Inhibition by brefeldin A of protein secretion from the apical cell surface of Madin-Darby canine kidney cells.

Low, Seng Hui; Wong, Siew Heng; Tang, Bor Luen; Tan, Pei Yi; Subramaniam, V.N.; Hong, Wanjin

doi:10.1016/s0021-9258(18)55184-x

Cited by 63 publications

(10 citation statements)

References 28 publications

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“…The response of cells to BFA is known to vary. For example, the Golgi apparatus in PtK1 cells is resistant to BFA (Ktistakis et al, 1991) at concentrations that cause tubulation of early endosomes in these cells (Lippincott-Schwartz et al, 1991), and at low concentrations of BFA the same is true of MDCK cells (Hunziker et al, 1991;Low et al, 1991). Our data indicate that in ART20 cells the situation is the opposite: the Golgi apparatus is more sensitive to a low concentration (I t~g/rnl) of BFA than the early endosomes.…”

Section: Discussionmentioning

confidence: 61%

In AtT20 and HeLa cells brefeldin A induces the fusion of tubular endosomes and changes their distribution and some of their endocytic properties.

Tooze

Hollinshead

1992

The Journal of Cell Biology

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Abstract. We have studied the effects of brefeldin A (BFA) on the tubular endosomes in AtT20 and HeLa cells (Tooze, J., and M. Hollinshead. 1991. J. Cell Biol. 115:635-653) by electron microscopy of cells labeled with three endocytic tracers, HRP, BSA-gold, and transfenin conjugated to HRP, and by immunofluorescence microscopy. For the latter we used antibodies specific for transferrin receptor, and, in the case of AtT20 ceils, also antibodies specific for synaptophysin. In HeLa cells BFA at concentrations ranging from 1 #g to 10/~g/ml causes the dispersed patches of network of preexisting tubular early endosomes to be incorporated within 5 min into tubules ~50 nm in diameter but up to 40-50/~m long. These long, straight tubular endosomes are aligned along microtubules; they branch relatively infrequently to form an open network or reticulum extending from the cell periphery to the microtubule organizing center (MTOC). As the incubation with BFA is prolonged beyond 5 min, a steady state is reached in which many tubules are located in a dense network enclosing the centrioles, with branches extending in a more open network to the periphery. This effect of BFA, which is fully reversed within 15-30 rain of washing out, is inhibited by preincubating the cells with sodium azide and 2-deoxy-D-glucose. In AtT20 cells BFA at 5 ftg/ml or above causes the same sorts of changes, preexisting tubular endosomes are recruited into a more continuous endosomal network, and there is a massive accumulation of this network around the MTOC. Maintenance of the BFA-induced endosomal reticulum in both cell types is dependent upon the integrity of microtubules. In AtT20 cells BFA at 1 #g/ml has no detectable effect on the early endosomal system but the Golgi stacks are converted to clusters of tubules and vesicles that remain in the region of the MTOC during prolonged incubations. Therefore, the Golgi apparatus in these cells is more sensitive to BFA than the early endosomes. The morphological evidence suggests that all the tubular early endosomes in BFA-treated HeLa and AtT20 cells are linked together in a single reticulum. Consistent with this, incubations as short as 1-3 min with 10 or 20 mg/ml HRP in the medium result in the entire endosomal reticulum in most of the BFA-treated cells being filled with HRP reaction product. Furthermore, using HRP at 0.1-0.5 mg/ml in the, concentrations that are too low to label the dispersed tubular endosomes in control AtT20 cells after 60 min uptake, we obtained heavy labeling of the networks in the BFAtreated cells. Apparently HRP is concentrated within the lumen of the tubular endosomal reticulum induced by BFA in AtT20 cells. In AtT20 ceils neither the morphology nor the immunocytochemical properties of late endosomes/prelysosomes were altered by incubations with BFA at concentrations ranging from 1 to 20/zg/ml for up to 180 min, the longest time tested.

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Section: Discussionmentioning

confidence: 61%

In AtT20 and HeLa cells brefeldin A induces the fusion of tubular endosomes and changes their distribution and some of their endocytic properties.

Tooze

Hollinshead

1992

The Journal of Cell Biology

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“…(1991) and Hunziker et al (1991) who examined the ability of a polarized epithelial cell to carry out secretion and transcytosis . Low et al (1991) demonstrated that in MDCK cells, where the Golgi apparatus but not the endosomal system is resistant to low concentrations of BFA, protein secretion at the apical surface is inhibited by BFA while basolateral secretion is enhanced . Using MDCK cells in culture, Hunziker et al (1991) demonstrated that IgA can be taken up from the basolateral surface in a normal fashion in the presence of BFA, but its release at the apical surface is inhibited .…”

Section: Receptor-mediated Recycling In Bfa-treated Cellsmentioning

confidence: 99%

“…Based on both kinetic and pharmacologic data, the inhibition of binding of coat proteins to Golgi membranes seems to be the most proximal effect of BFA on this organelle . It is of significance that the Golgi apparatus in some cells appears to be resistant to the effects of BFA (Kistakis et al ., 1991 ;Hunziker et al ., 1991 ;Low et al ., 1991 ;Sandvig et al ., 1991) . In both PtK1 cells (Kistakis et al ., 1991) and MDCK cells (Hunziker et al, 1991) the association of ß-COP with the Golgi apparatus is not changed with BFA treatment .…”

Section: Pbssible Role Of Tlrimeric G Proteins In Regulatingmentioning

confidence: 99%

Brefeldin A: insights into the control of membrane traffic and organelle structure.

Klausner

Donaldson

Lippincott‐Schwartz

1992

The Journal of Cell Biology

1,789

1,221

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“…The known Golgi-associated adaptors (HA-I/AP-1 and O-COP) are rapidly dissociated from the membrane by brefeldin A (20) (F. Brodsky, personal communication) . In MDCK cells brefeldin A blocks transport to the apical surface from both the TGN and the basolateral surface, suggesting that adaptors are involved in these processes (30,41). Permeabilized cells and cell-free systems have been used to reconstitute budding of vesicles from the TGN (54,64), and budding of transcytotic vesicle from early endosomes (M. Bomsel and K. Mostov, unpublished results) .…”

Section: Sorting Machinerymentioning

confidence: 99%

Plasma membrane protein sorting in polarized epithelial cells.

Mostov

Apodaca

Aroeti

et al. 1992

The Journal of Cell Biology

263

177

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Inhibition by brefeldin A of protein secretion from the apical cell surface of Madin-Darby canine kidney cells.

Cited by 63 publications

References 28 publications

In AtT20 and HeLa cells brefeldin A induces the fusion of tubular endosomes and changes their distribution and some of their endocytic properties.

In AtT20 and HeLa cells brefeldin A induces the fusion of tubular endosomes and changes their distribution and some of their endocytic properties.

Brefeldin A: insights into the control of membrane traffic and organelle structure.

Plasma membrane protein sorting in polarized epithelial cells.

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