Receptor-Mediated Transcytosis of Leptin through Human Intestinal Cells In Vitro
Author(s) -
Philippe Cammisotto,
Moı̈se Bendayan,
Alain Théophile Sané,
Michel Dominguez,
Carole Garofalo,
Émile Lévy
Publication year - 2010
Publication title -
international journal of cell biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.587
H-Index - 53
eISSN - 1687-8884
pISSN - 1687-8876
DOI - 10.1155/2010/928169
Subject(s) - transcytosis , endocytosis , leptin , clathrin , leptin receptor , receptor , microbiology and biotechnology , golgi apparatus , receptor mediated endocytosis , brefeldin a , medicine , endocrinology , biology , chemistry , endoplasmic reticulum , obesity
Gastric Leptin is absorbed by duodenal enterocytes and released on the basolateral side towards the bloodstream. We investigated in vitro some of the mechanisms of this transport. Caco-2/15 cells internalize leptin from the apical medium and release it through transcytosis in the basal medium in a time- temperature-dependent and saturable fashion. Leptin receptors are revealed on the apical brush-border membrane of the Caco-2 cells. RNA-mediated silencing of the receptor led to decreases in the uptake and basolateral release. Leptin in the basal medium was found bound to the soluble form of its receptor. An inhibitor of clathrin-dependent endocytosis (chlorpromazine) decreased leptin uptake. Confocal immunocytochemistry and the use of brefeldin A and okadaic acid revealed the passage of leptin through the Golgi apparatus. We propose that leptin transcytosis by intestinal cells depends on its receptor, on clathrin-coated vesicles and transits through the Golgi apparatus.
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