scholarly journals Isolation and Amino Acid Sequence of a Protein-synthesis Inhibitor from the Seeds of Rye (Secale cereale)

1998 ◽  
Vol 62 (6) ◽  
pp. 1152-1156 ◽  
Author(s):  
Yuji MINAMI ◽  
Ken-ichi YAMAGUCHI ◽  
Fumio YAGI ◽  
Kenjiro TADERA ◽  
Gunki FUNATSU
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Secale Cereale ◽  
Protein Synthesis Inhibitor ◽  
Synthesis Inhibitor

scholarly journals Effects of insulin and anchorage on hepatocytic protein metabolism and amino acid transport

1981 ◽  
Vol 48 (1) ◽  
pp. 1-18
Author(s):  
A. Poli ◽  
P.B. Gordon ◽  
P.E. Schwarze ◽  
B. Grinde ◽  
P.O. Seglen
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Protein Degradation ◽  
Amino Acid Transport ◽  
Protein Synthesis Inhibitor ◽  
Acid Transport ◽  
Synthesis Inhibitor ◽  
Insulin Effect ◽  
High Amino Acid ◽  
Amino Acid Concentrations

Insulin partially inhibits endogenous protein degradation in isolated hepatocytes. The inhibition seems to specifically affect the lysosomal pathway of degradation, since it is not additive to the effects of lysosome inhibitors such as propylamine and leupeptin. The insulin effect is potentiated by intermediate concentrations of amino acids, but is largely abolished at high amino acid concentrations which suppress degradation maximally, suggesting that the hormone may exert its effect indirectly by acting upon the more basal amino acid control mechanism. Glucagon, which stimulates protein degradation, similarly displays its effect only in the presence of intermediate amino acid concentrations. The insulin inhibition is not affected by the aminotransferase inhibitor, aminooxyacetate, indicating that it is not due to interference with amino acid metabolism. Protein synthesis furthermore does not seem to be required, since a significant insulin effect can be seen in the presence of the protein synthesis inhibitor, cycloheximide. The issue is, however, complicated by the fact that cycloheximide itself inhibits protein degradation to approximately the same extent as does insulin. Insulin stimulates uptake of the amino acid alpha-aminoisobutyrate (AIB), but not the uptake of valine, indicating a specific stimulation of ‘A’-type transport. Cycloheximide similarly stimulates AIB uptake, without completely obfuscating the transport effect of insulin. Neither protein synthesis, protein degradation, amino acid transport, nor the effects of insulin were affected by cell-to-substratum anchorage (attachment and spreading) in any detectable way.

scholarly journals Effect of emetine, a protein synthesis inhibitor, on larval tail resorption in the ascidian Halocynthia roretzi

2006 ◽  
Vol 23 (2) ◽  
pp. 43-46
Author(s):  
Kiyotaka Matsumura ◽  
Manami Nagano ◽  
Sachiko Tsukamoto ◽  
Haruko Kato ◽  
Nobuhiro Fusetani
Keyword(s):  
Protein Synthesis ◽  
Protein Synthesis Inhibitor ◽  
Synthesis Inhibitor ◽  
Halocynthia Roretzi

scholarly journals Local protein synthesis of neuronal MT1-MMP for agrin-induced presynaptic development

Development ◽  
2021 ◽  
Vol 148 (10) ◽  
Author(s):  
Jun Yu ◽  
Marilyn Janice Oentaryo ◽  
Chi Wai Lee
Keyword(s):  
Protein Synthesis ◽  
Neuronal Development ◽  
Neuromuscular Junctions ◽  
Neuronal Cell ◽  
Time Lapse ◽  
Protein Synthesis Inhibitor ◽  
Synthesis Inhibitor ◽  
Local Protein Synthesis ◽  
Presynaptic Differentiation ◽  
Local Protein

ABSTRACT Upon the stimulation of extracellular cues, a significant number of proteins are synthesized distally along the axon. Although local protein synthesis is crucial for various stages throughout neuronal development, its involvement in presynaptic differentiation at developing neuromuscular junctions remains unknown. By using axon severing and microfluidic chamber assays, we first showed that treatment of a protein synthesis inhibitor, cycloheximide, inhibits agrin-induced presynaptic differentiation in cultured Xenopus spinal neurons. Newly synthesized proteins are prominently detected, as revealed by the staining of click-reactive cell-permeable puromycin analog O-propargyl-puromycin, at agrin bead-neurite contacts involving the mTOR/4E-BP1 pathway. Next, live-cell time-lapse imaging demonstrated the local capturing and immobilization of ribonucleoprotein granules upon agrin bead stimulation. Given that our recent study reported the roles of membrane-type 1 matrix metalloproteinase (MT1-MMP) in agrin-induced presynaptic differentiation, here we further showed that MT1-MMP mRNA is spatially enriched and locally translated at sites induced by agrin beads. Taken together, this study reveals an essential role for axonal MT1-MMP translation, on top of the well-recognized long-range transport of MT1-MMP proteins synthesized from neuronal cell bodies, in mediating agrin-induced presynaptic differentiation.

Protein synthesis requirement of the Aplysia circadian clock. Tested by active and inactive derivatives of the inhibitor anisomycin

1980 ◽  
Vol 85 (1) ◽  
pp. 33-42
Author(s):  
J. W. Jacklet
Keyword(s):  
Protein Synthesis ◽  
Circadian Clock ◽  
Compound Action Potential ◽  
Phase Shifts ◽  
Protein Synthesis Inhibitor ◽  
Synthesis Inhibitor ◽  
Inhibitor Molecule ◽  
Group 5 ◽  
Characteristic Effect ◽  
Derivatives Of

1.The circadian rhythm of compound action potential frequency recorded from the isolated eye of Aplysia in culture medium and darkness was subjected to 6 h pulse treatments with either anisomycin, a protein synthesis inhibitor, or inactive derivatives of anisomycin. 2. Anisomycin caused phase-dependent phase shifts of the rhythm as expected from previous experiments, but none of the derivative molecules caused phase shifts or perturbed the rhythm. 3. Anisomycin inhibited eye-protein synthesis by 75% at the concentrations (10(−6) M) used in the phase shifting experiments but none of the derivatives inhibited synthesis. 4. Only those molecules that actually inhibited protein synthesis caused phase shifts of the clock, although the inactive derivatives differed from anisomycin by only an acetyl group. 5. The results strengthen the conclusion that the inhibition of protein synthesis caused by anisomycin is important in perturbing the timing of the circadian clock and not some other characteristic effect of the inhibitor molecule. Together with the results from other systems, these findings imply that the daily synthesis of protein is a general requirement for circadian clocks.

scholarly journals Transforming Potential of the Herpesvirus Oncoprotein MEQ: Morphological Transformation, Serum-Independent Growth, and Inhibition of Apoptosis

1998 ◽  
Vol 72 (1) ◽  
pp. 388-395 ◽  
Author(s):  
Juinn-Lin Liu ◽  
Ying Ye ◽  
Lucy F. Lee ◽  
Hsing-Jien Kung
Keyword(s):  
Protein Synthesis ◽  
Target Genes ◽  
Rapid Development ◽  
Fibroblast Cell ◽  
Protein Synthesis Inhibitor ◽  
Morphological Transformation ◽  
Synthesis Inhibitor ◽  
Necrosis Factor Alpha ◽  
Downstream Target ◽  
T Cell Lymphomas

ABSTRACT Marek’s disease virus (MDV) induces the rapid development of overwhelming T-cell lymphomas in chickens. One of its candidate oncogenes, meq (MDV Eco Q) which encodes a bZIP protein, has been biochemically characterized as a transcription factor. Interestingly, MEQ proteins are expressed not only in the nucleoplasm but also in the coiled bodies and the nucleolus. Its novel subcellular localization suggests that MEQ may be involved in other functions beyond its transcriptional potential. In this report we show that MEQ proteins are expressed ubiquitously and abundantly in MDV tumor cell lines. Overexpression of MEQ results in transformation of a rodent fibroblast cell line, Rat-2. The criteria of transformation are based on morphological transfiguration, anchorage-independent growth, and serum-independent growth. Furthermore, MEQ is able to distend the transforming capacity of MEQ-transformed Rat-2 cells through inhibition of apoptosis. Specifically, MEQ can efficiently protect Rat-2 cells from cell death induced by multiple modes including tumor necrosis factor alpha, C2-ceramide, UV irradiation, and serum deprivation. Its antiapoptotic function requires new protein synthesis, as treatment with a protein synthesis inhibitor, cycloheximide, partially reversed MEQ’s antiapoptotic effect. Coincidentally, transcriptional induction of bcl-2 and suppression of bax are also observed in MEQ-transformed Rat-2 cells. Taken together, our results suggest that MEQ antagonizes apoptosis through regulation of its downstream target genes involved in apoptotic and/or antiapoptotic pathways.

Sign in / Sign up

Export Citation Format

Share Document