The endocytic pathway for H‐ferritin established in live MOLT‐4 cells by laser scanning confocal microscopy

Moss, Dennis; Hibbs, Alan R.; Stenzel, Deborah; Powell, L. W.; Halliday, June W.

doi:10.1111/j.1365-2141.1994.tb05113.x

Cited by 11 publications

(5 citation statements)

References 36 publications

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“…Taken together these results indicate that the primary method for ferritin uptake into oligodendrocyte progenitors is by clathrin-dependent, receptor mediated endocytosis. Indeed, our results are consistent with microscopic analyses suggesting ferritin is internalized in Molt 4 cells via an endocytic pathway (Moss et al, 1994) and is associated with clathrin coated vesicles in HeLa cells (Bretscher and Thomson, 1983).…”

Section: Discussionsupporting

confidence: 81%

Oligodendrocyte progenitor cells internalize ferritin via clathrin-dependent receptor mediated endocytosis

et al. 2000

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Section: Discussionsupporting

confidence: 81%

Oligodendrocyte progenitor cells internalize ferritin via clathrin-dependent receptor mediated endocytosis

et al. 2000

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“…Our demonstration that TIM-2 binds to H-ferritin is the first identification of a cell surface receptor for ferritin, although the existence of ferritin receptors was postulated previously, based on saturable binding of ferritin to the surface of several cell types, including B and T lymphocytes. Thus, binding of H-ferritin to lymphocytes is increased in mitogen-stimulated cells, and purified H-ferritin forms surface patches on T cells, after which it is endocytosed into lysosomes (23,24,32). Studies using MOLT-4 human T cells indicated that they express a receptor for H-ferritin with an association constant of ‫ف‬ 7 ϫ 10 Ϫ 7 L/mol, and that the receptor is increased on proliferating cells (25,26).…”

Section: Discussionmentioning

confidence: 99%

TIM-2 is expressed on B cells and in liver and kidney and is a receptor for H-ferritin endocytosis

Chen

Chung

et al. 2005

The Journal of Experimental Medicine

197

186

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T cell immunoglobulin-domain and mucin-domain (TIM) proteins constitute a receptor family that was identified first on kidney and liver cells; recently it was also shown to be expressed on T cells. TIM-1 and -3 receptors denote different subsets of T cells and have distinct regulatory effects on T cell function. Ferritin is a spherical protein complex that is formed by 24 subunits of H- and L-ferritin. Ferritin stores iron atoms intracellularly, but it also circulates. H-ferritin, but not L-ferritin, shows saturable binding to subsets of human T and B cells, and its expression is increased in response to inflammation. We demonstrate that mouse TIM-2 is expressed on all splenic B cells, with increased levels on germinal center B cells. TIM-2 also is expressed in the liver, especially in bile duct epithelial cells, and in renal tubule cells. We further demonstrate that TIM-2 is a receptor for H-ferritin, but not for L-ferritin, and expression of TIM-2 permits the cellular uptake of H-ferritin into endosomes. This is the first identification of a receptor for ferritin and reveals a new role for TIM-2.

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“…It is also noteworthy that the cell lines that are particularly sensitive to trioxane dimers 14a and 14b all express transferrin. − Transferrin is an endogenous protein that transports iron from the circulation into cells. Most cancer cell lines express higher surface cell concentrations of transferrin receptors than normal cells and have higher rates of iron influx 26a.…”

Section: Antitumor Activitiesmentioning

confidence: 99%

Antimalarial and Antitumor Evaluation of Novel C-10 Non-Acetal Dimers of 10β-(2-Hydroxyethyl)deoxoartemisinin

et al. 2004

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Four series of C-10 non-acetal dimers were prepared from key trioxane alcohol 10beta-(2-hydroxyethyl)deoxoartemisinin (9b). All of the dimers prepared displayed potent low nanomolar antimalarial activity versus the K1 and HB3 strains of Plasmodium falciparum. The most potent compound assayed was phosphate dimer 14a, which was greater than 50 times more potent than the parent drug artemisinin and about 15 times more potent than the clinically used acetal artemether. In contrast to their potent activity versus malaria parasites, virtually all of the dimers expressed poor anticancer activity apart from the trioxane phosphate ester dimers 14a and 14b, which expressed nanomolar growth inhibitory (GI50) values versus a range of cancer cell lines in the NCI 60 human cell line screen. Further detailed studies on these dimers in vitro in HL60 cells demonstrate that both phosphate ester dimers (14a and 14b) are more potent than the anticancer agent doxorubicin. Interestingly, phosphate ester monomers 9c and 9d, antimalarially active in the low nanomolar region versus P. falciparum, are inactive as anticancer agents even at concentrations in the millimolar region. This observation emphasizes the importance of two trioxane units for high antiproliferative activity, and we propose that the nature of the linker in dimers of this type plays a crucial role in imparting potent anticancer activity.

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The endocytic pathway for H‐ferritin established in live MOLT‐4 cells by laser scanning confocal microscopy

Cited by 11 publications

References 36 publications

Oligodendrocyte progenitor cells internalize ferritin via clathrin-dependent receptor mediated endocytosis

Oligodendrocyte progenitor cells internalize ferritin via clathrin-dependent receptor mediated endocytosis

TIM-2 is expressed on B cells and in liver and kidney and is a receptor for H-ferritin endocytosis

Antimalarial and Antitumor Evaluation of Novel C-10 Non-Acetal Dimers of 10β-(2-Hydroxyethyl)deoxoartemisinin

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