IL4/PGE2 induction of an enlarged early endosomal compartment in mouse macrophages is Rab5-dependent

Wainszelbaum, Marisa J.; Proctor, Brandon M.; Pontow, Suzanne; Stahl, Philip D.; Barbieri, M. Alejandro

doi:10.1016/j.yexcr.2006.03.025

Cited by 55 publications

(53 citation statements)

References 42 publications

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“…Endosome-and lysosomeenriched fractions were isolated from cells by the flotation gradient fractionation method (38,39). Cells were harvested by being scraped into a mixture of 250 mM sucrose, 20 mM HEPES, and 0.5 mM EGTA at pH 7.0 (homogenization buffer [HB]) and immediately subjected to the isolation procedure.…”

Section: Cell Cultures (I) Olgsmentioning

confidence: 99%

The Major Myelin-Resident Protein PLP Is Transported to Myelin Membranes via a Transcytotic Mechanism: Involvement of Sulfatide

Baron

Ozgen

Klunder

et al. 2015

Molecular and Cellular Biology

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bMyelin membranes are sheet-like extensions of oligodendrocytes that can be considered membrane domains distinct from the cell's plasma membrane. Consistent with the polarized nature of oligodendrocytes, we demonstrate that transcytotic transport of the major myelin-resident protein proteolipid protein (PLP) is a key element in the mechanism of myelin assembly. Upon biosynthesis, PLP traffics to myelin membranes via syntaxin 3-mediated docking at the apical-surface-like cell body plasma membrane, which is followed by subsequent internalization and transport to the basolateral-surface-like myelin sheet. Pulse-chase experiments, in conjunction with surface biotinylation and organelle fractionation, reveal that following biosynthesis, PLP is transported to the cell body surface in Triton X-100 (TX-100)-resistant microdomains. At the plasma membrane, PLP transiently resides within these microdomains and its lateral dissipation is followed by segregation into 3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate (CHAPS)-resistant domains, internalization, and subsequent transport toward the myelin membrane. Sulfatide triggers PLP's reallocation from TX-100-into CHAPS-resistant membrane domains, while inhibition of sulfatide biosynthesis inhibits transcytotic PLP transport. Taking these findings together, we propose a model in which PLP transport to the myelin membrane proceeds via a transcytotic mechanism mediated by sulfatide and characterized by a conformational alteration and dynamic, i.e., transient, partitioning of PLP into distinct membrane microdomains involved in biosynthetic and transcytotic transport.

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Section: Cell Cultures (I) Olgsmentioning

confidence: 99%

The Major Myelin-Resident Protein PLP Is Transported to Myelin Membranes via a Transcytotic Mechanism: Involvement of Sulfatide

Baron

Ozgen

Klunder

et al. 2015

Molecular and Cellular Biology

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“…[7][8][9][10] IL-4, by itself, has profound effects on fluid phase and mannose receptor (MR)-dependent and independent endocytosis, as well as modifying other elements of the endocytic pathway. [11][12][13] However, the effects of IL-4 on phagocytosis of opsonized and unopsonized bacteria, yeasts, or other particles are not clear, [14][15][16] nor has the effect of phagocytic stimuli on intracellular signaling and secretion by IL-4-treated M⌽s been defined.…”

Section: Introductionmentioning

confidence: 99%

Alternative activation of macrophages by IL-4 impairs phagocytosis of pathogens but potentiates microbial-induced signalling and cytokine secretion

Varin

Mukhopadhyay

Herbein

et al. 2010

Blood

159

114

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Alternatively activated macrophages play an important role in host defense in the context of a T helper type 2 (Th2) microenvironment such as parasitic infection. However, the role of these macrophages during secondary challenge with Th1 pathogens is poorly defined. In this study, thioglycollate-elicited mouse peritoneal macrophages were treated with interleukin-4 (IL-4) or IL-13 in vitro and challenged with Neisseria meningitidis.

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“…Finally the relative Ca 2ϩ permeability of the ECC to K ϩ or Na ϩ (P Ca /P K ϭ 1.9) was slightly smaller but comparable with that of TRPV2 (P Ca /P Na ϭ 2.94) (28). The pharmacological similarity between the ECC and the TRPV2, together with the proteomics study (1), suggests that the ECC is likely a product of the TRPV2 channel or a closely related TRP gene family channel.…”

Section: Importance Of Ecc In Endocytosismentioning

confidence: 84%

“…The recent identification of the TRPV2 channel protein in an early endosomal fraction (1) has raised the possibility of characterizing the physiological roles of the TRP-like channel in the native environment of the endosome membrane. To achieve this goal, it would be necessary to apply the patch clamp technique directly to endosome membranes.…”

Section: From the Department Of Cell Biology And Physiology Washingtmentioning

confidence: 99%

Luminal Chloride-dependent Activation of Endosome Calcium Channels

Saito

Hanson

Schlesinger

2007

Journal of Biological Chemistry

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Although Ca2؉ release from early endosomes (EE) is important for the fusion of primary endosomes, the presence of an ion channel responsible for releasing calcium from the EE has not been shown. A recent proteomics study has identified the TRPV2 channel protein in EE, suggesting that transient receptor potential-like Ca 2؉ channels may be in endosomes. The submicron size of endosomes has made it difficult to study their ion channels in the past. We have overcome this problem by generating enlarged EE with the help of a hydrolysis-deficient SKD1/ VPS4B mutant in HEK293 cells. Here we report the first patch clamp recording of a novel endosome calcium channel (ECC) in these enlarged EE. The ECC shows a similar pharmacology to that of the TRPV2 channel. In addition, the ECC has a unique chloride-dependent regulation; it is inhibited by the endosome luminal chloride with a K 50 of 82 mM.A number of TRP 2 type calcium channels have been localized to intracellular vesicles; however, their physiological roles in situ have remained largely uncharacterized. The recent identification of the TRPV2 channel protein in an early endosomal fraction (1) has raised the possibility of characterizing the physiological roles of the TRP-like channel in the native environment of the endosome membrane. To achieve this goal, it would be necessary to apply the patch clamp technique directly to endosome membranes. Past attempts at such studies have been unsuccessful, mainly because of the submicron size of endosomes. We have been able to increase the size of the endosome membrane by introducing a hydrolysis-deficient mutant of SKD1/VPS4B (E235Q) into HEK293 cells. Overexpression of SKD1/VPS4B (E235Q), which disrupts endosome trafficking (2), leads to the formation of large endosomes (3-6 m in diameter) in HEK293 cells. Using these enlarged EE, we have made the first patch clamp recordings of a novel endosome calcium channel (ECC). This ECC was sensitive to Ͼ500 M La 3ϩ inhibition as reported in other TRP family channels, but was activated by 100 M La 3ϩ and by 200 M 2-aminoethoxydiphenyl borate (2-APB), whereas being insensitive to TRPV1 activator capsaicin. EXPERIMENTAL PROCEDURESHEK293 cells stably expressing the tetracycline-inducible SKD1/VPS4B (E235Q) gene (3) were treated with tetracycline 4 -6 h prior to the experiments. GFP-tagged SKD1/VPS4B (E235Q)-expressing cells were used to demonstrate co-localization of GFP-SKD1/VPS4B (E235Q) with endocytosed rhodamine sulfate. c-myc-SKD1/VPS4B (E235Q)-expressing cells were used to show Lysotracker Green negative staining in the rhodamine sulfate containing enlarged endosomes and were also used in patch clamp experiments.Enlarged endosomes of sizes from 3-6 m were visually identified and dissected manually with a glass electrode. Under the phase contrast microscope, enlarged endosomes were viewed as phase-bright (see Fig. 1C, circled). To facilitate slicing of the plasma membrane with an electrode, cells with enlarged endosomes, closer to the edge of cells, were used because cell thickness i...

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IL4/PGE2 induction of an enlarged early endosomal compartment in mouse macrophages is Rab5-dependent

Cited by 55 publications

References 42 publications

The Major Myelin-Resident Protein PLP Is Transported to Myelin Membranes via a Transcytotic Mechanism: Involvement of Sulfatide

The Major Myelin-Resident Protein PLP Is Transported to Myelin Membranes via a Transcytotic Mechanism: Involvement of Sulfatide

Alternative activation of macrophages by IL-4 impairs phagocytosis of pathogens but potentiates microbial-induced signalling and cytokine secretion

Luminal Chloride-dependent Activation of Endosome Calcium Channels

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