The Reorganization of the Golgi Complex in Anoxic Pancreatic Acinar Cells

Merisko, Elaine M.; Fletcher, Maryann D.; Palade, George E.

doi:10.1097/00006676-198603000-00001

Cited by 45 publications

(34 citation statements)

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“…In general, they occurred close to the ER cisternae and, in some instances, to vesicular protrusions of the ER (data not shown, but see below, Fig. 3, a and b), which resembled the transitional elements of the ER described in the exocrine pancreas (15,21,35,41). The tubulo-vesicular structures were morphologically distinguishable from the ER and Golgi stacks thanks to the circular appearance of the area (average diameter <1 #m), and the close clustering of the vesicles and tubules.…”

Section: Immunoelectron Microscopy Of Infected Cells Incubated At 15~supporting

confidence: 54%

“…Therefore, there appears to be no preferential localization in the perinuclear area, and the more frequent topological association was with the ER. In a few instances, the tubulovesicular units were near a specialized region of the ER that shows several features of the transitional elements of the ER as described in the exocrine pancreas (15,21,35,41). The ER in tissue cultured cells has yet to be morphologically characterized, thus it remains to be seen whether the tubulovesicular units we described are related to the "transitional elements" of the ER present in Vero cells.…”

Section: Discussionmentioning

confidence: 73%

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Immunocytochemical analysis of the transfer of vesicular stomatitis virus G glycoprotein from the intermediate compartment to the Golgi complex.

Lotti¹,

Torrisi²,

Pascale³

et al. 1992

The Journal of Cell Biology

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Abstract. We performed an immunocytochemical analysis to study the transfer of a marker protein (G glycoprotein coded by vesicular stomatitis virus ts 045 strain) from the intermediate compartment to the Golgi stacks in infected Vero cells. The intermediate compartment seemed to consist of about 30--40 separate units of clustered small vesicles and short tubules. The units contained Rab2 protein and were spread throughout the cytoplasm, with a ratio of about 6:4 in the peripheral versus perinuclear site. Time-course experiments revealed a progressive ~ransfer of G glycoprotein from the intermediate compartment to the Golgi stacks, while the tubulo-vesicular units did not appear to change their intracellular distribution. Moreover, the labeling density of peripheral and perinuclear units decreased in parallel during the transfer. These results support the notion that the intermediate compartment is a station in the secretory pathway, and that a vesicular transport connects this station to the Golgi complex.

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Section: Immunoelectron Microscopy Of Infected Cells Incubated At 15~supporting

confidence: 54%

Section: Discussionmentioning

confidence: 73%

Immunocytochemical analysis of the transfer of vesicular stomatitis virus G glycoprotein from the intermediate compartment to the Golgi complex.

Lotti¹,

Torrisi²,

Pascale³

et al. 1992

The Journal of Cell Biology

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“…We know of only two previous reports on the in vivo accumulation of structures matching the description of microcages: one was in pancreatic acinar cells deprived of oxygen (33,36) and the other in mosquito oocytes deprived of their normal supply of blood lipoprotein (39). Whether these conditions also involve some degree of cytoplasmic acidification remains to be seen, but seems quite likely.…”

Section: The Formation Of Microcagesmentioning

confidence: 99%

Hypertonic media inhibit receptor-mediated endocytosis by blocking clathrin-coated pit formation.

Heuser

Anderson

1989

The Journal of Cell Biology

875

707

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Abstract. Two seemingly unrelated experimental treatments inhibit receptor mediated endocytosis: (a) depletion of intracellular K ÷ (Larkin, J. M., M. S. Brown, J. L. Goldstein, and R. G. W. Anderson. 1983. Cell. 33:273-285); and (b) treatment with hypertonic media (Daukas, G., and S. H. Zigmond. 1985. J. Cell Biol. 101:1673-1679. Since the former inhibits the formation of clathrin-coated pits (Larkin, J. M., W. D. Donzell, and R. G. W. Anderson. 1986. J. Cell Biol. 103:2619-2627, we were interested in determining whether hypertonic treatment has the same effect, and if so, why. Fibroblasts (human or chicken) were incubated in normal saline made hypertonic with 0.45 M sucrose, then broken open by sonication and freezeetched to generate replicas of their inner membrane surfaces. Whereas untreated cells display typical geodesic lattices of clathrin under each coated pit, hypertonic cells display in addition a number of empty clathrin "microcages'. At first, these appear around the edges of normal coated pit lattices. With further time in hypertonic medium, however, normal lattices largely disappear and are replaced by accumulations of microcages. Concomitantly, low density lipoprotein (LDL) receptors lose their normal clustered distribution and become dispersed all over the cell surface, as seen by fluorescence microscopy and freeze-etch electron microscopy of LDL attached to the cell surface. Upon return to normal medium at 37°C, these changes promptly reverse. Within 2 min, small clusters of LDL reappear on the surfaces of cells and normal clathrin lattices begin to reappear inside; the size and number of these receptor/clathrin complexes returns to normal over the next 10 min. Thus, in spite of their seeming unrelatedness, both K ÷ depletion and hypertonic treatment cause coated pits to disappear, and both induce abnormal clathrin polymerization into empty microcages. This suggests that in both cases, an abnormal formation of microcages inhibits endocytosis by rendering clathrin unavailable for assembly into normal coated pits. C LATHRIN coated pits are the primary plasma membrane specialization involved in the uptake of a wide variety of molecules by receptor-mediated endocytosis (4, 38). Two broad functions have been attributed to these regions of membrane: (a) molecular determinants associated with the clathrin lattice may cause receptors to become clustered; and (b) the clathrin lattice may in some way control the invagination of the membrane to form endocytic vesicles. To understand the molecular mechanisms underlying these two aspects of coated pit function, one approach is to search for treatments that inhibit endocytosis and then to characterize the effects of these treatments on coated pit structure and receptor clustering.Currently, three experimental treatments are known to inhibit receptor-mediated endocytosis: (a) depletion of intracellular potassium (22, 24-26, 29, 30, 34, 40), (b) exposure of cells to hypertonic media (10), and (c) acidification of the cytoplasm (11,16, 21,41). Whereas potassi...

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“…As with anoxia, prolonged exposure to low temperatures leads to an accumulation of coat-protein complexes in the cytosol of mammalian cells (Goud et al, 1985;Merisko et al, 1986). In plants, prolonged cold treatment causes dramatic changes in the endomembrane system (Mollenhauer et al, 1975), also presumably a consequence of the prevention of vesicle traffic.…”

Section: Atsec21p and Atsec23p Are Both Membrane And Cytosol Locatedmentioning

confidence: 99%

Arabidopsis Sec21p and Sec23p Homologs. Probable Coat Proteins of Plant COP-Coated Vesicles1

et al. 1999

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Intracellular protein transport between the endoplasmic reticulum (ER) and the Golgi apparatus and within the Golgi apparatus is facilitated by COP (coat protein)-coated vesicles. Their existence in plant cellshas not yet been demonstrated, although the GTPbinding proteins required for coat formation have been identified. We have generated antisera against glutathione-S-transferase-fusion proteins prepared with cDNAs encoding the Arabidopsis Sec21p and Sec23p homologs (AtSec21p and AtSec23p, respectively). The former is a constituent of the COPI vesicle coatomer, and the latter is part of the Sec23/24p dimeric complex of the COPII vesicle coat. Cauliflower (Brassica oleracea) inflorescence homogenates were probed with these antibodies and demonstrated the presence of AtSec21p and AtSec23p antigens in both the cytosol and membrane fractions of the cell. The membrane-associated forms of both antigens can be solubilized by treatments typical for extrinsic proteins. The amounts of the cytosolic antigens relative to the membranebound forms increase after cold treatment, and the two antigens belong to different protein complexes with molecular sizes comparable to the corresponding nonplant coat proteins. Sucrose-densitygradient centrifugation of microsomal cell membranes from cauliflower suggests that, although AtSec23p seems to be preferentially associated with ER membranes, AtSec21p appears to be bound to both the ER and the Golgi membranes. This could be in agreement with the notion that COPII vesicles are formed at the ER, whereas COPI vesicles can be made by both Golgi and ER membranes. Both AtSec21p and AtSec23p antigens were detected on membranes equilibrating at sucrose densities equivalent to those typical for in vitro-induced COP vesicles from animal and yeast systems. Therefore, a further purification of the putative plant COP vesicles was undertaken.

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The Reorganization of the Golgi Complex in Anoxic Pancreatic Acinar Cells

Cited by 45 publications

References 0 publications

Immunocytochemical analysis of the transfer of vesicular stomatitis virus G glycoprotein from the intermediate compartment to the Golgi complex.

Immunocytochemical analysis of the transfer of vesicular stomatitis virus G glycoprotein from the intermediate compartment to the Golgi complex.

Hypertonic media inhibit receptor-mediated endocytosis by blocking clathrin-coated pit formation.

Arabidopsis Sec21p and Sec23p Homologs. Probable Coat Proteins of Plant COP-Coated Vesicles1

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