Article

Modification of Tight Junction Structure and Permeability by Nutritional Means

Lankenau Institute for Medical Research, Princeton University, Wynnewood, PA 19096, USA.
Annals of the New York Academy of Sciences (Impact Factor: 4.38). 06/2009; 1165(1):99-112. DOI: 10.1111/j.1749-6632.2009.04028.x
Source: PubMed

ABSTRACT

The relative abundance of various claudin proteins of LLC-PK(1) renal epithelial tight junctions (TJs) is modulated by culturing the cells in a medium that is sharply reduced in the sulfur-containing amino acids, cysteine, cystine, and methionine. The functional result is an epithelial barrier that has a higher transepithelial electrical resistance and a decreased paracellular leak to D-mannitol (i.e., improved barrier function). This is accomplished without affecting the culture's confluent cell density, its short circuit current, or its hallmark differentiated property, Na(+)-dependent sugar transport. The implications of being able to enhance epithelial TJ barrier function by nutritional means are discussed, particularly in light of the ability of methionine-restrictive diets to enhance life span and forestall age-related morbidity.

    • "Deprivation of glutamine (Gln) from cell culture medium and inhibition of Gln synthetase using methionine sulfoximine, led to significant decreases in transepithelial resistance of Caco-2 cell monolayers and increased permeability[92]. Also the sulfur-containing amino acids, cystine, cysteine and methionine enhance epithelial TJ permeability[93]. It can be speculated that the mTG mediated nonspecific linking of these amino acids to other molecules can induce a state of deprivation/surplus at the intestinal epithelial level, thus indirectly affecting TJ performance. "

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    ABSTRACT: Tight junctions of epithelial and endothelial cells form selective barriers that regulate paracellular transport of solutes, immune cells, and drugs. Tight junctions consist of proteins that physically “seal” the tight junction but also form channels that allow for permeation between the cells, resulting in epithelial surfaces of different tightness. The tight junction proteins occludin, tricellulin, and at least 24 members of the claudin family are characterized by four transmembranal domains and two extracellular loops that, like teeth of a zipper, contact the appropriate loops from opposing cell membranes. Tight junctions are regulated in their molecular composition, ultrastructure, and function by intracellular scaffolding proteins and the cytoskeleton; such regulation serves normal, physiologic adaptation but also occurs in numerous diseases.
    Preview · Article · May 2009 · Annals of the New York Academy of Sciences
  • [Show abstract] [Hide abstract]
    ABSTRACT: Tight junctions of epithelial and endothelial cells form selective barriers that regulate paracellular transport of solutes, immune cells, and drugs. Tight junctions consist of proteins that physically "seal" the tight junction but also form channels that allow for permeation between the cells, resulting in epithelial surfaces of different tightness. The tight junction proteins occludin, tricellulin, and at least 24 members of the claudin family are characterized by four transmembranal domains and two extracellular loops that, like teeth of a zipper, contact the appropriate loops from opposing cell membranes. Tight junctions are regulated in their molecular composition, ultrastructure, and function by intracellular scaffolding proteins and the cytoskeleton; such regulation serves normal, physiologic adaptation but also occurs in numerous diseases.
    No preview · Article · Jun 2009 · Annals of the New York Academy of Sciences
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