.org/10.1042/bj2940529
Pinches SA, Gribble SM, Beechey RB, Ellis A, Shaw JM, Shirazi-Beechey SP. Preparation and characterization of basolateral membrane vesicles from pig and human colonocytes: the mechanism of glucose transport. Biochem J. 1993 Sep 01;294:529-34. doi: 10.1042/bj2940529. PMID: 8396917; PMCID: PMC1134487.
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Biochem J. 1993 Sep 01;294:529-34. doi: 10.1042/bj2940529.

Preparation and characterization of basolateral membrane vesicles from pig and human colonocytes: the mechanism of glucose transport.

The Biochemical journal

S A Pinches, S M Gribble, R B Beechey, A Ellis, J M Shaw, S P Shirazi-Beechey

Affiliations

  1. Department of Biochemistry, University of Wales, Aberystwyth, Dyfed, U.K.

PMID: 8396917 PMCID: PMC1134487 DOI: 10.1042/bj2940529
Free PMC Article

Abstract

Membrane vesicles were isolated from the basolateral domains of pig and normal human colonocytes. The activity of the ouabain-sensitive K(+)-activated phosphatase, the basolateral membrane marker, was enriched 13-fold in these membrane vesicles over the original homogenate. The membranes displayed cross-reactions with antibodies to the (Na+/K+)ATPase and the RLA class I major histocompatibility antigen, both known indicators of the basolateral membrane. There was negligible contamination by other organelles and the luminal membrane, as revealed by marker-enzyme analysis and Western blotting, using an antibody to villin. The vesicles transported D-glucose in a cytochalasin B-inhibitable Na(+)-independent manner, with a Km of 28.1 +/- 0.8 mM and Vmax. of 3.1 +/- 0.4 nmol/s per mg of protein. The transport was inhibited by 2-deoxy-D-glucose and 3-O-methyl-D-glucose, but not by L-glucose or methyl-alpha-D-glucose. Probing the colonocyte basolateral membranes with an antibody against the C-terminus of the human liver GLUT 2 produced a cross-reaction at 52 kDa. These properties indicate the presence of a GLUT 2 isoform on the basolateral membranes of human and pig colonocytes.

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