Demonstration of protein absorption in the intestinal epithelium of fish and mice by laser scanning confocal microscopy
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Wan-fu Yue
Abstract
Selective permeability for small proteins and oligopeptides occurs in the intestinal epithelium of many animal species and humans. Whole proteins are sometimes endocytosed and undergo partial hydrolysis in intestinal epithelial cells with the probable release of essential oligopeptides into the bloodstream. Increased permeability to certain proteins can cause asthma and other metabolic disorders. Permeable proteins have also been successfully used to deliver vaccines or drugs via oral consumption. Protein absorption has been inferred in many cases and demonstrated in some cases by histochemical, tracer, and analytical techniques. However, the nature and importance of protein absorption remains largely unknown. Here, we demonstrate the movement of two lumenal proteins (GFP: 26 kDa and OFP: 23 kDa) across the intestinal epithelium of fish and mice using laser scanning confocal microscopy. The results provide evidence that small proteins can be taken up intact by intestinal epithelial cells, even though large proteins are digested to single amino acids or protein fragments before they are absorbed. Our results suggest that it is possible to orally administer some small proteinous medicines for therapeutic purposes.
©2010 by Walter de Gruyter Berlin New York
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Articles in the same Issue
- Guest Editorial
- Highlight: The Biology of Aging: Mechanisms and Intervention
- Highlight: 61th Mosbach Colloquium of the GBM ‘The Biology of Aging: Mechanisms and Intervention’
- Multiplex analysis of mitochondrial DNA pathogenic and polymorphic sequence variants
- The hypoxia-inducible factor HIF-1 functions as both a positive and negative modulator of aging
- E. coli hypoxia-inducible factor ArcA mediates lifespan extension in a lipoic acid synthase mutant by suppressing acetyl-CoA synthetase
- Glucose homeostasis and insulin sensitivity in growth hormone-transgenic mice: a cross-sectional analysis
- PROTEIN STRUCTURE AND FUNCTION
- New structural aspects of FKBP38 activation
- The neuronal proteins CIPP, Cypin and IRSp53 form a tripartite complex mediated by PDZ and SH3 domains
- CELL BIOLOGY AND SIGNALING
- Inhibition of interferon-α-induced signaling by hyperosmolarity and hydrophobic bile acids
- Role of the second disulfide bridge (Cys18-Cys274) in stabilizing the inactive AT1 receptor
- Demonstration of protein absorption in the intestinal epithelium of fish and mice by laser scanning confocal microscopy
- Non-genomic action of TCDD to induce inflammatory responses in HepG2 human hepatoma cells and in liver of C57BL/6J mice
- PROTEOLYSIS
- Amino acid residues modulating the activities of staphylococcal glutamyl endopeptidases
