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Identification of a novel protein (G210) specific to the Golgi apparatus.

A monoclonal antibody, 3C9, has enabled the detection of a novel Golgi-specific protein in bovine tissues. Immunohistochemical studies at the light microscopic level have detected the 3C9 antigen only in certain cells: exocrine pancreas, gut epithelium, and thymus epithelium. Examination of gut and pancreas by immunoelectron microscopy showed a localization exclusive to the Golgi apparatus. The relative molecular weight of the antigen detected by immunoblotting is 210,000 daltons. The antigen is not extracted from microsomal membranes of bovine gut epithelium by sodium carbonate solutions. Furthermore, the 3C9 antigen enters into the detergent phase when Triton X-114 partitioning methods are used. These data strongly suggest that this novel antigen is an intrinsic membrane protein, resident in the Golgi apparatus of certain cells. Moreover, they enhance the hypothesis that the distribution of enzymes and polypeptides in the Golgi apparatus is cell specific.

Animals↗

Inhibition of phosphatidic acid synthesis alters the structure of the Golgi apparatus and inhibits secretion in endocrine cells.

In mammalian cells, activation of a Golgi-associated phospholipase D by ADP-ribosylation factor results in the hydrolysis of phosphatidylcholine to form phosphatidic acid (PA). This reaction stimulates the release of nascent secretory vesicles from the trans-Golgi network of endocrine cells. To understand the role of PA in mediating secretion, we have exploited the transphosphatidylation activity of phospholipase D. Rat anterior pituitary GH3 cells, which secrete growth hormone and prolactin, were treated with 1-butanol resulting in the synthesis of phosphatidylbutanol rather than PA. Under these conditions transport from the ER through the Golgi apparatus and secretion of polypeptide hormones were inhibited quantitatively. Furthermore, the in vitro synthesis of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P(2)) by Golgi membranes was inhibited quantitatively. Most significantly, in the presence of 1-butanol the architecture of the Golgi apparatus was disrupted, resulting in its disassembly and fragmentation. Removal of the alcohol resulted in the rapid restoration of Golgi structure and secretion of growth hormone and prolactin. Our results suggest that PA stimulation of PtdIns(4,5)P(2) synthesis is required for maintaining the structural integrity and function of the Golgi apparatus.

1-Butanol↗

Subfractionation of rat liver Golgi apparatus by free-flow electrophoresis.

Using the technique of preparative free-flow electrophoresis, cisternae of unstacked rat liver Golgi apparatus were separated into a series of fractions of increasing content of sialic acid, thiamine pyrophosphatase and 5'-nucleotidase, markers regarded as being concentrated toward the mature Golgi apparatus face. These same fractions showed a decreasing content of nucleoside diphosphatase, an endoplasmic reticulum marker. Fractions enriched in sialic acid also were enriched in cisternae from the mature or trans face of the Golgi apparatus as deduced from cytochemical criteria. Those fractions least enriched in sialic acid contained cisternae that accumulated deposits of reduced osmium under standard conditions, a test used to mark the opposite, forming or cis-face. Thus subfractionation along the functional polarity axis of the Golgi apparatus with separation of cis and trans face cisternae has been achieved.

Animals↗

Retrograde transport of cholera toxin from the plasma membrane to the endoplasmic reticulum requires the trans-Golgi network but not the Golgi apparatus in Exo2-treated cells.

Cholera toxin (CT) follows a glycolipid-dependent entry pathway from the plasma membrane through the trans-Golgi network (TGN) to the endoplasmic reticulum (ER) where it is retro-translocated into the cytosol to induce toxicity. Whether access to the Golgi apparatus is necessary for transport to the ER is not known. Exo2 is a small chemical that rapidly blocks anterograde traffic from the ER to the Golgi and selectively disrupts the Golgi apparatus but not the TGN. Here we use Exo2 to determine the role of the Golgi apparatus in CT trafficking. We find that under the condition of complete Golgi ablation by Exo2, CT reaches the TGN and moves efficiently into the ER without loss in toxicity. We propose that even in the absence of Exo2 the glycolipid pathway that carries the toxin from plasma membrane into the ER bypasses the Golgi apparatus entirely.

Animals↗

Golgi apparatus is involved in intracellular Ca2+ regulation in epithelial LLC-PK1 cells.

Several lines of evidence suggest that the Golgi apparatus is involved in Ca2+ regulation in renal epithelial LLC-PK1 cells. Laser scanning confocal microscopy (LSCM) was employed to establish that a prominent perinuclear region is occupied mainly by the Golgi apparatus in this cell line. LSCM measurements in individual cells with the ionized Ca2+ indicator calcium green revealed that stimulation of LLC-PK1 cells with arginine vasopressin (AVP) resulted in the elevation of ionized Ca2+ levels. However, the vasopressin-induced rise in ionized Ca2+ was attenuated if the Golgi apparatus was disassembled by pretreating the cells with brefeldin A (BFA). Subcellular measurements of total Ca2+ with ion microscopy in cryogenically prepared cells indicated that 1) within 1 min of AVP treatment significant quantities of sequestered Ca2+ were released from the perinuclear Golgi region and 2) the BFA treatment reduced the total Ca2+ stored in the Golgi region. These observations indicate that the Golgi apparatus is sensitive to hormonal stimulation and may play important roles in intracellular Ca2+ regulation in LLC-PK1 cells.

Animals↗

Traffic through the Golgi apparatus as studied by radioautography.

The ability to radiolabel biological molecules, in conjunction with radioautographic or cell fractionation techniques, has brought about a revolution in our knowledge of dynamic cellular processes. This has been particularly true since the 1940's, when isotopes such as 35S and 14C became available, since these isotopes could be incorporated into a great variety of biologically important compounds. The first dynamic evidence for Golgi apparatus involvement in biosynthesis came from light microscope radioautographic studies by Jennings and Florey in the 1950's, in which label was localized to the supranuclear Golgi region of goblet cells soon after injection of 35S-sulfate. When the low energy isotope tritium became available, and when radioautography could be extended to the electron microscope level, a great improvement in spatial resolution was achieved. Studies using 3H-amino acids revealed that proteins were synthesized in the rough endoplasmic reticulum, migrated to the Golgi apparatus, and thence to secretion granules, lysosomes, or the plasma membrane. The work of Neutra and Leblond in the 1960's using 3H-glucose provided dramatic evidence that the Golgi apparatus was involved in glycosylation. Work with 3H-mannose (a core sugar in N-linked side chains), showed that this sugar was incorporated into glycoproteins in the rough endoplasmic reticulum, providing the first radioautographic evidence that glycosylation of proteins did not occur solely in the Golgi apparatus. Studies with the tritiated precursors of fucose, galactose, and sialic acid, on the other hand, showed that these terminal sugars are mainly added in the Golgi apparatus. With its limited spatial resolution, radioautography cannot discriminate between label in adjacent Golgi saccules. Nonetheless, in some cell types, radioautographic evidence (along with cytochemical and cell fractionation data) has indicated that the Golgi is subcompartmentalized in terms of glycosylation, with galactose and sialic acid being added to glycoproteins only within the trans-Golgi compartment. In the last ten years, radioautographic tracing of radioiodinated plasma membrane molecules has indicated a substantial recycling of such molecules to the Golgi apparatus.

Animals↗

Altered Golgi apparatus in hydrostatically loaded articular cartilage chondrocytes.

OBJECTIVES: Articular cartilage proteoglycan content is controlled by joint loading. This study aimed to elucidate the role of hydrostatic pressure in this regulation. METHODS: Primary cultures of chondrocytes from bovine articular cartilage, grown on coverslips, were subjected to 5, 15, or 30 MPa hydrostatic pressure, applied continuously or cyclically at 0.125 or 0.05 Hz. The Golgi apparatus was visualised either by a fluorochrome coupled wheat germ agglutinin or by transmission electron microscopy. Proteoglycan synthesis was studied by the incorporation of sulphur-35 labelled sulphate. RESULTS: After 30 MPa continuous hydrostatic pressure, the Golgi apparatus was observed in a compact form with a concomitant decrease in proteoglycan synthesis. The normal stacked appearance of the Golgi apparatus was no more visible in the electron microscopy preparation of the pressurised chondrocytes. This effect was reversible and was also noticed after 15 MPa continuous load, though to a minor extent. Cyclic pressures (5-30 MPa) caused no apparent change in the Golgi apparatus. The shape of some cells changed to a more retracted form after 30 MPa continuous pressure. Nocodazole, which causes disassembly of the microtubules, blocked the compacting influence of pressurisation on the Golgi apparatus, and reduced proteoglycan synthesis to about half of the control level. CONCLUSIONS: The packing of the Golgi apparatus is dependent on microtubules and may contribute to the inhibition of proteoglycan synthesis observed in articular cartilage subjected to high hydrostatic pressure.

Animals↗

Localization of thiamine pyrophosphatase activity in the golgi apparatus of a mollusc, Helix aspersa.

Spermatids of the snail Helix aspersa were studied after fixation in buffered osmium tetroxide and after applying Novikoff and Goldfischer's method (15) for demonstrating thiamine pyrophosphatase (TPPase) activity both with the light and the electron microscope. The appearance of cells in the light microscope after localizing the enzyme is very similar to the appearance after the application of classical Golgi techniques. The electron microscope shows the "dictyosomes" to consist of non-granular membranes, vesicles, and vacuoles typical of the ultrastructure of the Golgi apparatus. Sites of TPPase activity are localized by deposits of lead phosphate, and are found between the membranes of the Golgi apparatus, in the small vesicles, in multivesicular bodies often found associated with it, but not within the large Golgi vacuoles. Heavy deposits are found on the caudal part of the nuclear envelope, but not in the acrosomal granule. It is suggested that TPPase may act as an intermediary in acrosome formation by the Golgi apparatus or "acroblast" of this cell. The finding of diphosphatase activity in the Golgi apparatus of an invertebrate is suggested as additional evidence for the existence of a homology between the Golgi apparatus of all animal cells.

Animals↗

Morphological and cytochemical alterations of the Golgi apparatus and GERL in rat parotid acinar cells during ethionine intoxication and recovery.

The present electron microscopic cytochemical investigation was undertaken to characterize the alterations in the golgi apparatus and GERL of rat parotid acinar cells during ethionine intoxication and recovery. Although the Golgi apparatus and GERL were reduced in size, and some broadening of the Golgi saccules occurred as the result of ethionine treatment, the relative localization of thiamine pyrophosphatase (TPPase) activity in the Golgi saccules, and acid phosphatase activity (AcPase) in GERL, remained unchanged. Shortly after ethionine treatment was stopped, a dramatic redistribution of enzyme activities was noted. Within the first 24 hours of recovery, the Golgi apparatus began to enlarge, and the content of secretory granules increased. By day 3 of recovery, cisternae morphologically identifiable as GERL and forming secretory granules possessed TPPase activity, while AcPase activity was virtually undetectable. After seven days of recovery, the Golgi apparatus and GERL appeared both morphologically and cytochemically normal. The enzyme modulation observed during recovery may be correlated with increased secretory granule production. Furthermore, the presence of TPPase activity in GERL and forming secretory granules lends support to the suggestion that GERL may be derived from the trans Golgi saccule.

Acid Phosphatase↗

The Golgi apparatus in neurons and epithelial cells of the common limpet Patella vulgata.

1. In view of widely diverse views held about the identity and structure of the Golgi apparatus in neurons of Mollusca, particularly gastropods, a study has been made on neurons of the common limpet, Patella vulgata, both by light and electron microscopy. A report is given also of observations made on epithelial cells of Patella by electron microscopy. 2. As revealed by Kolatchev's method, the Golgi apparatus in neurons consists basically of black filaments lying to one side of the nucleus. The filaments generally anastomose to form networks of various complexity. Rarely some cells contain only discrete filaments. Associated with some of the filaments is a weakly osmiophilic substance identified as archoplasm. Kolatchev's method also revealed spheroidal bodies (neutral red bodies, "lipochondria," etc.). 3. It has not been possible to demonstrate the Golgi apparatus using either iron-haematoxylin or Sudan black. 4. Examination of Kolatchev's preparations by electron microscopy has revealed that some of the Golgi filaments consist of chromophilic and chromophobic components. The chromophilic component consists of dense lamellae. 5. After fixation in buffered osmium tetroxide solution and examination by electron microscopy, it has been concluded that (a) the chromophilic component of the Golgi apparatus corresponds to a system of paired membranes (which usually enclose an inner dense substance), (b) the chromophobic component corresponds to a substance lying within small dilations of the paired membrane, and (c) the archoplasm corresponds to numerous small vesicles. 6. The paired membranes branch, anastomose, and can often be traced back to a common source. They are interpreted as lamelliform folds, and occasionally tubular processes, of essentially a single Golgi membrane. In cells containing a Golgi network it is suggested that the membrane extends through the whole of the apparatus in such a way that the substance it encloses may be regarded as being in a continuous phase. 7. Epithelial cells of Patella contain a juxtanuclear Golgi apparatus with an ultrastructure similar to that described for neurons.

Cell Count↗

SNAP prevents Mg(2+)-ATP-induced release of N-ethylmaleimide-sensitive factor from the Golgi apparatus in digitonin-permeabilized PC12 cells.

The N-ethylmaleimide-sensitive factor (NSF), which is involved in the multisteps of protein transport, is released from Golgi membranes on in vitro incubation with Mg(2+)-ATP. However, several lines of evidence suggest that NSF is associated with membranes in spite of the presence of Mg2+ and ATP in vivo. We have used digitonin-permeabilized PC12 cells to investigate the mechanism underlying the association of NSF with membranes. In PC12 cells, immunoreactivity for NSF was observed in the nuclear membranes, the Golgi apparatus, and neuronal growth cones, where synaptic vesicles are concentrated. NSF associated with the Golgi apparatus was released on incubation with Mg(2+)-ATP, whereas NSF in the nuclear membranes and neuronal growth cones was not released on the same treatment. The addition of cytosol blocked the Mg(2+)-ATP-induced release of NSF from the Golgi apparatus. Chromatographic analyses revealed that the factor(s) that prevents NSF release from the Golgi apparatus was eluted at the same position as the soluble NSF attachment proteins (SNAPs). Purified His6-tagged alpha-SNAP exhibited such activity. His6-tagged alpha-SNAP also prevented the Mg(2+)-ATP-induced release of NSF from isolated Golgi membranes.

Adenosine Triphosphate↗

Three-dimensional visualization of the Golgi apparatus: observation of Brunner's gland cells by a confocal laser scanning microscope.

The three-dimensional structure of the Golgi apparatus in cells of the Brunner's gland in the mouse was observed by using a confocal laser scanning microscope. Two lectins, FITC-labeled soybean agglutinin and Texas red-labeled Griffonia simplicifolia agglutinin II, were used to visualize the whole Golgi apparatus. Staining with the former lectin, which has been known to label the cis-stacks, showed a lacy dome-like structure situated in the supranuclear region. Staining with the latter lectin, known to label the intermediate-to-trans-stacks and the secretory granules, showed a dome-like structure consisting of network and cobblestone-like patterns in the same region and also granular stainings near the surface of the cobblestone-like patterns and the apical region of a cell. Double-staining demonstrated that the soybean agglutinin-labeled network always surrounded the G. simplicifolia agglutinin II-stained structure. Based on these observations, we propose a new three-dimensional model of the Golgi apparatus: it forms a dome-like structure over a nucleus, a network of cis-stacks forms its outer boundary, and this outer boundary is lined and paved with successive intermediate and trans-stacks. It is thought that secretory granules are released toward the internal space of the Golgi apparatus and transported to the apical cytoplasm through the holes of the network.

Agglutinins↗

A golgi apparatus associated with mating in Tetrahymena pyriformis.

The classical Golgi apparatus has not been observed in the several strains of Tetrahymena pyriformis examined in this laboratory at the ultrastructural level when the ciliates are grown vegetatively. However, sexually active strains, when starved for the purpose of inducing conjugation, contain stacked saccules in the oral region. When such opposite mating types are mixed for mating, the stacked saccules become swollen at their ends and vesicles appear to pinch off from them. These bodies possess the configuration of the classical Golgi apparatus of other eucells. Vesicles seem to be formed from the saccules just prior to, and toward the end of conjugation, suggesting a relationship with the mating process.

Animals↗

Mechanism of glycosylation in the Golgi apparatus.

A major role of the Golgi apparatus in liver is the terminal glycosylation of secreted serum proteins and of plasma membrane glycoproteins. Galactosyltransferase is a membrane-bound Golgi enzyme that transfers galactose directly from uridine diphosphogalactose (UDP-Gal) to terminal N-acetylglucosamine groups of N-asparagine-linked glycoproteins during secretion. Sialytransferase then transfers sialic acid from cytidine monophosphosialic acid (CMP-NAN) to the newly added terminal galactose of the glycoprotein. In the cell, the transfer reaction must occur on the lumen side of the Golgi membrane. UDP-Gal is synthesized mainly in the cytoplasm and CMP-NAN is synthesized in the nucleus in liver. An important question for understanding the mechanism is, how do these nucleotide sugars gain access to the transferases? A second question involves uridine diphosphate (UDP), a highly inhibitory product of galactosyltransferase. How is UDP removed from the lumen of the Golgi fast enough to prevent product inhibition of the galactosyltransferase? We have shown that isolated Golgi, although vesiculated, retains its original orientation. The vesicles are oriented with greater than 90% of both galactosyltransferase and sialyl-transferase on the luminal side of the vesicles. Using intact vesicles, we can show that UDP-Gal is taken up via a saturable carrier system present in the Golgi membrane. During galactosylation in vitro, UDP formed in the lumen of Golgi vesicles is rapidly converted to UMP by a nucleoside diphosphatase in the lumen. Uridine monophosphate, which is much less inhibitory to the galactosyltransferase than UDP, is then transported out of the lumen by a second carrier and is broken down further to uridine by 5'-nucleotidase on the cytoplasmic side of the Golgi vesicles. The transport of nucleotides appears unique to the Golgi membranes, since neither rough endoplasmic reticulum nor plasma membrane vesicles from rat liver accumulate these nucleotides.

Animals↗

Modifications of the Golgi apparatus in Saccharomyces cerevisiae lacking microtubules.

BACKGROUND: Disassembly of cytoplasmic microtubules by nocodazole in cultured mammalian cells leads to the disruption of the continuous ribbonlike Golgi apparatus and dispersal of the Golgi elements from their normal juxtanuclear location, close to the microtubule-organizing center (MTOC), toward the cell periphery. Clearing of the drug induces reassembly of the microtubules from the MTOC and reorganization of the Golgi elements into a continuous ribbonlike juxtanuclear structure. In the yeast Saccharomyces cerevisiae, the Golgi apparatus does not form a continuous structure as in mammalian cells but instead constitutes independent units dispersed throughout the cytoplasm. It is the purpose of this article to investigate the role of microtubules in the structure and distribution of the Golgi elements in S. cerevisiae by studying the ultrastructure of cell organelles either in mutant cells deficient in beta-tubulin or in wild-type cells treated with the microtubule-depolymerizing drug nocodazole. METHODS: Two S. cerevisiae yeast strains were used in this study: a control wild-type strain, CUY226 (ade2-101, his3-delta 200, leu2-delta 1, lys2-801, ura3-52 Mat alpha), and a mutant strain, CUY66 (tub2-401, ade2-101, ura3-52, Mat alpha). Nocodazole was added to the wild-type cells cultivated at 30 degrees C, and cells were fixed 5 min, 20 min, and 60 min, respectively, after adding the drug to the culture. Both strains were fixed and examined 5 min, 20 min, and 60 min after shifting the cultures from the permissive temperature of 30 degrees C to the restrictive temperature of 14 degrees C. Cells were fixed in 2% glutaraldehyde, treated for 15 min in 1% sodium metaperiodate, postfixed in reduced osmium, and embedded in Epon. To visualize the three-dimensional configuration of cell organelles, stereopairs were prepared from sections stained with lead citrate and tilted at +/- 15 degrees from the 0 degree position of the goniometric stage of the electron microscope. RESULTS: In mutant cells shifted to restrictive temperature and wild-type cells treated with nocodazole, the main ultrastructural modification was a fragmentation of networks of membranous tubules, which probably correspond to the yeast Golgi apparatus. Secretion granules were still present in growing buds, and they were dispersed in the cytoplasm, which contained in addition numerous small vesicles in the 30-60-nm diameter range. CONCLUSIONS: In normal cells, small vesicles may originate from the endoplasmic reticulum and fuse together to give rise to Golgi networks (Rambourg et al. 1994. Anat. Rec., 240:32-41). If this hypothesis is correct, the observations reported might indicate that intact microtubules orient the flow of small vesicles and favour their fusion into Golgi networks.

Golgi Apparatus↗

Traffic through the Golgi apparatus.

The role of vesicles in cargo transport through the Golgi apparatus has been controversial. Large forms of cargo such as protein aggregates are thought to progress through the Golgi stack by a process of cisternal maturation, balanced by a return flow of Golgi resident proteins in COPI-coated vesicles. However, whether this is the primary role of vesicles, or whether they also serve to transport small cargo molecules in a forward direction has been debated. Two papers (Martínez-Menárguez et al., 2001; Mironov et al., 2001, this issue) use sophisticated light and electron microscopy to provide evidence that the vesicular stomatitis virus membrane glycoprotein (VSV G)* is largely excluded from vesicles in vivo, and does not move between cisternae, whereas resident Golgi enzymes freely enter vesicles as predicted by the cisternal maturation model. Both papers conclude that vesicles are likely to play only a minor role in the anterograde transport of cargo through the Golgi apparatus in mammalian tissue culture cells.

COP-Coated Vesicles↗

Chlamydia trachomatis interrupts an exocytic pathway to acquire endogenously synthesized sphingomyelin in transit from the Golgi apparatus to the plasma membrane.

Chlamydia trachomatis acquires C6-NBD-sphingomyelin endogenously synthesized from C6-NBD-ceramide and transported to the vesicle (inclusion) in which they multiply. Here we explore the mechanisms of this unusual trafficking and further characterize the association of the chlamydial inclusion with the Golgi apparatus. Endocytosed chlamydiae are trafficked to the Golgi region and begin to acquire sphingolipids from the host within a few hours following infection. The transport of NBD-sphingolipid to the inclusion is energy- and temperature-dependent with the characteristics of an active, vesicle-mediated process. Photo-oxidation of C5-DMB-ceramide, in the presence of diaminobenzidine, identified DMB-lipids in vesicles in the process of fusing to the chlamydial inclusion membrane. C6-NBD-sphingomyelin incorporated into the plasma membrane is not trafficked to the inclusion to a significant degree, suggesting the pathway for sphingomyelin trafficking is direct from the Golgi apparatus to the chlamydial inclusion. Lectins and antibody probes for Golgi-specific glycoproteins demonstrate the close association of the chlamydial inclusion with the Golgi apparatus but do not detect these markers in the inclusion membrane. Collectively, the data are consistent with a model in which C.trachomatis inhabits a unique vesicle which interrupts an exocytic pathway to intercept host sphingolipids in transit from the Golgi apparatus to the plasma membrane.

4-Chloro-7-nitrobenzofurazan↗

Sphingomyelin synthesis in rat liver occurs predominantly at the cis and medial cisternae of the Golgi apparatus.

The intracellular site of sphingomyelin (SM) synthesis was examined in subcellular fractions from rat liver using a radioactive ceramide analog N-([1-14C]hexanoyl)-D-erythro-sphingosine. This lipid readily transferred from a complex with bovine serum albumin to liver fractions without disrupting the membranes, and was metabolized to radioactive SM. To prevent degradation of the newly synthesized SM to ceramide, all experiments were performed in the presence of EDTA to minimize neutral sphingomyelinase activity and at neutral pH to minimize acid sphingomyelinase activity. An intact Golgi apparatus fraction gave an 85-98-fold enrichment of SM synthesis and a 58-83-fold enrichment of galactosyltransferase activity. Controlled trypsin digestion demonstrated that SM synthesis was localized to the lumen of intact Golgi apparatus vesicles. Although small amounts of SM synthesis were detected in plasma membrane and rough microsome fractions, after accounting for contamination by Golgi apparatus membranes, their combined activity contributed less than 13% of the total SM synthesis in rat liver. Subfractions of the Golgi apparatus were obtained and characterized by immunoblotting and biochemical assays using cis/medial (mannosidase II) and trans (sialyltransferase and galactosyltransferase) Golgi apparatus markers. The specific activity of SM synthesis was highest in enriched cis and medial fractions but far lower in a trans fraction. We conclude that SM synthesis in rat liver occurs predominantly in the cis and medial cisternae of the Golgi apparatus and not at the plasma membrane or endoplasmic reticulum as has been previously suggested.

Animals↗