Polarized transport of the polymeric immunoglobulin receptor in transfected rabbit mammary epithelial cells

Détails

ID Serval
serval:BIB_534D86EE1715
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Polarized transport of the polymeric immunoglobulin receptor in transfected rabbit mammary epithelial cells
Périodique
Journal of Cell Biology
Auteur⸱e⸱s
Schaerer  E., Verrey  F., Racine  L., Tallichet  C., Reinhardt  M., Kraehenbuhl  J. P.
ISSN
0021-9525 (Print)
Statut éditorial
Publié
Date de publication
04/1990
Volume
110
Numéro
4
Pages
987-98
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Apr
Résumé
A cDNA for the rabbit low Mr polymeric immunoglobulin (poly-Ig) receptor was expressed in an immortalized rabbit mammary cell line. The intracellular routing of the receptor and its cell surface expression was analyzed in stably transfected cells grown on permeable supports. Initially the cells formed a monolayer with no transmural electrical resistance. All monolayer cells expressed the poly-Ig receptor and cytokeratin 7 filaments characteristic of luminal mammary cells but absent in myoepithelial cells. Within 7 d in culture, the cells underwent cytodifferentiation and formed a bilayer with a transepithelial electrical resistance of approximately 500 omega x cm2. Upper layer cells formed tight junctions with adjacent cells and gap junctions with basal cells. Expression of the poly-Ig receptor and cytokeratin 7 was restricted to the cells from the upper layer. The kinetics of receptor biosynthesis and processing was similar to that reported for rabbit mammary gland and rat liver. The receptor was cleaved at the apical cell surface and release of secretory component into the apical medium occurred with a half-time of approximately 2 h. Selective cell surface trypsinization combined with pulse-chase experiments served to determine at which cell surface domain newly synthesized receptor appeared first. The receptor was digested with a half-time of approximately 60 min with trypsin present in the basolateral medium and 90 min with apical trypsin. These data are consistent with selective targeting of newly synthesized receptor to the basolateral surface. The results indicate that transcytosis of the receptor from basolateral to apical membrane in the presence or the absence of its ligand requires approximately 30 min. Cleavage of the receptor by endogenous protease is not concomitant with its appearance at the apical surface, but requires additional time, thus explaining the presence of intact receptor on the apical membrane.
Mots-clé
Animals Antibodies, Monoclonal/diagnostic use Biological Transport Cell Differentiation Cells, Cultured Cloning, Molecular DNA/genetics Epithelial Cells Epithelium/immunology/ultrastructure Female Immunoglobulin G/immunology Intercellular Junctions/ultrastructure Lactation Mammary Glands, Animal/*immunology Membrane Glycoproteins/metabolism Microscopy, Electron Microvilli/ultrastructure Poly A/genetics Pregnancy RNA/genetics RNA, Messenger Rabbits Receptors, Immunologic Secretory Component/genetics/*metabolism *Transfection
Pubmed
Web of science
Open Access
Oui
Création de la notice
25/01/2008 15:05
Dernière modification de la notice
20/08/2019 14:08
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