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Query: UNIPROT:P06889 (Mol)
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Primary cultured sensory neurons prepared from adult mice were maintained for 8 days in vitro. Such cultures were exposed to either a range of ethanol concentrations (50-300 mM) or acetaldehyde (0.5-2 mM) in serum-free medium for up to 24 h. Treated neuronal cultures, together with untreated controls in both the presence and absence of serum, were prepared for transmission electron microscopy. Nuclear morphology was not changed following treatment with either substance at the doses studied. A number of changes were observed, however, in the cytoplasm of neurons, and these were intensified by an increase in concentration and the length of exposure. Acetaldehyde induced effects at a much lower concentration than was required to induce a response with ethanol. Myelin lamellae loosely wound around dense granular core material appeared in multivesicular bodies at low doses. The prevalence of these increased with concentrations of 100 mM ethanol and 1 mM acetaldehyde; the numbers of lamellae in each myelin figure also increased but the core material was less prominent. Electron-dense bodies were also evident at higher dosages together with evidence of vacuolation of the endoplasmic reticulum and Golgi complexes. Mitochondrial profiles similar to those in untreated neurons persisted throughout the exposure periods. The generation of these inclusions may reflect a mechanism of membrane turnover, both of internal systems and cell membrane cycling, as a response to alcohol and aldehyde treatment.
Virchows Arch B Cell Pathol Incl Mol Pathol 1991
PMID:Cytoplasmic changes in primary cultured adult mouse sensory neurons induced by ethanol and acetaldehyde treatments. 168 82

A human fetal bronchial epithelial cell line (HFBE) grew in an undifferentiated pattern under conventional culture conditions. Despite a somewhat fibroblastic shape the cells maintained immunoreactivity to cytokeratin, carcinoembryonic antigen and epithelial membrane antigen. When grown on a collagen gel in a growth-hormone-supplemented medium, their spindle shape became more conspicuous. With an additional supplement of vitamin A (6 micrograms/ml), most of the cells underwent differentiation by producing many bright inclusion bodies which proved to be strongly positive with periodic acid-Schiff and weakly positive with alcian blue staining. Electron microscopy revealed a well-developed rough endoplasmic reticulum, an enlarged Golgi apparatus and many highly electron-dense secretory granules resembling those of Clara cells. Biochemical analysis demonstrated that HFBE cells cultured on collagen gel with vitamin A secreted hyaluronic acid and neutral glycoproteins containing mainly N-linked glycoproteins whose glycans were of a complex type. A monoclonal antibody (SEC-41) generated against the neutral glycoproteins detected a glycoprotein of approximately 52 kDa in the spent culture medium of differentiated HFBE cells. This antibody also reacted with the intracytoplasmic secretory granules in these cells. When tested on frozen sections of lung tissue, the immunohistochemical reactivity of the SEC-41 antibody was confined to Clara cells, some type II pneumocytes in the adult lung, and respiratory epithelial cells in the fetal lung. Moreover, this antibody could detect secretory glycoprotein in broncho-alveolar lavages from two patients. This paper clearly demonstrates that cells derived from human fetal bronchial epithelium can be cultivated in an undifferentiated precursor state and, under appropriate culture conditions, can be stimulated to undergo differentiation into a Clara cell type.
Virchows Arch B Cell Pathol Incl Mol Pathol 1991
PMID:Secretory differentiation and cell type identification of a human fetal bronchial epithelial cell line (HFBE). 168 83

The ultrastructural localization of RNA in myeloma cells was studied by the RNase-gold method. Gold particles indicating the presence of RNA were observed in large numbers, particularly in the granular component of the nucleolus and periphery of the rough endoplasmic reticulum, but not in the Golgi area, mitochondria, intranuclear inclusion bodies, cytoplasmic inclusion bodies, dense bodies, or cisternae of the rough endoplasmic reticulum. In the nuclear chromatin and nucleolus, gold particles were more numerous as these structures were less mature. They were found in larger numbers also in the cytoplasm of immature cells. In plasma cells from patients with macroglobulinemia, gold particles were fewer than in myeloma cells of multiple myeloma, but there was no difference in their distribution pattern.
Exp Mol Pathol 1990 Jun
PMID:Fine structural localization of RNA in myeloma cells detected by the enzyme-gold method. 169 57

The application of 3H-uridine radioautography results in labeling of the liver cells in which RNA is synthesized at various ages of the mouse. Quantitative changes of RNA synthesis in the hepatocytes of aging mice were studied by electron microscopic radioautography. The silver grains were mainly located in the nucleoli and nuclei and a few in the mitochondria and rough surfaced endoplasmic reticulum of almost all of the cell populations at various ages. The number of silver grains in the hepatocyte gradually increased after birth, reached the maximum at 14 days of postnatal age, then decreased to 24 months with aging. The number of silver grains of the euchromatin was more than those of the heterochromatin of the hepatocyte nuclei at various ages. The number of silver grains of the granular components was more than those of the fibrillar components of the hepatocyte nucleoli at various ages. However, the ratio of silver grains among euchromatin, heterochromatin, granular components and fibrillar components remained approximately constant.
Cell Mol Biol 1990
PMID:Study of RNA synthesis in the livers of aging mice by means of electron microscopic radioautography. 170 65

Cyclophilin is a ubiquitously expressed cytosolic peptidyl-prolyl cis-trans isomerase that is inhibited by the immunosuppressive drug cyclosporin A. A degenerate oligonucleotide based on a conserved cyclophilin sequence was used to isolate cDNA clones representing a ubiquitously expressed mRNA from mice and humans. This mRNA encodes a novel 20-kDa protein, CPH2, that shares 64% sequence identity with cyclophilin. Bacterially expressed CPH2 binds cyclosporin A and is a cyclosporin A-inhibitable peptidyl-prolyl cis-trans isomerase. Cell fractionation of rat liver followed by Western blot (immunoblot) analysis indicated that CPH2 is not cytosolic but rather is located exclusively in the endoplasmic reticulum. These results suggest that cyclosporin A mediates its effect on cells through more than one cyclophilin and that cyclosporin A-induced misfolding of T-cell membrane proteins normally mediated by CPH2 plays a role in immunosuppression.
Mol Cell Biol 1991 Jul
PMID:An endoplasmic reticulum-specific cyclophilin. 171 Jul 67

The mammalian signal recognition particle (SRP) is a small cytoplasmic ribonucleoprotein required for the cotranslational targeting of secretory proteins to the endoplasmic reticulum membrane. The heterodimeric protein subunit SRP9/14 was previously shown to be essential for SRP to cause pausing in the elongation of secretory protein translation. RNase protection and filter binding experiments have shown that binding of SRP9/14 to SRP RNA depends solely on sequences located in a domain of SRP RNA that is strongly homologous to the Alu family of repetitive DNA sequences. In addition, the use of hydroxyl radicals, as RNA-cleaving reagents, has revealed four distinct regions in this domain that are in close contact with SRP9/14. Surprisingly, the nucleotide sequence in one of these contact sites, predicted to be mostly single stranded, was found to be extremely conserved in SRP RNAs of evolutionarily distant organisms ranging from eubacteria and archaebacteria to yeasts and higher eucaryotic cells. This finding suggests that SRP9/14 homologs may also exist in these organisms, where they possibly contribute to the regulation of protein synthesis similar to that observed for mammalian SRP in vitro.
Mol Cell Biol 1991 Aug
PMID:Binding sites of the 9- and 14-kilodalton heterodimeric protein subunit of the signal recognition particle (SRP) are contained exclusively in the Alu domain of SRP RNA and contain a sequence motif that is conserved in evolution. 171

Alph alpha 2-macroglobulin (alpha 2M), a protease inhibitor which also binds growth factors and cytokines, is temporally expressed in association with remodelling phenomena in the ovary: ovulation and luteinization. Specific hormonal, cellular, subcellular, and molecular events regulating alpha 2M mRNA and protein have been analyzed during follicular growth, ovulation, and luteinization using complementary in vivo and in vitro models. Data demonstrate that alpha 2M mRNA and protein are synthesized in thecal cells of developing follicles in response to low levels of LH. Conversely, alpha 2M mRNA and protein are only synthesized by granulosa cells of follicles that have been stimulated to luteinize either in vivo by the LH surge or in vitro by FSH and testosterone and are also exposed to PRL. The obligatory requirement for PRL is specific; associated with increased numbers of PRL-binding sites; mediated by time-dependent appearance of alpha 2M in the endoplasmic reticulum (12 h), Golgi apparatus (24 h), and secretion vesicles (48 h); and involves in part increased transcription of the alpha 2M gene.
Mol Endocrinol 1991 Sep
PMID:Regulation of alpha 2-macroglobulin by luteinizing hormone and prolactin during cell differentiation in the rat ovary. 172 70

We have constructed three gene fusions that encode portions of a membrane protein, arginine permease, fused to a reporter domain, the cytoplasmic enzyme histidinol dehydrogenase (HD), located at the C-terminal end. These fusion proteins contain at least one of the internal signal sequences of arginine permease. When the fusion proteins were expressed in Saccharomyces cerevisiae and inserted into the endoplasmic reticulum (ER), two of the fusion proteins placed HD on the luminal side of the ER membrane, but only when a piece of DNA encoding a spacer protein segment was inserted into the fusion joint. The third fusion protein, with or without the spacer included, placed HD on the cytoplasmic side of the membrane. These results suggest that (i) sequences C-terminal to the internal signal sequence can inhibit membrane insertion and (ii) HD requires a preceding spacer segment to be translocated across the ER membrane.
Mol Cell Biol 1992 Jan
PMID:C-terminal sequences can inhibit the insertion of membrane proteins into the endoplasmic reticulum of Saccharomyces cerevisiae. 172 4

The application of 3H-leucine results in labeling of the liver cells of mice in which protein is synthesized at various ages of the animals. Quantitative changes of protein synthesis in the hepatocytes of aging mice were studied by electron microscopic radioautography. The silver grains in the hepatocytes were mainly located over the rough surfaced endoplasmic reticulum, mitochondria, Golgi apparatus, cytoplasmic matrix, and a few over the nuclei. The number of silver grains in the cytoplasm and nuclei of the hepatocytes gradually increased after birth, reached the maximum at 1 month after birth, thereafter it continued to decrease with aging until the 24th month. The number of silver grains in the hepatocyte cytoplasm was more than that in nuclei at various ages. The number of silver grains in the rough surfaced endoplasmic reticulum and mitochondria gradually increased from embryo to 1 month after birth, thereafter it continued to decrease with aging until the 24th month. The number of silver grains in the Golgi apparatus showed almost no change from fetal stage to 6 months after birth, thereafter it continued to decrease with aging until the 24th month. The number of silver grains in the cytoplasmic matrix gradually increased from fetal stage to 2 months after birth, then decreased with aging until the 24th month. These changes reflect the quantity of protein synthesized in each cell organelle at various ages of animals.
Cell Mol Biol 1991
PMID:Protein synthesis in the livers of aging mice studied by electron microscopic radioautography. 174 95

Cholera toxin and Escherichia coli heat-labile enterotoxins are responsible, in part, for the symptomatology of cholera and traveller's diarrhoea, respectively. Effects of the toxins result from ADP-ribosylation of regulatory guanine nucleotide-binding (G) proteins; the ADP-ribosylated G protein is stabilized in an activated state, resulting in prolonged effects on its target. Toxin-catalysed ADP-ribosylation is stimulated in vitro by a family of guanine nucleotide-binding proteins, c. 20 kDa, termed ADP-ribosylation factors or ARFs. In the presence of GTP, but not GDP or adenine analogues, ARFs serve as allosteric activators of the toxin. The effects are amplified by certain phospholipids and detergents which promote guanine nucleotide binding. Six different mammalian ARF genes have been identified. They encode highly conserved, ubiquitous proteins of 175 to 181 amino acids, containing consensus domains responsible for guanine nucleotide binding. Differences in amino acid sequences are localized near the amino terminus and in the carboxy half of the protein. Although the physiological functions of ARFs have not been precisely defined, their immunological localization to the Golgi is consistent with a role in the regulated orderly movement of newly synthesized proteins from the endoplasmic reticulum, through the Golgi system to their ultimate destination.
Mol Microbiol 1991 Nov
PMID:Activation of cholera toxin and Escherichia coli heat-labile enterotoxins by ADP-ribosylation factors, a family of 20 kDa guanine nucleotide-binding proteins. 177 53


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