Zobrazeno 1 - 10
of 21
pro vyhledávání: '"K E, Mostov"'
Publikováno v:
Traffic (Copenhagen, Denmark). 1(6)
Quantitative confocal microscopic analyses of living, polarized MDCK cells demonstrate different pH profiles for apical and basolateral endocytic pathways, despite a rapid and extensive intersection between the two. Three-dimensional characterization
Publikováno v:
The Journal of biological chemistry. 275(40)
Protease-activated receptor-1 (PAR1), a G protein-coupled receptor (GPCR) for thrombin, is irreversibly activated by a proteolytic mechanism, then internalized and degraded in lysosomes. The latter is critical for temporal fidelity of thrombin signal
Publikováno v:
The Journal of biological chemistry. 275(27)
Caveolin-1 is a principal component of caveolae membranes that may function as a transformation suppressor. For example, the human caveolin-1 gene is localized to a suspected tumor suppressor locus (D7S522; 7q31.1) that is deleted in human cancers, i
Publikováno v:
The Journal of biological chemistry. 273(26)
Brefeldin A (BFA) treatment of Caco-2 cells (5 microg/ml for 12 h) reduced by 90% the cholesterol, but not the phospholipid (PL), levels of the basolateral membrane (BLM), thus altering its PL/cholesterol molar ratio from 2.6 to 22.0, and decreasing
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 155(2)
Polymeric IgA (pIgA) is transcytosed across epithelial cells and into external secretions by the polymeric Ig receptor (pIgR). Binding of dimeric IgA (dIgA) to the pIgR stimulates transcytosis of the pIgR. The pIgA in secretions is found as dimers (d
Autor:
K E, Mostov
Publikováno v:
Histology and histopathology. 10(2)
The plasma membrane of polarized epithelial cells is divided into apical and basolateral surfaces with different compositions. Proteins can be sent directly from the trans Golgi network (TGN) to either surface, or can be sent first to one surface and
Publikováno v:
The Journal of biological chemistry. 269(22)
S726 of the cytoplasmic domain of the polymeric immunoglobulin receptor (pIgR) resides within a consensus sequence for phosphorylation by protein kinases A, G, and C, and casein kinase II. Mutation of S726 to Ala and expression of this mutant pIgR in
Autor:
M, Bomsel, K E, Mostov
Publikováno v:
The Journal of biological chemistry. 268(34)
In endosomes the polymeric immunoglobulin receptor (pIgR) is sorted into transcytotic vesicles. Transcytosis of the pIgR in polarized Madin-Darby canine kidney (MDCK) cells is regulated both by phosphorylation of Ser664 and by binding of ligand, dime
Autor:
G, Apodaca, K E, Mostov
Publikováno v:
The Journal of biological chemistry. 268(31)
Two signals are known that regulate the entry of the polymeric immunoglobulin receptor (pIgR) into the transcytotic pathway: binding of the ligand, dimeric IgA, and phosphorylation of Ser664 in the cytoplasmic domain of the receptor. Mutation of Ser6
Publikováno v:
The Journal of biological chemistry. 268(16)
In the classical secretory pathway proteins containing a signal peptide are translocated from the cytoplasm of the cell into the lumen of the endoplasmic reticulum (ER). From the ER they are transported to the Golgi apparatus and finally to the plasm