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PubMed1995

MG-160, a membrane sialoglycoprotein of the medial cisternae of the rat Golgi apparatus, binds basic fibroblast growth factor and exhibits a high level of sequence identity to a chicken fibroblast growth factor receptor.

We report the primary structure of MG-160, a 160 kDa membrane sialoglycoprotein residing in the medial cisternae of the Golgi apparatus of rat neurons, pheochromocytoma (PC-12), and several other cells. The cDNA encodes a polypeptide of 1,171 amino acids with an M(r) of 133,403. An intralumenal cleavable signal peptide is followed by a Pro-Gln-rich segment and 16 contiguous, approx. 60-residue-long, regularly spaced cysteine-rich segments showing sequence identities ranging from 15 to 35%. The lumenal domain is followed by a single membrane spanning domain and a short carboxy-terminal cytoplasmic tail. The protein contains 5 potential NXT glycosylation sites. The sequence of MG-160 shows no homologies with enzymes and other membrane proteins of the Golgi apparatus. MG-160 displays a so far unique feature for a membrane protein of the Golgi apparatus: namely, an upstream, open reading frame (uORF), encoding 58 amino acids, located in front of the major open reading frame (ORF). Most vertebrate mRNAs containing uORF or AUG codons in front of the major ORF encode growth factors and cell surface receptors (Geballe and Morris 1994). In that regard a 90% identity between the primary structure of MG-160 and a receptor for acidic and basic fibroblast growth factors (CFR), isolated from chicken embryos (Burrus et. al., 1992), may be relevant. Immunoreactivity for MG-160 has been detected in the Golgi apparatus of neural and other cells of 2-day-old chicken embryos and adult chicken; furthermore, recombinant human basic fibroblast growth factor (bFGF) binds MG-160 purified from rat brain. MG-160 shows no sequence similarity with members of the family of fibroblast growth factor receptors (FGFR) involved in signal transduction. These findings are consistent with the hypothesis that MG-160 is involved in the traffic and processing of endogenous or autocrine FGFs. This is the first example of an intrinsic membrane protein of the Golgi apparatus which binds a growth factor and may be involved in its regulation.

Amino Acid Sequence↗
PubMed1985

Transport to cell surface of intestinal sucrase-isomaltase is blocked in the Golgi apparatus in a patient with congenital sucrase-isomaltase deficiency.

A case of congenital sucrase-isomaltase deficiency in man was investigated. An intestinal biopsy sample from a 5-year-old girl lacked sucrase but possessed low residual isomaltase activity. Immunoelectron microscopy with monoclonal antibodies to sucrase-isomaltase in biopsy samples from healthy subjects revealed that sucrase-isomaltase was confined predominantly to the microvillus membrane of enterocytes and there was minimal labeling of the Golgi apparatus. In the patient immunoreactive sucrase-isomaltase was found almost exclusively in about three trans-Golgi cisternae and associated vesicular structures, while no specific labeling was associated with the microvillus membrane. Immunoprecipitation experiments with iodinated mucosal homogenates and a mixture of four monoclonal antibodies to sucrase-isomaltase revealed absence of enzyme subunits in the patients but presence of a Mr 210,000 protein that was also expressed in normal control biopsy specimens. This protein presumably is the high-mannose precursor of sucrase-isomaltase. Additional proteins of Mr 160,000-200,000 found in the patient but not in normal subjects might correspond to the crossreacting material found in the Golgi apparatus of the patient. Overall, the findings suggest that in the patient sucrase-isomaltase is synthesized and transported to the Golgi apparatus, where further transport is interrupted. The data imply that signals in sucrase-isomaltase that mediate its transfer from the endoplasmic reticulum to the Golgi apparatus differ from those mediating its transport from the Golgi apparatus to the cell surface.

Antibodies, Monoclonal↗
PubMed1988

An anti-organelle antibody in pathology. The chromatolytic reaction studied with a monoclonal antibody against the Golgi apparatus.

To evaluate the use of an anti-organelle antibody in a pathologic reaction the chromatolytic reaction was chosen for study. Qualitative analysis was made of rat hypoglossal nuclei stained with a cresyl violet method for Nissl substance and a monoclonal antibody against rat Golgi apparatus (10A8) 0 and 3 days, and 1, 2, 3, 4, 5, and 6 weeks after section of the right hypoglossal nerve. Marked dispersion of Nissl substance was noted at 2 weeks and of Golgi apparatus at 4 weeks. Reaggregation of staining had occurred for both organelles by 6 weeks. A quantitative light microscopic analysis was carried out for both stains on randomly selected hypoglossal sections from 0, 2, 4, and 6 weeks. The analysis confirmed the qualitative observations and showed them to be highly significant. In addition, it revealed an increase in nuclear area from 0 to 2 weeks, an increase in cytoplasmic area at 4 weeks, decrease in the total area of Nissl substance from 0 to 2 and 4 to 6 weeks, decrease in the percent cytoplasmic areas occupied by Nissl from 0 to 2 weeks and decreases in both the total and percent cytoplasmic area occupied by Golgi apparatus maximal at 4 weeks. Both qualitative and quantitative analyses confirmed the use of this monoclonal antibody to study morphologic changes of the Golgi apparatus secondary to an experimental pathologic lesion. In addition, a previously unrecognized temporal dissociation between the changes of Nissl substance and Golgi apparatus was described.

Animals↗
PubMed1992

Interphotoreceptor retinoid-binding protein in the Golgi apparatus of monkey foveal cones. Electron microscopic immunocytochemical localization.

The presence of interphotoreceptor retinoid-binding protein (IRBP) in the Golgi apparatus of monkey cone photoreceptors was examined by electron microscopic immunocytochemistry. Intracellular labeling for IRBP was light to moderate over the Golgi complex of foveal and peripheral cones in the retinas of all four monkeys examined. Composite drawings of two to seven serial sections of inner segments indicated that the highest density of intracellular labeling occurred over the Golgi apparatus. The labeling density over the Golgi complex was 8.5-29-fold higher than that over a comparable area of inner segment cytoplasm. The presence of immunolabel for IRBP in the Golgi apparatus supported the findings of in situ hybridization studies that cone photoreceptors can synthesize IRBP.

Animals↗
PubMed2005

Dynamic transport of SNARE proteins in the Golgi apparatus.

Localization of a membrane protein in a subcellular compartment can be achieved by its retention in the compartment or by its continuous transport toward this compartment. Previous results have suggested that specific enzymes are localized in the Golgi apparatus at least in part by selective retention and exclusion from transport vesicles. However, the function of some Golgi SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins is not compatible with their exclusion from transport vesicles. To help understand the mechanism accounting for the localization of SNARE proteins in the Golgi apparatus, we analyzed their lateral distribution in the Golgi cisternae and their incorporation into transport vesicles. According to our results, all SNARE proteins are efficiently incorporated into transport vesicles, indicating that the localization of SNARE proteins in the Golgi apparatus is not based on a static retention mechanism. Detailed analysis suggested that incorporation into transport vesicles was more efficient for SNARE proteins restricted to the cis face of the Golgi as compared with SNAREs present at the trans face. Furthermore, overexpression of a cis-Golgi SNARE protein altered concomitantly its incorporation in transport vesicles and its intra-Golgi localization. These observations suggest that, contrary to resident Golgi enzymes, SNARE proteins are localized in the Golgi apparatus as the result of a dynamic transport equilibrium.

Animals↗
PubMed2002

Buds of the Golgi apparatus in parotid acinar cells.

The Golgi apparatus (GA) is a membranous organelle composed of stacked cisterns with associated vesicles. This study was undertaken to determine its origin in rat parotid acinar cells. The morphogenesis of the GA could be recognized in the developmental process as well as in mitotic division of cells. EM studies depicted an aggregation of small vesicles in the early stage of postnatal development or mitosis, that appeared to be the rudimental element of GA. Brefeldin A induced rapid degradation of the cisternal structure to vesicular aggregates. Reconstruction of the GA structure based on these remnant vesicles was observed upon removal of the drug. Similar membranous assembly could be observed after destruction of microtubules. These membranous aggregates presumably corresponded to 'buds of the GA' in parotid acinar cells. However, conventional cytochemical markers for GA were not detected on such immature form of GA. We found that the GA matrix protein GM130 and osmium reductivity (a classical marker for cis-Golgi elements) were consistently localized in the GA elements. Therefore, immunohistochemical distribution of GM130 and osmium impregnation of parotid acinar cells were studied under various dynamic conditions that produced structural modification of the GA.

Animals↗
PubMedDate not supplied

The Golgi apparatus of Tetrahymena thermophila.

Electron microscopic investigations reveal that the Golgi apparatus of Tetrahymena thermophila consists of numerous tiny dictyosomes, each consisting of one or two cisternae. The dictyosomes are localized predominantly in the cell cortex closely associated with the mitochondria, arranged in meridians alternating with the ciliary meridians. We estimated about 300-400 of these dictyosomes in the periphery of a cell, a value corresponding to the number of somatic cilia per cell. Cytochemical assays of thiamine pyrophosphatase and acid phosphatase, both marker enzymes of trans Golgi cisternae, resulted in deposits of lead or cerium phosphate in the outermost cisternae of the dictyosomes. In addition, cisternae located at the bases of the basal body/parasomal sac arrangements are stained. This indicates that these cisternae may belong to the Golgi apparatus of the cell.

Acid Phosphatase↗
PubMed1984

Monodehydroascorbate as an electron acceptor for NADH reduction by coated vesicle and Golgi apparatus fractions of rat liver.

Coated vesicles were isolated from rat liver in about 80% fraction purity as determined from electron microscopy and analyses of marker enzymes and compared with Golgi apparatus and other membrane fractions isolated in parallel. The fractions were enriched in NADH-monodehydroascorbate reductase, ascorbate oxidase and ascorbic acid. The NADH-monodehydroascorbate reductase and ascorbate oxidase of the Golgi apparatus and coated vesicles differed from that of the endoplasmic reticulum in being inhibited by the sodium selective ionophore, monensin, at physiological concentrations while these activities were stimulated by ethylenediaminetetraacetic acid in coated vesicles but not in Golgi apparatus. Activities of both coated vesicles and Golgi apparatus fractions depleted in the coat protein, clathrin, were activated by the addition of clathrin-rich supernatant fractions. The results are discussed in the context of monodehydroascorbate as an acceptor for electron transport-mediated transfer of electrons from NADH by coated vesicles as part of a possible mechanism to drive membrane translocations or to acidify the interiors of vesicles.

Animals↗
PubMed1995

BCMAp: an integral membrane protein in the Golgi apparatus of human mature B lymphocytes.

BCMA is a human gene expressed preferentially in mature B lymphocytes as a 1.2 kb mRNA, which encodes a 184 amino acid peptide (BCMAp). The study of BCMA mRNA expression, using human malignant B cell lines characteristic of different stages of B lymphocyte differentiation, demonstrated that the BCMA mRNA is absent in the pro-B lymphocyte stage. It is expressed faintly at the pre-B cell stage and its expression increases with B lymphocyte maturation. Polyclonal antibodies were used to show, by cellular fractionation and immunoprecipitation, that BCMAp is a non-glycosylated integral membrane protein. Furthermore, BCMAp inserts, in vitro, into canine microsomes, as a type I integral membrane protein. Cell surface labeling showed that BCMAp is not expressed in the plasma membrane of mature B lymphocytes. Immunofluorescence studies revealed that BCMAp lies in a cap-like structure near the nucleus, that was identified as the Golgi apparatus by co-localization of BCMAp with CTR433, a marker of the medial cisternae of the Golgi apparatus. Confocal scanning laser microscopy of U266 plasma cells labeled with markers of various Golgi apparatus subcompartments strongly suggests that BCMAp is located in the cis part of the Golgi apparatus. Thus, BCMAp is the first Golgi resident protein with a tissue specificity and whose expression is linked to the stage of differentiation of B lymphocytes. The location of BCMAp in the Golgi apparatus and its high expression in plasmocytes (secreting large amounts of Ig) suggest that BCMAp is implicated in the intracellular traffic of Ig.

B-Cell Maturation Antigen↗
PubMed2001

The Golgi apparatus of goblet cells in the mouse descending colon: three-dimensional visualization using a confocal laser scanning microscope.

The three-dimensional structure of the Golgi apparatus was studied in goblet cells in lectin-stained sections of the mouse descending colon by using a confocal laser scanning microscope. In the lower part of the crypt, the Golgi apparatus formed a dome- or globe-like structure in the supranuclear region. The wall of the dome had some holes, one of which usually faced toward the nucleus and others toward the apical cytoplasm. Mucous granules seemed to be initially released into the interior of the dome and transported toward the apical cytoplasm through the holes. In the upper part of the crypt, on the other hand, the Golgi apparatus formed a cup- or funnel-like structure with a larger opening toward the cell apex and a smaller opening toward the nucleus. A large mass of mucous granules occupied the inside of the cup to the apical cytoplasm. It is thought that the accumulation of mucous granules enlarges holes at the ceiling of the dome to form a large opening, which makes the configuration of the Golgi apparatus cup-shaped.

Animals↗
PubMed1984

Biosynthesis of a disialylated sequence in N-linked oligosaccharides: identification of an N-acetylglucosaminide (alpha 2----6)-sialyltransferase in Golgi apparatus from rat liver.

Rat liver Golgi apparatus are shown to have a CMP-N-acetylneuraminate: N-acetylglucosaminide (alpha 2----6)-sialyltransferase which catalyzes the conversion of the human milk oligosaccharide LS-tetrasaccharide-a (NeuAc alpha 2----3Gal beta 1---- 3GlcNAc beta 1----3Gal beta 1----4Glc) to disialyllacto -N- tetraose containing the terminal sequence: (formula: see text) found in N-linked oligosaccharides of glycoproteins. The N-acetylglucosaminide (alpha 2----6)-sialyltransferase has a marked preference for the sequence NeuAc alpha 2----3-Gal beta 1---- 3GlcNAc as an acceptor substrate. Thus, the order of addition of the two sialic acids in the disialylated structure shown above is proposed to be first the terminal sialic acid in the NeuAc alpha 2----3Gal linkage followed by the internal sialic acid in the NeuAc alpha 2---- 6GlcNAc linkage. Sialylation in vitro of the type 1 branches (Gal beta 1---- 3GlcNAc -) of the N-linked oligosaccharides of asialo prothrombin to produce the same disialylated sequence is also demonstrated.

Animals↗
PubMed1990

Fragmentation of re-formation of mitotic Golgi apparatus detected by a centrifugal method.

The fragmentation/re-formation process of the Golgi apparatus during mitosis was studied by flotation centrifugation in a stepwise sucrose density gradient. The mitotic Golgi fraction was obtained from Chinese hamster ovary cells synchronized with thymidine and nocodazole. The Golgi apparatus detected by a marker enzyme, galactosyltransferase, was separated into two peaks by the flotation centrifugation. The amount of the Golgi recovered at the lower density peak was less in the mitotic cells than in the interphase cells. The separation profile of the mitotic Golgi returned to that of the interphase Golgi by further incubation of the mitotic cells. The re-formation of the fragmented Golgi was inhibited by nocodazole and vinblastine, but not by actinomycin D and cycloheximide.

Animals↗
PubMed1993

Effect of brefeldin A on the structure of the Golgi apparatus and on the synthesis and secretion of proteins and polysaccharides in sycamore maple (Acer pseudoplatanus) suspension-cultured cells.

Brefeldin A (BFA), a specific inhibitor of Golgi-mediated secretion in animal cells, has been used to study the organization of the secretory pathway and the function of the Golgi apparatus in plant cells. To this end, we have employed a combination of electron microscopical, immunocytochemical, and biochemical techniques to investigate the effects of this drug on the architecture of the Golgi apparatus as well as on the secretion of proteins and complex cell wall polysaccharides in sycamore maple (Acer pseudoplatanus) suspension-cultured cells. We have used 2.5 and 7.5 micrograms/mL of BFA, which is comparable to the 1 to 10 micrograms/mL used in experiments with animal cells. Electron micrographs of high-pressure frozen and freeze-substituted cells show that although BFA causes swelling of the endoplasmic reticulum cisternae, unlike in animal cells, it does not induce the disassembly of sycamore maple Golgi stacks. Instead, BFA induces the formation of large clusters of Golgi stacks, an increase in the number of trans-like Golgi cisternae, and the accumulation in the cytoplasm of very dense vesicles that appear to be derived from trans Golgi cisternae. These vesicles contain large amounts of xyloglucan (XG), the major hemicellulosic cell wall polysaccharide, as shown by immunocytochemical labeling with anti-XG antibodies. All of these structural changes disappear within 120 min after removal of the drug. In vivo labeling experiments using [3H]leucine demonstrate that protein secretion into the culture medium, but not protein synthesis, is inhibited by approximately 80% in the presence of BFA. In contrast, the incorporation of [3H]fucose into N-linked glycoproteins, which occurs in trans-Golgi cisternae, appears to be affected to a greater extent than the incorporation of [3H]xylose, which has been localized to medial Golgi cisternae. BFA also affects secretion of complex polysaccharides as evidenced by the approximate 50% drop in incorporation of [3H]xylose and [3H]fucose into cell wall hemicelluloses. Taken together, these findings suggest that at concentrations of 2.5 to 7.5 mu g/mL BFA causes the following major changes in the secretory pathway of sycamore maple cells: (a) it inhibits the transport of secretory proteins to the cell surface by about 80% and of hemicelluloses by about 50%; (b) it changes the patterns of glycosylation of N-linked glycoproteins and hemicelluloses; (c) it reduces traffic between trans Golgi cisternae and secretory vesicles; (d) it produces a major block in the transport of XG-containing, dense secretory vesicles to the cell surface; and (e) it induces the formation of large aggregates of Golgi apparatus of plant and animal cels share many functional and structural characteristics, the plant Golgi apparatus possesses properties that make its response to BFA unique.

Brefeldin A↗
PubMed1998

Inheritance of the mammalian Golgi apparatus during the cell cycle.

The creation and propagation of the intricate Golgi architecture during the cell cycle poses a fascinating problem for biologists. Similar to the inheritance process for nuclear DNA, the inheritance of the Golgi apparatus consists of biogenesis (replication) and partitioning (mitosis/meiosis) phases, in which Golgi components must double in unit mass, then be appropriately divided between nascent daughter cells during cytokinesis. In this article we focus discussion on the recent advances in the area of Golgi inheritance, first outlining our current understanding of the behaviour of the Golgi apparatus during cell division, then concluding with a more conceptual discussion of the Golgi biogenesis problem. Throughout, we attempt to integrate ultrastructural and biochemical findings with more recent information obtained using live cell microscopy and morphological techniques.

Animals↗
PubMed1986

Differential subcompartmentation of terminal glycosylation in the Golgi apparatus of intestinal absorptive and goblet cells.

Two terminal glycosyltransferases, a sialyltransferase and the blood group A alpha 1,3 N-acetylgalactosaminyltransferase, were found to exhibit differential subcompartmentation in the Golgi apparatus of intestinal goblet and absorptive cells. As expected from their role in terminal glycosylation, the two glycosyltransferases and their products, sialic acid residues and blood group A substance, were localized in the trans cisternae of the Golgi apparatus of goblet cells. In contrast, however, they were found throughout the Golgi apparatus stack of adjacent absorptive cells, with the exception of the fenestrated first cis cisterna. The results are in contrast to the general view that enzymes in the glycosylation pathway are arranged in a cis to trans gradient across the Golgi apparatus and that such polarized distributions may instead be cell type-specific.

ABO Blood-Group System↗
PubMed1995

The polyprotein precursor to the Euglena light-harvesting chlorophyll a/b-binding protein is transported to the Golgi apparatus prior to chloroplast import and polyprotein processing.

The major Euglena thylakoid protein, the light harvesting chlorophyll a/b-binding protein of photosystem II (pLHCPII) is synthesized in the cytoplasm as a polyprotein precursor composed of a 141 amino acid presequence containing a signal peptide domain followed by eight mature LHCPIIs covalently linked by a decapeptide. To determine the transport route from cytoplasm to chloroplast and the site of polyprotein processing, Euglena was pulse labeled with [35S]sulfate, organelles separated on sucrose gradients, and pLHCPII and LHCPII immunoprecipitated and separated on SDS gels. After a 10-min pulse, the pLHCPII polyprotein was found in the endoplasmic reticulum (ER) and Golgi apparatus. LHCPII was undetectable after a 10-min pulse consistent with the 20-min half-life for pLHCPII processing. When pulse-labeled cells were chased for 20 or 40 min with unlabeled sulfate, the fraction of pLHCPII in the ER decreased, and the fraction in the Golgi apparatus increased. LHCPII appeared only in thylakoids and chloroplasts, never in the ER or Golgi apparatus. Na2CO3 extraction, a treatment that releases soluble but not integral membrane proteins, did not remove pLHCPII from ER and Golgi membranes. Trypsin digestion of ER and Golgi membranes produced 4 pLHCPII membrane protected fragments. The Euglena pLHCPII polyprotein is transported as an integral membrane protein from the ER to the Golgi apparatus and from the Golgi apparatus to the chloroplast. Polyprotein processing appears to occur during or soon after chloroplast import of the membrane-bound precursor.

Animals↗
PubMed1999

Three-dimensional structure of the Golgi apparatus in mouse spermatids: a scanning electron microscopic study.

In this study, the three-dimensional organization of the Golgi apparatus in mouse spermatids was elucidated by preparing testicular tissue with the osmium-DMSO-osmium method and examining it by stereo-scanning electron microscopy. The cis-most saccule was found to be a regular network of anastomotic membranous tubules covered by a single cisterna of ER. The trans-Golgi network was seen to be composed of irregular saccules perforated by pores at the edge. It appears that the anastomosing trans-Golgi network breaks down into strings of connected vesicles which arise from the edge of the saccules during the cap phase of spermiogenesis. Many apparently individual vesicles seen in thin sections through the trans-Golgi network are actually joined in continuous strings. This was the first time that these structures could be visualized directly without three-dimensional image reconstruction. By correlating the morphology of the Golgi apparatus with the stage of acrosome formation, the Golgi cisternae were found to change dynamically in a cis-trans direction from fenestrated saccules to continuous strings of vesicles, which finally dissipated as transport vesicles at the trans aspect. This suggests that the hypothetical model of cisternal maturation, which dictates that cargo moves through the Golgi apparatus without leaving the cisternal lumen and the secretion occurs by progressive maturation of the Golgi cisternae as they move in the cis-trans direction, may be applicable to acrosome formation.

Acrosome↗