Effect of Chloroquine on Thyroliberin Interaction with Clonal Rat Prolactin Cells

Tixier-Vidal, A; Moreau, Marie-Françoise; Picart, R; Gourdji, D.

doi:10.1159/000123298

Cited by 4 publications

(3 citation statements)

References 23 publications

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“…To our surprise, the membrane of the GERL cisternae, which is particularly apparent in both PRL cell types, was never labeled with the A-Ly-M, whereas it always contained abundant acid phosphatase-positive material (22). There is a large overlap between the present results and previous staining with Golgi antibodies of the same cell types (25), since both antibodies label the membranes of medial saccules, lysosomes, and endosome-like vacuoles, but not the secretory granule membrane.…”

Section: Figure 3 Lmmunochemical Staining Of the Plasma Membrane Of Gmentioning

confidence: 70%

Antibodies against a lysosomal membrane antigen recognize a prelysosomal compartment involved in the endocytic pathway in cultured prolactin cells.

Tougard¹,

Louvard²,

Picart³

et al. 1985

The Journal of Cell Biology

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Antibodies against a lysosomal membrane antigen (A-Ly-M) have recently been obtained and characterized (Reggio, H., D. Bainton, E. Harms, E. Coudrier, and D. Louvard, 1984, J. Cell Biol., 99:1511-1526. They recognize a 100,000-mol-wt antigen immunologically related to a purified [H+,K+]ATPase from pig gastric mucosa. In the present study, we have localized this antigen during adsorptive endocytosis in rat prolactin cells in culture using cationized ferritin (CF) as a tracer. CF was rapidly internalized (after 5 min) in coated pits and vesicles that were labeled by antibodies against clathrin. The tracer was then delivered (after 15 rain) to vacuoles and multivesicular bodies. These structures were labeled with A-Ly-M. These organelles were devoid of acid phosphatase activity. At later stages (after 30 min) CF was observed within larger structures that were strongly stained by A-Ly-M and displayed a strong acid phosphatase activity. These findings clearly indicate that A-Ly-M react with prelysosomal and lysosomal compartments involved in the endocytic pathway in cultured prolactin cells. The membrane of these structures therefore contains antigenic determinant(s) related to the 100,000-mol-wt polypeptide. Our results suggest that the prelysosomal structure stained by A-Ly-M may represent in GH3 cells the acidic prelysosomal compartment recently described in the early steps of endocytosis in other cell types (Tycko, B., and F. R. Maxfield, 1982, Cell, 28:643-651).Acidification of endocytic vesicles involved as an early step in adsorptive or receptor-mediated endocytosis has recently been demonstrated using pH-sensitive fluorescent probes (4,12,19,26). This rapid acidification occurs before the fusion of endocytic vesicles with lysosomes and in the absence of lysosomal hydrolases.To explain the molecular mechanisms responsible for the acidification of both the prelysosomal and lysosomal compartments, the existence of an ATP-dependent proton pump has been postulated (for review, see reference 16). Such an activity has recently been demonstrated pharmacologically using isolated brain clathrin-coated vesicles (3), partially isolated endosomes, and lysosomes taken from fibroblasts and macrophages (4), or intact permeabilized fibroblasts (29).A new approach for studying membrane components that are possibly involved in the acidification of the endocytic pathway is provided by the recently characterized antibodies against a lysosomal membrane fraction that recognize a 100,000-mol-wt antigen immunologically related to a purified [H+,K+]ATPase from pig gastric mucosa (17, 18). Immunoelectron microscope localization of this antigen in normal rat kidney cells, rat macrophages, and hepatocytes revealed its presence not only in the membrane of secondary lysosomes but also in the membranes of several intracellular organelles known to be involved in receptor-mediated endocytosis (4,12,19,26). Moreover, some patches on the plasma membrane and some Golgi cisternae were also labeled (18).This prompted us to localize this...

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Section: Figure 3 Lmmunochemical Staining Of the Plasma Membrane Of Gmentioning

confidence: 70%

Antibodies against a lysosomal membrane antigen recognize a prelysosomal compartment involved in the endocytic pathway in cultured prolactin cells.

Tougard¹,

Louvard²,

Picart³

et al. 1985

The Journal of Cell Biology

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“…To evaluate this hypothesis we applied compounds that disrupt ion channel processing and insertion at different stages in the protein synthesis-exocytosis pathway. Chloroquine (CQ) interferes with vesicle recycling [20], membrane fusion events [21], and Na + channel trafficking [10],[22],[23]. N-ethylmaleimide (NEM) is widely used to disrupt vesicle docking and recycling.…”

Section: Resultsmentioning

confidence: 99%

Circadian and Social Cues Regulate Ion Channel Trafficking

et al. 2009

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“…If CQ could inhibit endocytosis, metabolism of 3H Con A would be prevented. However, several investigators (21)(22)(23) have shown that CQ does not inhibit endocytosis to any appreciable degree.…”

Section: Discussionmentioning

confidence: 99%

Chloroquine inhibits the production of a mononuclear cell factor by inhibition of lectin binding

Baker

Baumgarten

Dwyer

1984

Arthritis & Rheumatism

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The effect of chloroquine (CQ) on the ability of normal human peripheral blood monocytes to produce a soluble mononuclear cell factor (MCF) capable of stimulating prostaglandins from adherent rheumatoid synovial cells was studied. CQ inhibited concanavalin A (Con A)-and bacterial peptidoglycan-induced MCF activity, but not colchicine-induced activity, in a dosedependent manner. After incubation with CQ for 20 minutes, ' H Con A binding was reduced by 50% ; and metabolism of pre-bound ' H Con A was inhibited. These data suggest that CQ can inhibit MCF production by inhibition of lectin binding, perhaps by inhibition of receptor recycling.Soluble peptide mediators originating from mononuclear cells are clearly important for communication among immunocompetenl cells. In addition, such mediators affect cells not classically considered to be immunocompetent, such as fibroblasts.Dayer et al (1) have described one such mediator produced by monocytes. which can markedly stimulate the production of prostaglandin E2 (PGE2) ~_ _ From the

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Effect of Chloroquine on Thyroliberin Interaction with Clonal Rat Prolactin Cells

Cited by 4 publications

References 23 publications

Antibodies against a lysosomal membrane antigen recognize a prelysosomal compartment involved in the endocytic pathway in cultured prolactin cells.

Antibodies against a lysosomal membrane antigen recognize a prelysosomal compartment involved in the endocytic pathway in cultured prolactin cells.

Circadian and Social Cues Regulate Ion Channel Trafficking

Chloroquine inhibits the production of a mononuclear cell factor by inhibition of lectin binding

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