Intestinal fat and iron transport, goblet cell mucus secretion, and cellular changes in protein deficiency observed with the electron microscope

1965 ◽  
Vol 10 (12) ◽  
pp. 1004-1023 ◽  
Author(s):  
James A. Freeman ◽  
Jack C. Geer
2015 ◽  
Vol 8 (4) ◽  
pp. 712-719 ◽  
Author(s):  
G M H Birchenough ◽  
M EV Johansson ◽  
J K Gustafsson ◽  
J H Bergström ◽  
G C Hansson

Cell ◽  
2014 ◽  
Vol 156 (5) ◽  
pp. 1045-1059 ◽  
Author(s):  
Marta Wlodarska ◽  
Christoph A. Thaiss ◽  
Roni Nowarski ◽  
Jorge Henao-Mejia ◽  
Jian-Ping Zhang ◽  
...  

2020 ◽  
Vol 9 (2) ◽  
pp. 239-255 ◽  
Author(s):  
Rainelli Koumangoye ◽  
Salma Omer ◽  
Mustafa H. Kabeer ◽  
Eric Delpire

2013 ◽  
Vol 33 (5) ◽  
Author(s):  
Christina Helmis ◽  
Christine Blechner ◽  
Hongying Lin ◽  
Michaela Schweizer ◽  
Georg W. Mayr ◽  
...  

In colon enterocytes and in well-differentiated colon cancer CaCo-2 cells, InsP6 (inositol hexakisphosphate) inhibits iron uptake by forming extracellular insoluble iron/InsP6 complexes. In this study, we confirmed that CaCo-2 cells are not able to take up iron/InsP6 but, interestingly, found that the cells are able to internalize metal-free and Cr3+-bound InsP6. Thus, the inability of CaCo-2 cells to take up iron/InsP6 complexes seems to be due to the iron-bound state of InsP6. Since recently we demonstrated that the highly malignant bronchial carcinoma H1299 cells internalize and process InsP6, we examined whether these cells may be able to take up iron/InsP6 complexes. Indeed, we found that InsP6 dose-dependently increased uptake of iron and demonstrated that in the iron-bound state InsP6 is more effectively internalized than in the metal-free or Cr3+-bound state, indicating that H1299 cells preferentially take up iron/InsP6 complexes. Electron microscope and cell fraction assays indicate that after uptake H1299 cells mainly stored InsP6/iron in lysosomes as large aggregates, of which about 10% have been released to the cytosol. However, this InsP6-mediated iron transport had no significant effects on cell viability. This result together with our finding that the well-differentiated CaCo-2 cells did not, but the malignant H1299 cells preferentially took up iron/InsP6, may offer the possibility to selectively transport cytotoxic substances into tumour cells.


1966 ◽  
Vol 30 (1) ◽  
pp. 119-136 ◽  
Author(s):  
Marian Neutra ◽  
C. P. Leblond

It is known that colonic goblet cells utilize glucose to synthesize the carbohydrate portion of mucus glycoprotein. To determine the intracellular site of this synthesis, glucose-H3 was injected into 10-g rats. At 5, 20, 40 min, 1, 1½, and 4 hr after injection, segments of colon were fixed and prepared for electron microscope radioautography. By 5 min after injection, label had been incorporated into substances present in the flattened saccules of the Golgi complex. At 20 min, both Golgi saccules and nearby mucigen granules were labeled. By 40 min, mucigen granules carried almost all detectable radioactivity. Between 1 and 4 hr, these labeled granules migrated from the supranuclear region to the apical membrane; here, they were extruded singly, retaining their limiting membrane. The evidence indicates that the Golgi saccule is the site where complex carbohydrate is synthesized and is added to immigrant protein to form the complete glycoprotein of mucus. The Golgi saccule, distended by this material, becomes mucigen granules. It is roughly estimated that one saccule is released by each Golgi stack every 2 to 4 min: a conclusion implying continuous renewal of Golgi stacks. It appears that the Golgi synthesis, intracellular migration, and release of mucus glycoprotein occur continually throughout the life of the goblet cell.


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