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At least 397 records · Page 22Linked to original sources
PubMed2002

Glyceraldehyde-3-phospate dehydrogenase is translocated into nuclei through Golgi apparatus during apoptosis induced by 6-hydroxydopamine in human dopaminergic SH-SY5Y cells.

6-Hydroxydopamine is a neurotoxin specific to dopamine neurons, and this neurotoxin at 20 muM was confirmed to induce mainly apoptosis in human dopaminergic neuroblastoma SH-SY5Y cells. During the apoptotic process, translocation of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) into nuclei was observed, which is now proposed as an apoptogenic signal in various types of apoptosis. However, it remains to be clarified, how GAPDH is translocated into nuclei. In this paper, GAPDH translocation was followed by fluoro- and electron-microscopic observation using antibody against GAPDH. Before the nuclear translocation, a condensed mass of GAPDH protein was detected in the Golgi apparatus, which was identified by 6-([N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino]hexanoyl)-sphingosine, a selective marker of Golgi apparatus. These results suggest that the Golgi apparatus may be involved in the compartmentalization of GAPDH from cytosol to nuclei.

Active Transport, Cell Nucleus↗
PubMed1990

Effects of CCl4 poisoning on metabolism of dolichol in rat liver microsomes and Golgi apparatus.

Carbon tetrachloride (CCl4) poisoning affects glycoprotein processing and maturation at the level of rat liver microsomes and Golgi apparatus. HPLC analysis showed that within 5-60 min after CCl4 administration the levels of total dolichol, free dolichol and dolichyl-phosphate strongly decreased both in total microsomes and in Golgi apparatus. The most marked and early reduction of total dolichol was observed in the secretory membranes of Golgi area already 15 min after CCl4 poisoning. The incubation of CCl4-pretreated isolated hepatocytes with [3H]-mevalonate showed a significant slowing down of the label incorporation into both free-dolichol and dolichyl-phosphate. Moreover, lipid peroxidation might cause alterations in the molecular structure of both free-dolichol and dolichyl-phosphate. A notable prevention of dolichol decrease was observed in animals pretreated with vitamin E. The results suggest that the prooxidant activity of CCl4 is able to affect the metabolism of dolichol either by increasing the oxidative degradation or impairing the biosynthetic pathway.

Animals↗
PubMed1970

Evidence for the participation of the Golgi apparatus in the intracellular transport of nascent albumin in the liver cell.

A comparative biochemical and radioautographic in vivo study was performed to identify the site of synthesis and route of migration of albumin in the parenchymal liver cell after labeling with leucine-(14)C or leucine-(3)H via the portal vein. Free cytoplasmic ribosomes, membrane-bound ribosomes, rough- and smooth-surfaced microsomes, and Golgi membranes were isolated. The purity of the Golgi fraction was examined morphologically and biochemically. After administration of leucine-(14)C, labeled albumin was extracted, and the sequence of transport was followed from one fraction to the other. Approximately 2 min after the intravenous injection, bound ribosomes displayed a maximal rate of leucine-(14)C incorporation into albumin. 4 min later, a peak was reached for rough microsomes. Corresponding maximal activities for smooth microsomes were recorded at 15 min, and for the Golgi apparatus at approximately 20 min. The relative amount of albumin, calculated on a membrane protein basis, was higher in the Golgi fraction than in the microsomes. By radioautography the silver grains were preferentially localized over the rough-surfaced endoplasmic reticulum at the 5 min interval. Apparent activity in the Golgi zone was noted 9 min after the injection; at 15 and 20 min, the majority of the grains were found in this location. Many of the grains associated with the Golgi apparatus were located over Golgi vacuoles containing 300-800 A electron-opaque bodies. It is concluded that albumin is synthesized on bound ribosomes, subsequently is transferred to the cavities of rough-surfaced endoplasmic reticulum, and then undergoes migration to the smooth-surfaced endoplasmic reticulum and the Golgi apparatus. In the latter organelle, albumin can be expected to be segregated together with very low density lipoprotein in vacuoles known to move toward the sinusoidal portion of the cell and release their content to the blood.

Animals↗
PubMed1981

Effect of colchicine on the Golgi apparatus and on GERL of rat jejunal absorptive cells. Ultrastructural localization of thiamine pyrophosphatase and acid phosphatase activity.

Ultrastructural localization of thiamine pyrophosphatase (TTP) and acid phosphatase (AcPase) activity was performed on jejunal absorptive cells of rats pretreated with the antimicrotubular agent colchicine and of control animals. Demonstration of TPP activity showed that most of the dislocated Golgi stacks after colchicine application lacked positively staining cisternae of the mature side. This cytochemical finding is in agreement with the morphologically demonstrable changes of the Golgi stacks resulting in a loss of polarity and give evidence for a colchicine-induced deficiency of the Golgi apparatus. The cytochemical localization of AcPase activity showed deposits of reaction product over lysosomes and GERL and demonstrated a dislocation of GERL occurring concomitantly with the changes of the Golgi apparatus. The antimicrotubular effect of colchicine is well documented; thus the morphological and cytochemical changes of the Golgi apparatus and of GERL might be due to a disturbed microtubular function after application of this agent suggesting an influence of microtubules in the maintenance of the integrity of these organelles. This hypothesis includes the possibility of an involvement of microtubules in formation and differentiation of Golgi stacks and GERL as well as a kind of "skeletal"function being responsible for their characteristic structure and fashion.

Acid Phosphatase↗
PubMed1998

Nucleotide sugars, nucleotide sulfate, and ATP transporters of the endoplasmic reticulum and Golgi apparatus.

The lumina of the endoplasmic reticulum and Golgi apparatus are the subcellular sites where glycosylation, sulfation, and phosphorylation of secretory and membrane-bound proteins, proteoglycans, and lipids occur. Nucleotide sugars, nucleotide sulfate, and ATP are substrates in the above reactions and must first be translocated from the cytosol into the lumen of these organelles. Translocation of these nucleotide derivatives is mediated by highly specific transporters, which are antiporters with the corresponding nucleoside monophosphate, as shown by genetic and biochemical approaches in mammals and yeast. Studies with mammalian, yeast, and protozoa mutants have shown that a defect in a specific translocator results in selective impairments of glycosylation of proteins, lipids and proteoglycans in vivo. Several of these transporters have been purified, cloned, and found to encode very hydrophobic proteins with multitransmembrane domains. Experiments with yeast and mammalian cells demonstrate that these transporters play a regulatory role in posttranslational modifications.

ATP-Binding Cassette Transporters↗
PubMed2003

Identification of a five-pass transmembrane protein family localizing in the Golgi apparatus and the ER.

A family of five-pass transmembrane proteins (FinGERs) were identified from the protein sequence database. The family includes yeast Yip1p, Yip4p, Yip5p, and Yif1p, and also their plant, insects, nematode, and mammalian homologues, suggesting their conserved function in a broad range of species. Eight family members were found in human. Multiple sequence alignment revealed three regions conserved among all family members. All of the human family members were expressed widely in various tissues. The human proteins were localized in and around the Golgi apparatus and may also be in the ER to some extent. The Golgi apparatus was fragmented by overexpression of the five of the family members. Some of the members were found to interact by yeast two-hybrid analysis, suggesting the formation of a complex. These results suggest that FinGERs function in maintenance of the Golgi structure and/or transport between the ER and the Golgi apparatus.

Amino Acid Sequence↗
PubMed2002

Inheritance of the endoplasmic reticulum and Golgi apparatus.

Yeast and mammalian cells use a variety of different mechanisms to ensure that the endoplasmic reticulum and Golgi apparatus are inherited by both daughter cells on cell division. In yeast, endoplasmic reticulum inheritance involves both active microtubule and passive actin-based mechanisms, while the Golgi is transported into the forming daughter cell by an active actin-based mechanism. Animal cells actively partition the endoplasmic reticulum and Golgi apparatus, but association with the mitotic spindle-rather than the actin cytoskeleton-appears to be the mechanism

Actins↗
PubMed1979

Different aspects of membrane differentiation at the inner side (GERL) of the Golgi apparatus in rabbit luteal cells.

After luteinization, during the growth phase, rabbit luteal cells showed a well-developed Golgi apparatus, which was clearly reduced at the end of pseudo-pregnancy. During this whole period, acid phosphatase was demonstrated in the saccules (g) of the Golgi stack and in the innermost Golgi element (G2), which may be part of GERL. Between both acid phosphatase-positive compartments, a negative or slightly positive element (G1) was present paralleling the saccules of the Golgi stack. This element was composed of cisternal (G1 c) and perforated portions (G1 p) and directly bordered the thiamine pyrophosphatase-positive saccules of the Golgi stack (g1 -g2). Arylsulphatase activity was present in two saccules in the middle of the stack (g3 -g4) and in the innermost Golgi element (G2). In the acid phosphatase and arylsulphatase reactions the limiting membrane of the lysosomes was more reactive than the matrix. After phosphotungstic acid staining at a low pH, the inner elements of the Golgi apparatus (G1 and G2) and the border of the lysosomes were heavily contrasted. The lysosomal matrix and the other Golgi stack saccules were either almost unstained or displayed a clearly lower contrast. It is concluded that the cytochemical difference between Golgi (g) and GERL (G) membranes is most probably the result of a specific process of membrane differentiation, which takes place at G1. There is also evidence that the lysosomal matrix hydrolases may be formed in the saccules of the Golgi stack. The strongly phosphotungstic acid-positive inner elements are, although more extended, comparable in large part with the GERL elements as described in neurons (Novikoff et al., 1971).

Acid Phosphatase↗
PubMed1996

Apolipoprotein-mediated cellular cholesterol and phospholipid efflux depend on a functional Golgi apparatus.

Several studies have demonstrated that lipid-free apolipoproteins can promote cholesterol and phospholipid efflux from cells; however, the mechanisms and the role of cell-mediated pathways involved remain incompletely elucidated. We have recently demonstrated that brefeldin A or monensin, agents that disrupt Golgi apparatus structure and function, inhibit intracellular cholesterol efflux from cells to high density lipoproteins. In the present study we examined the effects of those agents on cell cholesterol and phospholipid efflux to purified apolipoprotein A-I (apoA-I) and apolipoprotein-depleted acceptors from cholesterol-loaded fibroblasts. Brefeldin A or monensin treatment of cells during incubation with apoA-I inhibited efflux of cellular cholesterol by greater than 80% compared with control cells, measured by changes in cellular cholesterol radioactivity, mass, and the substrate pool of cholesterol available for esterification by acyl coenzyme A:cholesterol acyltransferase. Inhibition of cholesterol efflux by these agents could not be overcome by increasing the apoA-I concentration and persisted during incubations up to 24 h. Similarly, brefeldin A and monensin inhibited up to 80% of apoA-I-mediated efflux of labeled phospholipids from cholesterol-loaded cells relative to controls. In contrast, lipid efflux mediated by apolipoprotein-depleted acceptors (trypsin-modified HDL and sonicated phospholipid vesicles) was not sensitive to these drugs. On the basis the known effects of brefeldin A and monensin on Golgi apparatus structure and function, these results are consistent with the notion that efflux of cell lipids by apolipoprotein-dependent mechanisms, but not by apolipoprotein-independent mechanisms, require active cellular processes involving an intact and functional Golgi apparatus.

Apolipoproteins↗
PubMed1983

Polarization of the Golgi apparatus and the microtubule-organizing center within cloned natural killer cells bound to their targets.

In cell couples formed between a cloned murine natural killer (NK) cell and either of two target cells, we have obtained evidence by immunofluorescence observations for a rapid coordinate repositioning of two organelles, the microtubule organizing center and the perinuclear Golgi apparatus, inside the NK cell to face the region of contact with the target cell. With microtubule-disrupting drugs, which also cause a dispersion of the Golgi apparatus throughout the periphery of the NK cell, it was found that target cell lysis is reversibly inhibited. It is proposed that the coordinate repositioning of the two organelles serves the function of directing secretory vesicles derived from the Golgi apparatus to the bound target cells, the secretory vesicles containing components that induce target cell lysis.

Animals↗
PubMed1975

Anesthesia and the golgi apparatus: enzyme activity changes in a golgi-rich fraction of rat liver after a short ether anesthesia.

Activity changes of enzymes in isolated rat liver Golgi preparations at different times (1-48 h) after a short ether anesthesia are reported. Activity of galactosyl-transferase showed a slight gradual increase but thiamine pyrophosphatase decreased sharply, and after 24 h increased to above control level. Arylsulphatase-A remained largely unchanged, and B was significantly decreased. Acid phosphatase activity did remain at the control level, but alkali phosphatase showed a gradual and highly significant increase. Five other enzymes representing probable contaminations from other subcellular organelles, have also been assayed. Correlation is sought between the enzyme activity changes and some other metabolic effects of anesthesia.

Acid Phosphatase↗
PubMed1999

Membrane flow through the Golgi apparatus: specific disassembly of the cis-Golgi network by ATP depletion.

Incubation of NRK cells for 30 to 45 minutes with 50 mM 2-deoxy-D-glucose (DOG) in glucose and pyruvate-free medium results in depletion of the cellular ATP pool and in specific disassembly of the cis-Golgi network (CGN), with the stack of Golgi cisternae (SGC) and the trans-Golgi network (TGN) remaining intact and sensitive to BFA. The disassembly of the CGN is mediated by long tubular structures extending outwards from the Golgi complex and involves microtubules. Upon removal of DOG and addition of glucose and pyruvate to the culture medium, the morphology of the CGN is slowly reestablished. Reconstruction of the CGN involves COPI/COPII-positive vesicles that resume the transport of proteins and in particular of CGN membrane proteins out of the ER. Exit of CGN membrane proteins from the ER is insensitive to BFA. In cells pretreated with nocodazole, the CGN membrane proteins are transported to the vicinity of the SGC fragments dispersed throughout the cytoplasm. Ultrastructural studies of cells engaged in the reconstruction of the CGN revealed that the CGN cisterna emerge as tubular structures extending from 0.2-0.3 microm uncoated vesicles prior to their organization on the cis-side of the SGC.

Adenosine Triphosphate↗
PubMed1997

Retention of glycosyltransferases in the Golgi apparatus.

A number of Golgi glycosyltransferases has been cloned to date. They all are membrane proteins and share the same type II topology, but they do not possess an obvious sequence homology which would suggest a common Golgi retention signal. However, it was shown that the membrane-spanning domain and its flanking regions contain necessary and sufficient information for Golgi retention of these enzymes. Currently, two mutually complementary models have been proposed to explain the mechanism of Golgi retention of glycosyltransferases mediated by their transmembrane domain. The first model postulates the retention through oligomerization, which prevents enzymes from entering the transport vesicles. The second suggests that retention depends on the length of a membrane-spanning domain and thickness of the membrane along the Golgi complex. It has to be pointed out that neither the oligomerization nor the membrane thickness model alone can answer all questions and further work is still needed to elucidate the retention process of Golgi proteins.

Animals↗
PubMed1992

Lectin cytochemistry in the gastrointestinal tract with special reference to glycosylation in the Golgi apparatus of Brunner's gland cells.

Two hydrophilic, low temperature-embedding resins, Lowicryl K4M and LR White, were compared in lectin cytochemistry. Post-embedding staining of colloidal gold-labeled Griffonia symplicifolia agglutinin II (GSA-II) resulted in staining of the Golgi apparatus and mucous granules of mucous neck cells in the gastric fundic gland, pylorocytes, and Brunner's gland cells embedded in either resin, although it was much easier to make ultra-thin sections with LR White-embedded material than with the other. Post-fixation with uranyl acetate followed by LR White embedding improved general ultrastructure so that lectin binding sites were identified precisely. All examined lectins, soybean agglutinin (SBA), Maclura pomifera agglutinin (MPA), GSA-II, and Ulex europaeus agglutinin I (UEA-I), stained mucous granules and the Golgi apparatus, in which the staining pattern was characteristic of each lectin: cis cisternae were labeled with SBA and MPA, intermediate cisternae with GSA-II, and trans cisternae and mucous granules with SBA, GSA-II, UEA-I, and lightly with MPA. No labeling was observed in the rough endoplasmic reticulum with any lectin. These findings suggest that the Golgi apparatus is the site of O-linked glycosylation and can be divided into at least three distinct compartments with regard to the glycosylation.

Animals↗
PubMed1977

Cytoenzymology of benign and malignant tumours of the corpus uteri. II. Lysosomal enzymes in relation to Golgi apparatus.

Cytological and cytochemical studies were carried out on benign and malignant tumours of the human corpus uteri. It was found that the Golgi complex was present in the form of granules of crescent-like structure. The elements of Golgi apparatus have two modes of distribution, the perinuclear and scattered types. The activity of acid phosphatase only which was located in the lysosomes had the same topographical configuration as Golgi apparatus. The degree of development of Golgi elements and the activity of both acid phosphatase and aryl sulphatase increased in malignant tumours as compared with benign tumours and normal tissues.

Acid Phosphatase↗
PubMed1992

Changes of cytochemical properties in the Golgi apparatus during in vivo differentiation of the ameloblast in developing rat molar tooth germs.

The cytochemical changes of the Golgi stacks occurring concomitantly with cell differentiation were examined in ameloblasts of developing rat molar tooth germs using osmium impregnation and cytochemistry with nicotinamide adenine dinucleotide phosphatase (NADPase), thiamine pyrophosphatase (TPPase), and acid phosphatase (Acpase). NADPase, TPPase, and Acpase activities were already present in the Golgi stacks of the inner enamel epithelial cells, the undifferentiated form of the ameloblast: NADPase activity existed in the medial Golgi cisternae, TPPase activity in the trans Golgi cisternae, and Acpase activity in almost all cisternae and strongly in the trans-most cisterna of the Golgi stack. At this stage, however, osmium deposits after impregnation were not observed in the cisterna of Golgi stacks but were present in some small vesicles. These vesicles were located throughout the cytoplasm. Osmiophilic cisternae in the Golgi stacks were apparent for the first time at the stage when the Golgi apparatus developed and migrated to the region distal to the nucleus with the progression of cell differentiation. These findings indicate that the cis subcompartment of the Golgi apparatus was incomplete in the inner enamel epithelial cells with regard to appearance of its cytochemical property, as compared with the medial and trans subcompartments. It is suggested that the cis compartment of the Golgi stack may be completed only in the last stage of the compartmentalized Golgi organization during differentiation of the ameloblast.

Acid Phosphatase↗
PubMed1990

Three-dimensional observation of the Golgi apparatus in rat tracheal gland during the secretory cycle.

The purpose of the present work is three-dimensional clarification of the overall configuration of the Golgi apparatus in rat tracheal serous cells including the sequence of structural modification during the secretory cycle induced by pilocarpine. From the results of both transmission electron microscopy from the serial sections, and scanning electron microscopy using the osmium-DMSO-osmium method based on maceration in dilute osmium tetroxide, the overall configuration of the Golgi apparatus shows that the Golgi stacks are joined together to make an interconnected, single Golgi complex in a cell. Connections, not only between the TGN (trans Golgi network) and rough ER (endoplasmic reticulum), but also between rough ER and cis cisternae are observed. This finding offers alternative routes for movement of substances through the cellular endomembrane system. During the secretory cycle induced by pilocarpine injection, it is evidenced that the disappearance of the TGN is accompanied by rapid discharge of secretory granules and the reconstitution of the TGN is followed by reformation of secretory materials. The beginning of the reconstitution of the TGN is indicated by vesicular buds from the sacculotubular element. These results indicate that the TGN participates directly in membrane recycling and in formation of secretory granules.

Animals↗
PubMed1991

Differential distribution of salivary agglutinin and amylase in the Golgi apparatus and secretory granules of human salivary gland acinar cells.

The secretory granules of salivary glands often display complex internal substructures, yet little is known of the molecular organization of their contents or the mechanisms involved in packaging of the secretory proteins. We used post-embedding immunogold labeling with antibodies to two secretory proteins, agglutinin and alpha-amylase, to determine their distribution in the Golgi apparatus and secretory granules of the human submandibular gland acinar cells. With monoclonal antibodies specific for carbohydrate epitopes of the agglutinin, reactivity was found in the trans Golgi saccules, trans Golgi network, and immature and mature secretory granules. In the granules, labeling was seen in regions of low and medium electron density, but not in the dense cores. Reactivity seen on the apical and basolateral membranes of acinar and duct cells was attributed to a shared epitope on a membrane glycoprotein. Labeling with a polyclonal antibody to amylase was found in the Golgi saccules, immature and mature secretory granules, but not in the trans Golgi network. In the granules, amylase was present in the dense cores and in areas of medium density, but not in the regions of low density. These results indicate that these two proteins are distributed differently within the secretory granules, and suggest that they follow separate pathways between the Golgi apparatus and forming secretory granules. Small vesicles and tubular structures that labeled only with the antibodies to the agglutinin were observed on both faces of the Golgi apparatus and in the vicinity of the cell membrane. These structures may represent constitutive secretion vesicles involved in transport of the putative membrane glycoprotein to the cell membrane.

Agglutinins↗