The subcellular localization of immunoglobulin in mouse plasma cells, as studied with immunoferritin cytochemistry on ultrathin frozen sections

Geuze, Hans J.; Slot, Jan W.

doi:10.1002/aja.1001580206

Cited by 16 publications

(9 citation statements)

References 30 publications

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“…This observation is in accordance with studies localizing secretory and membrane proteins in the pancreas (23), IgG in plasma cells (24), and VSV-G in Chinese hamster ovary cells (25,26). In all cases, each of the proteins were found in all cisternae of the Golgi stack.…”

Section: Discussionsupporting

confidence: 92%

Vesicular stomatitis virus glycoprotein, albumin, and transferrin are transported to the cell surface via the same Golgi vesicles.

Strous¹,

Willemsen²,

Kerkhof³

et al. 1983

The Journal of Cell Biology

110

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Human hepatoma cells, infected by vesicular stomatitis virus, offer a good system to study simultaneously the intracellular localization of a well defined transmembrane glycoprotein (VSV-G), a secretory glycoprotein (transferrin), and a nonglycosylated secretory protein (albumin) . We used monospecific antibodies in combination with 5-and 8-nm colloidal gold particles complexed with protein A to immunolabel these proteins simultaneously in thin frozen sections of hepatoma cells. VSV-G, transferrin, and albumin are present in the same rough endoplasmic reticulum cisternae, the same Golgi compartments, and the same secretory vesicles. In the presence of the ionophore monensin intracellular transport is blocked at the trans cisternae of the Golgi complex, and VSV-G, transferrin, and albumin accumulate in dilated cisternae, which are apparently derived from the trans-Golgi elements. Glycoproteins, synthesized and secreted in the presence of monensin, are less acidic than those in control cultures . This is probably caused by a less efficient contact between the soluble secretory proteins and the membrane-bound glycosyltransferases that are present in the most monensinaffected (trans) Golgi cisternae .Secretory proteins and plasma membrane glycoproteins in eucaryotic cells are synthesized in the rough endoplasmic reticulum (ER),' and are transported in a series of membrane vesicles to the cell surface (1, 2). A number of lines ofevidence suggests that both classes of proteins migrate through the Golgi complex, but it is not known whether exactly the same intracellular pathway is employed. In favorable cases, a combination of cell fractionation and immunoelectron microscopic techniques were used to show the transient accumulation of proteins such as vesicular stomatitis virus glycoprotein (VSV-G), histocompatibility proteins, and predominant secreted proteins in the Golgi cisternae (2-4). Additionally, the high-mannose oligosaccharides added to nascent secretory and plasma membrane glycoproteins undergo the same intracellular modifications ; many of the modifying enzymes have been localized either to the rough ER or to the Golgi complex (5,6).I Abbreviations used in this paper: Endo-H, endo-ß-N-acetylglucosaminidase H; ER, endoplasmic reticulum, PBS, phosphate-buffered saline; VSV-G vesicular stomatitis virus glycoprotein.

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Section: Discussionsupporting

confidence: 92%

Vesicular stomatitis virus glycoprotein, albumin, and transferrin are transported to the cell surface via the same Golgi vesicles.

Strous¹,

Willemsen²,

Kerkhof³

et al. 1983

The Journal of Cell Biology

110

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“…The cellular morphology of the pre-PC was more consistent with GC cells than mature PCs (Figure 1D), although they showed some expansion in their ER, consistent with early stages of plasma cell differentiation (Geuze and Slot, 1980). …”

Section: Resultsmentioning

confidence: 60%

Development and Migration of Plasma Cells in the Mouse Lymph Node

et al. 2010

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Summary In this study, we imaged the differentiation and migratory behavior of nascent plasma cells (PCs) in mouse lymph nodes by intravital microscopy.. Pre-PCs exhibited a unique migration pattern characterized by long, linear paths that were randomly oriented. Although chemotaxis via Gαi coupled-receptors has been implicated in PC migration, treatment with Pertussis toxin (Ptx), which ablates these signals, did not prevent movement of pre-PCs while it arrested other lymphocytes. In vitro, pre-PCs displayed processive amoeboid locomotion on surfaces coated with integrin ligand, while fully-differentiated PC moved slowly or were arrested. Both PC arrest and differentiation occurred in the medullary cords. Ptx treatment before PC differentiation blocked their accumulation in the medullary cords but pre-PCs still differentiated in other lymph node regions. Taken together, we suggest pre-PCs undergo a persistent random walk to find the medullary cords, where localized chemokines help retain these cells until they undergo differentiation and arrest in situ.

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“…The secretory material is rapidly transported in small vesicles from the Golgi complex and gains the exterior by a fission-fusion process at the plasma membrane. These transport vesicles have half-life of only some 10 min and are not electron-dense (Geuze & Slot, 1980;Kelly, 1985). In AR4-2J cells, such transport vesicles are therefore likely to be responsible for basal amylase secretion via the constitutive pathway with freshly synthesised amylase largely confined to these small transport vesicles.…”

Section: Discussionmentioning

confidence: 99%

Photodynamic action of sulphonated aluminium phthalocyanine (SALPC) on AR4-2J cells, a carcinoma cell line of rat exocrine pancreas

Matthews

Cui²

1990

Br J Cancer

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Summary The photodynamic effects of sulphonated aluminium phthalocyanine (SALPC) have been compared on cultured AR4-2J cells of a pancreatic carcinoma cell line and on exocrine cells of the normal phenotype freshly isolated from the rat pancreas; a multi-channel perifusion system was used for this kinetic study in vitro. Whereas light alone or SALPC alone was without effect on either cell type, photon activation of cellularly-bound SALPC with light > 570 nm permeabilised the cells and caused an increase in amylase secretion from normal acinar cells but a dose-dependent inhibition (10' to 10-0 M) of amylase release from AR4-2J cells. In contrast, direct permeabilisation of the plasma membrane with digitonin, jg ml-', evoked a marked release of amylase from both types of cell. Elevation of [Ca2"]i by the ionophore A23187, 10-6 M, elicited secretion of amylase from normal cells but had little effect on AR4-2J cells. Finally, it was established that the differential photodynamic effects of SALPC on amylase release were not attributable to any topographical differences in the microanatomical organisation of normal or tumour-derived cells; furthermore, the structural integrity of normal and AR4-2J cells was maintained after the photodynamic action of SALPC. It is concluded that the generation of singlet oxygen is responsible for permeabilisation of both types of cell and that photon-activated SALPC has functionally distinct effects on the constitutive secretion of amylase of tumour cells and the regulated secretory pathway of normal cells. These observations may be important in the development of drugs with a selective photodynamic action on pancreatic tumour cells.

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The subcellular localization of immunoglobulin in mouse plasma cells, as studied with immunoferritin cytochemistry on ultrathin frozen sections

Cited by 16 publications

References 30 publications

Vesicular stomatitis virus glycoprotein, albumin, and transferrin are transported to the cell surface via the same Golgi vesicles.

Vesicular stomatitis virus glycoprotein, albumin, and transferrin are transported to the cell surface via the same Golgi vesicles.

Development and Migration of Plasma Cells in the Mouse Lymph Node

Photodynamic action of sulphonated aluminium phthalocyanine (SALPC) on AR4-2J cells, a carcinoma cell line of rat exocrine pancreas

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