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2.
J Cell Biol ; 112(2): 237-43, 1991 Jan.
Article in English | MEDLINE | ID: mdl-1988459

ABSTRACT

We have isolated the cDNA for 42Sp48 and EF-1 alpha from mixed stage oocytes and tailbud (stage 22) Xenopus laevis cDNA libraries by use of the cDNA for human elongation factor-1 alpha (EF-1 alpha) as probe. The nucleotide and deduced amino acid sequences of the entire coding region of 42Sp48 and EF-1 alpha cDNA were established. The proposed functional homology of the proteins is reflected in highly conserved amino acid sequences (91% identity), while the large number of silent mutations at the gene level may serve to prevent recombination at their loci. 42Sp48 is apparently encoded by two genes in Xenopus, while no sequences corresponding to 42Sp48 could be found in murine or human genomic DNA. 42Sp48 has been proposed to act as a stage-specific elongation factor in Xenopus. Comparison of the deduced amino acid sequences of 42Sp48 and EF-1 alpha with that of elongation factor Tu from E. coli, for which the three-dimensional structure including that of the GTP binding sites have been determined, supports this hypothesis.


Subject(s)
Peptide Elongation Factors/genetics , Xenopus laevis/genetics , Amino Acid Sequence , Animals , Base Sequence , Blotting, Southern , DNA/genetics , DNA/isolation & purification , Gene Expression Regulation , Genes , Molecular Sequence Data , Mutation , Oocytes , Peptide Elongation Factor 1 , Sequence Homology, Nucleic Acid , Xenopus Proteins
3.
Psychiatry Res ; 31(3): 235-41, 1990 Mar.
Article in English | MEDLINE | ID: mdl-2333355

ABSTRACT

It is generally assumed that anticholinergic drugs have no effects on schizophrenic symptomatology. A few studies, however, indicate that anticholinergic agents aggravate psychotic symptoms and antagonize therapeutic effects of neuroleptics in schizophrenic patients; more recently, some investigators have observed that these agents appear to benefit negative symptoms. In an effort to resolve this issue, we studied the effects of 2 days of treatment with biperiden on positive and negative symptoms in 15 medication-free schizophrenic patients. Positive symptoms increased significantly, while there was a trend toward a decrease in negative symptoms. The implications of these findings for the role of the cholinergic system in schizophrenia are discussed.


Subject(s)
Biperiden/therapeutic use , Piperidines/therapeutic use , Schizophrenia/drug therapy , Schizophrenic Psychology , Adult , Brain/drug effects , Female , Humans , Male , Psychiatric Status Rating Scales , Psychometrics , Receptors, Muscarinic/drug effects
4.
EMBO J ; 6(8): 2409-13, 1987 Aug.
Article in English | MEDLINE | ID: mdl-2444435

ABSTRACT

We have undertaken an immunological and biochemical analysis of the most abundant soluble protein of previtellogenic Xenopus oocytes, 42S p48. We show that this protein shares immunological cross-reactivity with elongation factor 1 alpha (EF-1 alpha). Direct assays of both 42S fractions and purified 42S p48 show that this cross-reactivity is of functional significance since 42S p48, like EF-1 alpha, can transfer charged amino acids to ribosomes. We further demonstrate that 42S p48 is degraded soon after the onset of vitellogenesis, while the EF-1 alpha concentration remains essentially unchanged during this transition. These properties of 42S p48 are discussed with regard to its role in oogenesis.


Subject(s)
Egg Proteins/isolation & purification , Oocytes/cytology , Peptide Elongation Factors/isolation & purification , Animals , Cross Reactions , Egg Proteins/immunology , Epitopes/analysis , Female , Oocytes/analysis , Oogenesis , Peptide Elongation Factor 1 , Peptide Elongation Factors/immunology , Vitellogenins , Xenopus laevis
5.
FEBS Lett ; 164(2): 330-4, 1983 Dec 12.
Article in English | MEDLINE | ID: mdl-6317455

ABSTRACT

Two-dimensional gel electrophoretic (NEPHGE) analysis of proteins from mouse 3T3B and 3T3B/SV40 cells labelled with [methyl-3H]methionine in the presence of cycloheximide have revealed that the elongation factor 1 alpha (EF-1 alpha) in these cells is methylated and that the extent of methylation is higher in the SV40 transformed cell type. It is suggested that methylation may account for differences in growth properties for the different cell types.


Subject(s)
Cell Transformation, Viral , Peptide Elongation Factors/metabolism , Animals , Cell Line , Cycloheximide/pharmacology , Electrophoresis, Polyacrylamide Gel , Fibroblasts/metabolism , Methylation , Mice , Peptide Elongation Factor 1 , Simian virus 40
6.
J Cell Biol ; 96(2): 416-23, 1983 Feb.
Article in English | MEDLINE | ID: mdl-6187751

ABSTRACT

Mouse polyclonal antibodies have been raised against two human proteins (IEF [isoelectric focusing] 31, Mr = 50,000; IEF 46, Mr = 43,500) that have previously been shown to be present in HeLa cytoskeletons enriched in intermediate-sized filaments. Immunoprecipitation studies show that both proteins share common antigenic determinants with each other and with the putative human keratins IEF 36 and 44, also present in HeLa cytoskeletons. Indirect immunofluorescence studies showed that both antibodies revealed similar filamentous networks in various cultured epithelial cells of human origin. These included AMA (transformed amnion), HeLa (cervical carcinoma), normal amnion cells, Fl-amnion (transformed amnion), WISH-amnion (transformed amnion), Chang liver (liver), and Detroid-98 (sternal marrow). Human cells that did not react with both antibodies included skin fibroblasts, lung fibroblasts (WI-38), SV40-transformed lung fibroblasts, Molt 4 (leukemia), lymphocytes, and monocytes. These results were in complete agreement with the presence or absence of both proteins in two-dimensional gels of the different cell types. Exposure of AMA cells to demecolcine (24 h; 10 micrograms/ml) caused the total collapse of vimentin filaments but, as seen by indirect immunofluorescence, caused only a partial redistribution of the IEF 31 and 46 filaments. These results are taken to suggest that both proteins are components of the intermediate-sized filaments of the "keratin" type. The antibodies could be clearly differentiated by staining human bladder carcinoma EJ 19 cells, as only the IEF 46 antibody stained a filamentous network in these cells The occurrence of keratins IEF 31, 36, 44, and 46 in different cultured human epithelial cells has been studied using two-dimensional gel electrophoresis.


Subject(s)
Cytoskeleton/analysis , Keratins/analysis , Antibody Specificity , Cells, Cultured , Electrophoresis, Polyacrylamide Gel , Epithelium/ultrastructure , Fluorescent Antibody Technique , Humans , Isoelectric Point , Keratins/immunology , Molecular Weight
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