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Journal of Cell Science, Vol 113, Issue 24 4435-4440, Copyright © 2000 by Company of Biologists
JOURNAL ARTICLES |
W Wang, S Uzzau, SE Goldblum and A Fasano
Division of Pediatric Gastroenterology and Nutrition, Gastrointestinal Pathophysiology Section, Center for Vaccine Development, Baltimore, MD 21201, USA.
Intercellular tight junctions are dynamic structures involved in vectorial transport of water and electrolytes across the intestinal epithelium. Zonula occludens toxin derived from Vibrio cholerae interacts with a specific intestinal epithelial surface receptor, with subsequent activation of a complex intracellular cascade of events that regulate tight junction permeability. We postulated that this toxin may mimic the effect of a functionally and immunologically related endogenous modulator of intestinal tight junctions. Affinity-purified anti-zonula occludens toxin antibodies and the Ussing chamber assay were used to screen for one or more mammalian zonula occludens toxin analogues in both fetal and adult human intestine. A novel protein, zonulin, was identified that induces tight junction disassembly in non-human primate intestinal epithelia mounted in Ussing chambers. Comparison of amino acids in the active zonula occludens toxin fragment and zonulin permitted the identification of the putative receptor binding domain within the N-terminal region of the two proteins. Zonulin likely plays a pivotal role in tight junction regulation during developmental, physiological, and pathological processes, including tissue morphogenesis, movement of fluid, macromolecules and leukocytes between the intestinal lumen and the interstitium, and inflammatory/autoimmune disorders.
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 E. J. Israel, L. L. Levitsky, S. A. Anupindi, and M. B. Pitman Case 3-2005 - A 14-Year-Old Boy with Recent Slowing of Growth and Delayed Puberty N. Engl. J. Med., January 27, 2005; 352(4): 393 - 403. [Full Text] [PDF]
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 J. R. Broughman, R. M. Brandt, C. Hastings, T. Iwamoto, J. M. Tomich, and B. D. Schultz Channel-forming peptide modulates transepithelial electrical conductance and solute permeability Am J Physiol Cell Physiol, June 1, 2004; 286(6): C1312 - C1323. [Abstract] [Full Text] [PDF]
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M G Clemente, S De Virgiliis, J S Kang, R Macatagney, M P Musu, M R Di Pierro, S Drago, M Congia, and A Fasano Early effects of gliadin on enterocyte intracellular signalling involved in intestinal barrier function Gut, February 1, 2003; 52(2): 218 - 223. [Abstract] [Full Text] [PDF]
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A Fasano Toxins and the gut: role in human disease Gut, May 1, 2002; 50(90003): iii9 - 14. [Abstract] [Full Text] [PDF]
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A FASANO Intestinal zonulin: open sesame! Gut, August 1, 2001; 49(2): 159 - 162. [Full Text] [PDF]
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 M. Di Pierro, R. Lu, S. Uzzau, W. Wang, K. Margaretten, C. Pazzani, F. Maimone, and A. Fasano Zonula Occludens Toxin Structure-Function Analysis. IDENTIFICATION OF THE FRAGMENT BIOLOGICALLY ACTIVE ON TIGHT JUNCTIONS AND OF THE ZONULIN RECEPTOR BINDING DOMAIN J. Biol. Chem., May 25, 2001; 276(22): 19160 - 19165. [Abstract] [Full Text] [PDF]
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