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At least 19 recordsLinked to original sources
PubMed1992

Studies on the mechanism of different collagen glucosyltransferase reactions (Golgi apparatus, smooth endoplasmic reticulum, rough endoplasmic reticulum) in chick embryo liver.

1. The galactosylhydroxylysylglucosyltransferase (GGT) specific to collagen is located in the RER (rough endoplasmic reticulum), SER (smooth endoplasmic reticulum) and Golgi apparatus for the chick embryo liver. 2. The UDP-glucose collagen glucosyltransferase activities in chick embryo liver were solubilized by Nonidet P-40. 3. The mechanism of collagen glucosyltransferase reaction was studied with enzyme preparation of Golgi apparatus CF2, smooth endoplasmic reticulum CF4 and rough endoplasmic reticulum CF8. 4. For the three fractions, data obtained in experiments were consistent with a sequential ordered mechanism in which the substrates are bound to the enzyme in the following order: Mn2+, collagen and UDP-glucose substrate, with different values for Km and Vmax.

Animals↗
PubMed1974

Changes in the ribosome content, principal microsomal protein composition, and secretory character of mammary epithelial rough endoplasmic reticulum during differentiation. Evidence that messenger RNAs specific for milk proteins are incorporated into rough endoplasmic reticulum formed de novo after parturition.

The equilibrium density distribution, protein composition, and secretory character of mouse mammary epithelial rough microsomes have been determined during differentiation. The density range exhibited by the rough microsomes broadens during mammary development; rough microsomes within the 1.25-1.29 g/ml density range appear soon after conception and then within the 1.30-1.34 range after the onset of lactation. The appearance of these denser microsomes represents the progressive increase of the average ribosome content of the rough endoplasmic reticulum (ER) during gestation and lactation. Fractionation of rough microsomal proteins by sodium dodecyl sulfate-polyacrylamide gel electrophoresis reveals that two proteins, having molecular weights of 57,000 and 76,000, occur to a significant extent only during lactation and are then most prominent in the very dense rough microsomes of the 1.30-1.34 range. Nascent polypeptide chains discharged (by incubation with puromycin) from 17-days lactation rough microsomes in either the 1.21-1.29 or 1.30-1.34 density range are distributed equally between the intra- and extravesicular compartments. Whereas 36% of the chains are discharged intravesicularly from 1-day lactation rough microsomes in the 1.30-1.34 range, only 25% are so discharged from those in the 1.21-1.29 range. The results indicate (a) that there is no correlation between the relative levels in lactation rough microsomes of the two microsomal proteins which become prominent during lactation and the extent of secretory activity and (b) that for a short period after parturition the rough ER elements bearing high surface densities of ribosomes have a greater proportion of ribosomes synthesizing milk proteins than the rough ER elements with moderate ribosome densities.

Animals↗
PubMed1984

Biosynthesis of rat liver cytochrome P-450 in mitochondria-associated rough endoplasmic reticulum and in rough microsomes in vivo.

The hypothesis of a preferential biosynthesis of a major phenobarbital inducible form of hepatic cytochrome P-450 (P-450b) in mitochondria-associated rough endoplasmic reticulum (RERmito) was tested by measuring incorporation rates of [35S]methionine and delta-amino[3H]levulinate into the hemoprotein in adult rats. RERmito, rough microsomes (RM representing RER not associated with mitochondria) and smooth microsomes (SM) were quantitatively isolated from the same homogenate by rate zonal centrifugation and their content of P-450b determined by rocket immunoelectrophoresis. P-450b was isolated by immunoprecipitation from detergent-solubilized membrane fractions. The time course and rate of incorporation of [35S] methionine into immunoprecipitable P-450b of RERmito and of RM were similar at all time points studied (2-15 min) both under conditions of maximal induction (4 injections of phenobarbital in 4 days) and after a single injection of phenobarbital. The incorporation of [35S]methionine into P-450b of SM was slower at early time points (2-8 min) but similar to RERmito and RM after 15 min. In contrast, at short labeling periods (less than 8 min) more delta-amino[3H]levulinate was incorporated into P-450b of RERmito than into P-450b of RM and SM. No significant accumulation of free apocytochrome P-450b was found in either membrane fraction. These data indicate a close coordination of the biosynthesis and assembly of apocytochrome P-450b and its prosthetic heme but do not support the hypothesis of a major functional role of MITO X RER complexes in the synthesis of microsomal cytochrome P-450b.

Animals↗
PubMed2001

The tubulovesicular system of gastric parietal cells is connected to the intracellular canaliculus, rough endoplasmic reticulum and Golgi complex. A study by high resolution scanning electron microscopy.

The three-dimensional configuration of the tubulovesicular system of resting rat gastric parietal cells was determined by ultra-hihg-resolution scanning electron microscopy (SEM). Rat gastric mucosae were fixed in 1.0% glutaraldehyde and 0.5% formaldehyde in cacodylate buffer, (334 milliosmoles/kgH2O (mOsm)). To render cytoplasmic membranes visible by SEM, fixed mucosae were frozen and fractured, and the cytoplasm of fractured parietal cells was macerated by the aldehyde-osmium-DMSO-osmium procedure. With much of the cell matrix and filaments removed, SEM revealed numerous 30-60 nm tubukes, which formed a meshwork and also small cisternae about 100 nm. Some cisternae had a small, central 10 nm fenestration. The cytoplasmic surface of the tubules was smooth surfaced but some cisternal areas had attached polyribosomes. Isolated vesicles or tubules were not found in adequately macerated parietal cells. The tubulocisternal network was also connected to the Golgi apparatus. In favorable sites connections of the tubular membranes to the canaliculi were clearly visible. Continuity between these two membrane compartments suggests the probability of rapid membrane transposition when cells are stimulated to secrete acid.

Animals↗
PubMed1978

The in vitro reassembly of rough endoplasmic reticulum: ribosome binding capacity.

Rough endoplasmic reticulum membranes were dissolved in 1% deoxycholate and the deoxycholate was then dialysed out for five days. Well-defined bilayer vesicles were formed only if the dialysis was performed at room temperature for the first six hours. The vesicles were separated into a pelleted fraction (Fraction 1) and a fluffy layer (Fraction II) by centrifugation. As measured by amino acid incorporation ability, Fraction II bound polysomes, while Fraction I did not. When smooth endoplasmic reticulum was assembled, it was found that Fraction II so derived had a polysome binding capacity which was more sensitive to increased KCl concentrations (25 mM - 100 mM KCl) and that it bound significantly more monosomes than the corresponding fraction derived from rough membranes. The SDS-polyacrylamide polypeptide patterns of the various fractions were compared.

Binding Sites↗
PubMed1989

Domains of rough endoplasmic reticulum (a review).

The rough endoplasmic reticulum isolated from several eukaryotic cell lines can be separated into subfractions. These subfractions possess different properties indicating that they represent separate domains of the endoplasmic reticulum system.

Animals↗
PubMed1991

Characterization of the rough endoplasmic reticulum ribosome-binding activity.

The rough endoplasmic reticulum membranes of mammalian cells contain specific ribosome-binding sites. A purification to apparent homogeneity of a negatively charged protein (ERp180) of relative molecular mass 180,000 (180 K) was reported which was proposed to function as a rough endoplasmic reticulum ribosome receptor. We report here that ribosome-binding site activity quantitatively solubilized from rough endoplasmic reticulum membranes does not cofractionate with ERp180. By contrast, ribosome-binding site activity fractionates as a much smaller, positively charged protein.

Animals↗
PubMed1999

Purification and characterization of glutamate dehydrogenase as another isoprotein binding to the membrane of rough endoplasmic reticulum.

Glutamate dehydrogenase (GDH) was purified from rough endoplasmic reticulum (RER) in rat liver using anion-exchange and affinity chromatography. As GDH has been known as an enzyme that exists mainly in the matrix of mitochondria, the properties of purified GDH were compared with those of mitochondrial GDH. The GDH activity in 0. 1% Triton X-100-treated RER subcellular fraction was nearly the same as intact RER, whereas that of the mitochondrial fraction increased by 50% after the detergent treatment. In kinetic values, in addition, mitochondrial GDH had a higher K(m) value for NADP(+) than NAD(+), whereas the K(m) value for NAD(+) was higher than that for NADP(+) in the case of GDH of RER, which showed a difference in specificity to cofactors. Moreover, when two GDH isoproteins were incubated at 42 degrees C or treated with trypsin, GDH from RER was more stable against heat inactivation and less susceptible to proteolysis than mitochondrial GDH in both cases. In addition, GDH of RER had at least five amino acids different from mitochondrial GDH when sequences of N-terminal and several internal peptide fragments were analyzed. These results showed that GDH of RER is another isoprotein of GDH, of whose properties are different from those of mitochondrial GDH.

Amino Acid Sequence↗
PubMed2002

Omental malignant fibrous histiocytoma with a unique rough endoplasmic reticulum inclusion.

The laminated inclusions in the rough endoplasmic reticulum (RER) are peculiar structures seen only in some cases of chondrocytes of pseudoachondroplasia. These ultrastructurally unique organelles have not yet been reported in inflammatory malignant fibrous histiocytoma (MFH). We describe an omental mass showing unique laminated inclusions in the RER in a young man with intra-abdominal inflammatory MFH. The most striking ultrastructural feature was a dilated RER containing a fine granular substance and a more electron-dense material exhibiting an onion skin-like lamellated or maze-like pattern, mimicking that of so-called laminated inclusions. These lamellated inclusions occupied most of the cytoplasm of the tumor cells. We speculate that the ultrastructural finding of the laminated RER inclusion is not specific for cartilage cells, but may represent abnormal accumulation of some kind of glycoprotein material or matrix protein. This granular material may undergo organization to form a peculiar laminated structure, probably due to a metabolic or fixation process. Further study is needed to elucidate the nature of this material.

Adult↗
PubMed1986

Depression of cytochrome P-450 and alterations of protein metabolism in mice treated with the interferon inducer polyriboinosinic acid X polyribocytidylic acid.

Treatment of mice with the interferon inducer polyriboinosinic acid X polyribocytidylic acid [poly(IC)] results in the depression of several hepatic proteins. In this study we examined synthesis and degradation of the proteins of liver cell organelles in mice treated with poly(IC). Effects on synthesis were determined by using [14C]- and L-[3H]leucine incorporation into control and poly(IC)-treated mice, respectively. At selected times after poly(IC) treatment the 3H/14C ratio was established for preparations of nuclei, mitochondria, lysosomes, smooth endoplasmic reticulum, rough endoplasmic reticulum, and 105,000g supernatant (cytosol). Time-dependent alterations in de novo protein synthesis were greatest in lysosomal and rough endoplasmic reticular fractions; both were depressed 9 h after treatment. The effects of poly(IC) on protein degradation were determined with [14C]bicarbonate. Poly(IC) treatment decreased the time required for disappearance of 50% of 14C-labeled protein (t1/2) of smooth and rough endoplasmic reticula. Examination of endoplasmic reticulum marker enzymes showed depression of cytochromes P-450 and b5 from 9 h onward after poly(IC) administration. Tyrosine aminotransferase activity was elevated 6 h after treatment with poly(IC), and then depressed after 9 h. The other organelle marker enzymes were not affected significantly. We conclude that poly(IC) decreases the content of proteins of the hepatic endoplasmic reticulum, including certain cytochrome P-450 isozymes, by decreasing rates of protein synthesis and increasing rates of protein degradation.

Amino Acids↗
PubMed1973

Effect of gibberellic Acid and actinomycin d on the formation and distribution of rough endoplasmic reticulum in barley aleurone cells.

Analysis of structural changes in barley aleurone cells during germination or following incubation of isolated layers in gibberellic acid with or without actinomycin D revealed extensive development of rough endoplasmic reticulum. Following the assembly of stacked rough endoplasmic reticulum, vesiculation occurred mainly in basal regions of the cell, resulting in a polar distribution of rough endoplasmic reticulum vesicles. It is postulated that these vesicles are involved in protein secretion, because smooth vesicles, derived from the rough endoplasmic reticulum, apparently become appressed to the plasma membrane. The increased alpha-amylase in the ambient medium and in cell homogenates correlated directly with formation and subsequent vesiculation of the rough endoplasmic reticulum. Furthermore, when cells were treated with actinomycin D and gibberellic acid, alpha-amylase synthesis was inhibited by 45% and secretion by 63%. These cells were characterized cytologically by large areas of disarrayed segments of fragmented rough endoplasmic reticulum, corresponding to a high intracellular level of alpha-amylase. In addition, small lipid bodies common to the segmented regions of rough endoplasmic reticulum were surrounded by fine fibrous material, short segments of rough endoplasmic reticulum, and free ribosomes, suggesting that actinomycin D had interfered with development and organization of rough endoplasmic reticulum.

Journal Article↗
PubMed1978

Fenestrae in the rough endoplasmic reticulum of Xenopus laevis hepatocytes.

The rough endoplasmic reticulum (RER) of Xenopus laevis hepatocytes was examined by freeze-fracture and by conventional thin section electron microscopy. Much of the RER was present as stacks of cisternae at the cell periphery but, in addition, large whorls of cisternae were seen in the cytoplasm in most sections. Freeze-fracture replicas revealed fenestrae in both stacked and whorled cisternae, although the fenestrae were more numerous in the whorls. The role of these fenestrae is unknown, but such structures would facilitate access of precursors to the protein synthetic machinery in this highly metabolically active cell type. This would be particularly important in RER whorls, where the innermost cisternae would otherwise be isolated from the rest of the cytoplasm.

Animals↗
PubMed1972

Binding of rat liver and hepatoma polyribosomes to stripped rough endoplasmic reticulum in vitro. Biological or an artifact?

Exposed thiol groups do not appear to be related to the binding of (32)P-labelled polyribosomes to stripped rough endoplasmic reticulum in vitro. Treating stripped rough endoplasmic reticulum with GSSG did not diminish binding of polyribosomes, suggesting that binding in vitro has no correlation with the inhibition of protein synthesis in vitro reported by Kosower et al. (1971). Thiol reagents, which are known to dissociate ribosomes, did not significantly decrease binding of (32)P-labelled polyribosomes to stripped rough endoplasmic reticulum. Denaturing the protein of (32)P-labelled polyribosomes or stripped rough endoplasmic reticulum of liver or hepatoma with heat, trichloroacetic acid, or HClO(4) did not alter the binding in vitro. Therefore, the practice of measuring the binding of (32)P-labelled polyribosomes to stripped rough endoplasmic reticulum in vitro (Shires et al., 1971b) is an unsuitable indicator of biological significance in the intact cell.

Animals↗
PubMedDate not supplied

Hepatoma secretory proteins migrate from rough endoplasmic reticulum to Golgi at characteristic rates.

In eukaryotic cells, secretory proteins and glycoproteins migrate from the rough endoplasmic reticulum, their site of synthesis, through Golgi vesicles before being released from the cell. Cellular and viral integral plasma membrane glycoproteins are co-translationally inserted into the rough endoplasmic reticulum membrane and follow a similar pathway to the cell surface. Previous studies using endoglycosidase H (Endo H) suggested that in rat hepatoma cells the vesicular stomatitis virus (VSV) G protein, albumin and transferrin migrate from the rough endoplasmic reticulum to the Golgi apparatus at different rates. Here we show directly that in human hepatoma HepG2 cells, five secreted proteins mature from the rough endoplasmic reticulum to Golgi vesicles at characteristic rates which differ at least threefold. The results are incompatible with bulk-phase movement of the luminal contents of the endoplasmic reticulum, and suggest that there is a membrane-bound receptor that selectively mediates the transport of secretory proteins from the rough endoplasmic reticulum to the Golgi.

Animals↗
PubMed1990

Microtubular aggregates within rough endoplasmic reticulum in myxopapillary ependymoma of the filum terminale.

Aggregates of microtubules with-in rough endoplasmic reticulum were found in many neoplastic cells of three cases of myxopapillary ependymoma of the filum terminale studied ultrastructurally. The cytoplasm and cellular processes of some neoplastic cells were distended by the aggregates. In general the involved rough endoplasmic reticulum contained three to six microtubules, but some enclosed more than 10 microtubules. The enclosed microtubules were straight parallel hollow cylindrical structures with fuzzy coats. They had an inner diameter of 12 to 15 nm, an outer diameter of 30 to 35 nm, and a center-to-center distance of 50 to 62 nm. The involved rough endoplasmic reticulum often showed various degrees of loss of surface ribosomes and some appeared totally degranulated. Vacuolar degeneration of involved rough endoplasmic reticulum with fragmentation and disintegration of the enclosed microtubules was frequent. Direct relationship of the enclosed microtubules to the cytoplasmic microtubules and ciliary formation was not found. This unusual microtubular aggregate has not been described in other types of ependymoma, or in other brain tumors. They may represent a characteristic ultrastructural feature of myxopapillary ependymoma.

Adult↗
PubMed1989

Release of soluble resident as well as secretory proteins from HepG2 cells by partial permeabilization of rough-endoplasmic-reticulum membranes.

Secretory proteins migrate from the rough endoplasmic reticulum (ER) to the Golgi complex at different rates. Selective retention of specific proteins to rough-ER membrane constituents could explain this phenomenon. We have permeabilized HepG2 cells with low concentrations of saponin. Release of newly synthesized proteins was studied after brief labelling in the presence of [35S]methionine. The efflux of several secretory proteins was studied at various saponin concentrations; a 2-fold higher saponin concentration was required to release transferrin compared with that required to release albumin and orosomucoid. Glucosidase II, a soluble resident protein of the ER, is released at the same saponin concentration as albumin. Saponin did not destroy the membrane skeleton structure; at the concentrations used, the integral membrane protein G of vesicular-stomatitis virus remained fully associated with the cells.

Albumins↗
PubMed1977

Effect of ethionine on the rough endoplasmic reticulum from male and female rat liver.

Ethionine causes a decrease in the amount of rough endoplasmic reticulum in rat liver, the effect being greater in female than in male rats. Rough endoplasmic reticulum isolated from rat liver 24 hr after ethionine injection and stripped of its ribosomes partially lost its in vitro ribosome binding capacity. However, no differences were detected between the binding affinities of ribosomes, isolated from either untreated animals or intoxicated rats, to stripped rough membranes derived from normal rats. Structural changes occur in the rough endoplasmic reticulum of the ethionine treated rats, while the ribosomes are still bound to the membrane.

Animals↗