Sucrase-isomaltase is and adenosine 3′,5′-cyclic monophosphate-dependent epithelial chloride channel

Arthur L. Finn, Eldo V. Kuzhikandathil, Gerry S. Oxford, Yoshi Itoh-Lindstrom

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Background and Aims: We previously isolated a monoclonal antibody against a Necturus gallbladder epitope that blocks native adenosine 3′,5′-cyclic monophosphate (cAMP)-dependent chloride channels in intestine, gallbladder, urinary bladder, and airway epithelia in various animals. Methods: Using this antibody, we purified a 200-kilodalton protein that, when reconstituted in lipid bilayers, forms 9-pS chloride channels that are blocked by the antibody. Results: Amino acid sequencing of the purified protein showed strong homology to rabbit sucrase-isomaltase, an abundant intestinal enzyme. Western blot analysis of the in vitro-translated sucrase-isomaltase was indistinguishable from that of the protein used in the lipid bilayer studies. Expression of this protein in Chinese hamster ovary cells and in Xenopus laevis oocytes yielded cAMP-dependent chloride currents that in the latter system were blocked by the antibody. Conclusions: Because the monoclonal antibody blocks cAMP-dependent currents in epithelia as well as those produced both by the reconstituted and by the heterologously expressed protein, sucrase-isomaltase is a cAMP-dependent epithelial chloride channel. Thus an enzyme that can also function as an ion channel has been described for the first time.

Original languageEnglish (US)
Pages (from-to)117-125
Number of pages9
JournalGastroenterology
Volume120
Issue number1
StatePublished - 2001
Externally publishedYes

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Oligo-1,6-Glucosidase
Sucrase
Chloride Channels
Adenosine
Lipid Bilayers
Gallbladder
Proteins
Antibodies
Epithelium
Necturus
Monoclonal Antibodies
Protein Sequence Analysis
Xenopus laevis
Enzymes
Cricetulus
Ion Channels
Oocytes
Intestines
Chlorides
Epitopes

ASJC Scopus subject areas

  • Gastroenterology

Cite this

Finn, A. L., Kuzhikandathil, E. V., Oxford, G. S., & Itoh-Lindstrom, Y. (2001). Sucrase-isomaltase is and adenosine 3′,5′-cyclic monophosphate-dependent epithelial chloride channel. Gastroenterology, 120(1), 117-125.

Sucrase-isomaltase is and adenosine 3′,5′-cyclic monophosphate-dependent epithelial chloride channel. / Finn, Arthur L.; Kuzhikandathil, Eldo V.; Oxford, Gerry S.; Itoh-Lindstrom, Yoshi.

In: Gastroenterology, Vol. 120, No. 1, 2001, p. 117-125.

Research output: Contribution to journalArticle

Finn, AL, Kuzhikandathil, EV, Oxford, GS & Itoh-Lindstrom, Y 2001, 'Sucrase-isomaltase is and adenosine 3′,5′-cyclic monophosphate-dependent epithelial chloride channel', Gastroenterology, vol. 120, no. 1, pp. 117-125.
Finn AL, Kuzhikandathil EV, Oxford GS, Itoh-Lindstrom Y. Sucrase-isomaltase is and adenosine 3′,5′-cyclic monophosphate-dependent epithelial chloride channel. Gastroenterology. 2001;120(1):117-125.
Finn, Arthur L. ; Kuzhikandathil, Eldo V. ; Oxford, Gerry S. ; Itoh-Lindstrom, Yoshi. / Sucrase-isomaltase is and adenosine 3′,5′-cyclic monophosphate-dependent epithelial chloride channel. In: Gastroenterology. 2001 ; Vol. 120, No. 1. pp. 117-125.
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N2 - Background and Aims: We previously isolated a monoclonal antibody against a Necturus gallbladder epitope that blocks native adenosine 3′,5′-cyclic monophosphate (cAMP)-dependent chloride channels in intestine, gallbladder, urinary bladder, and airway epithelia in various animals. Methods: Using this antibody, we purified a 200-kilodalton protein that, when reconstituted in lipid bilayers, forms 9-pS chloride channels that are blocked by the antibody. Results: Amino acid sequencing of the purified protein showed strong homology to rabbit sucrase-isomaltase, an abundant intestinal enzyme. Western blot analysis of the in vitro-translated sucrase-isomaltase was indistinguishable from that of the protein used in the lipid bilayer studies. Expression of this protein in Chinese hamster ovary cells and in Xenopus laevis oocytes yielded cAMP-dependent chloride currents that in the latter system were blocked by the antibody. Conclusions: Because the monoclonal antibody blocks cAMP-dependent currents in epithelia as well as those produced both by the reconstituted and by the heterologously expressed protein, sucrase-isomaltase is a cAMP-dependent epithelial chloride channel. Thus an enzyme that can also function as an ion channel has been described for the first time.

AB - Background and Aims: We previously isolated a monoclonal antibody against a Necturus gallbladder epitope that blocks native adenosine 3′,5′-cyclic monophosphate (cAMP)-dependent chloride channels in intestine, gallbladder, urinary bladder, and airway epithelia in various animals. Methods: Using this antibody, we purified a 200-kilodalton protein that, when reconstituted in lipid bilayers, forms 9-pS chloride channels that are blocked by the antibody. Results: Amino acid sequencing of the purified protein showed strong homology to rabbit sucrase-isomaltase, an abundant intestinal enzyme. Western blot analysis of the in vitro-translated sucrase-isomaltase was indistinguishable from that of the protein used in the lipid bilayer studies. Expression of this protein in Chinese hamster ovary cells and in Xenopus laevis oocytes yielded cAMP-dependent chloride currents that in the latter system were blocked by the antibody. Conclusions: Because the monoclonal antibody blocks cAMP-dependent currents in epithelia as well as those produced both by the reconstituted and by the heterologously expressed protein, sucrase-isomaltase is a cAMP-dependent epithelial chloride channel. Thus an enzyme that can also function as an ion channel has been described for the first time.

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