In Vitro Membrane Protein Synthesis Inside Cell-Sized Vesicles Reveals the Dependence of Membrane Protein Integration on Vesicle Volume

2013 ◽  
Vol 3 (6) ◽  
pp. 372-379 ◽  
Author(s):  
Haruka Soga ◽  
Satoshi Fujii ◽  
Tetsuya Yomo ◽  
Yasuhiko Kato ◽  
Hajime Watanabe ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Membrane Protein

scholarly journals In vitro membrane protein synthesis inside Sec translocon-reconstituted cell-sized liposomes

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Naoki Ohta ◽  
Yasuhiko Kato ◽  
Hajime Watanabe ◽  
Hirotada Mori ◽  
Tomoaki Matsuura
Keyword(s):  
Protein Synthesis ◽  
Membrane Protein ◽  
Sec Translocon

Direct preparation of giant proteo-liposomes by in vitro membrane protein synthesis

2008 ◽  
Vol 133 (2) ◽  
pp. 190-195 ◽  
Author(s):  
Shin-ichiro M. Nomura ◽  
Satoshi Kondoh ◽  
Wakiko Asayama ◽  
Akikazu Asada ◽  
Shigemichi. Nishikawa ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Membrane Protein ◽  
Direct Preparation

scholarly journals Phagocytosis stimulates alternative glycosylation of macrosialin (mouse CD68), a macrophage-specific endosomal protein

1999 ◽  
Vol 338 (3) ◽  
pp. 687-694 ◽  
Author(s):  
Rosângela P. da SILVA ◽  
Siamon GORDON
Keyword(s):  
Protein Synthesis ◽  
Sialic Acid ◽  
Membrane Protein ◽  
Lectin Binding ◽  
Peritoneal Macrophages ◽  
Binding Activity ◽  
Amaranthus Caudatus ◽  
Galanthus Nivalis ◽  
Particle Internalization

Macrosialin (mouse CD68), a macrophage-specific member of the lysosomal-associated membrane protein family, displays N-linked glycosylation and a heavily sialylated, mucin-like domain. We show that phagocytosis of zymosan by inflammatory peritoneal macrophages potently alters glycan processing of macrosialin in vitro. The phagocytic glycoform is not induced by other forms of endocytosis and depends on particle internalization. Zymosan uptake does not influence macrosialin protein synthesis, but increases the specific incorporation of d-[2-3H]mannose, d-[6-3H]galactose, N-acetyl-d-[1-3H]glucosamine and l-[5,6-3H]fucose by 2–15-fold. The phagocytic glycoform displays increased binding of agglutinins from peanut, Amaranthus caudatus and Galanthus nivalis, whereas binding of the sialic-acid-specific Maakia amurensis agglutinin is slightly reduced. Digestion by N-Glycanase abolishes the incorporation of [3H]mannose label and Galanthus nivalis agglutinin binding activity, but preserves the incorporation of galactose and N-acetylglucosamine and specific lectin binding. We also show that phagocytosis increases the complexity and length of O-linked chains. The data presented highlight the importance of differential glycosylation in the biology of macrosialin, phagosomes and macrophages in general.

scholarly journals Combining in Vitro Folding with Cell Free Protein Synthesis for Membrane Protein Expression

Biochemistry ◽  
2016 ◽  
Vol 55 (30) ◽  
pp. 4212-4219 ◽  
Author(s):  
Paul J. Focke ◽  
Christopher Hein ◽  
Beate Hoffmann ◽  
Kimberly Matulef ◽  
Frank Bernhard ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Membrane Protein ◽  
Protein Expression ◽  
Free Protein ◽  
Membrane Protein Expression ◽  
Cell Free Protein Synthesis

Increased Protein Synthesis by Human Platelets during Phagocytosis of Latex Particles in Vitro

1976 ◽  
Vol 35 (02) ◽  
pp. 350-357 ◽  
Author(s):  
Hana Bessler ◽  
Galila Agam ◽  
Meir Djaldetti
Keyword(s):  
Protein Synthesis ◽  
Fold Increase ◽  
Human Platelets ◽  
Polystyrene Latex ◽  
Latex Particles ◽  
The Third ◽  
Platelet Protein ◽  
Dose Dependent ◽  
Phagocytotic Activity

SummaryA three-fold increase of protein synthesis by human platelets during in vitro phagocytosis of polystyrene latex particles was detected. During the first two hours of incubation, the percentage of phagocytizing platelets and the number of latex particles per platelet increased; by the end of the third hour, the first parameter remained stable, while the number of latex particles per cell had decreased.Vincristine (20 μg/ml of cell suspension) inhibited platelet protein synthesis. This effect was both time- and dose-dependent. The drug also caused a decrease in the number of phagocytizing cells, as well as in their phagocytotic activity.

EFFECT OF ACTINOMYCIN D ON TSH-INDUCED STIMULATION OF THYROIDAL PROTEIN SYNTHESIS IN THE RAT

1974 ◽  
Vol 77 (1) ◽  
pp. 64-70 ◽  
Author(s):  
Gustav Wägar
Keyword(s):  
Protein Synthesis ◽  
Actinomycin D ◽  
The Other ◽  
Leucine Incorporation ◽  
Short Term ◽  
Other Hand ◽  
Thyroid Glands ◽  
Translational Level ◽  
Stimulation Of

ABSTRACT Whether the short-term regulation of thyroidal protein synthesis by TSH occurs at the transcriptional or the translational level was tested by measuring the effect of actinomycin D (act D) on the TSH-induced stimulation of L-14C-leucine incorporation into the thyroidal proteins of rats. TSH was injected 6 h before the rats were killed. The thyroid glands were then removed and incubated in vitro in the presence of L-14C-leucine for 2 h. The pronounced stimulation of leucine incorporation in the TSH-treated animals was depressed as compared with controls but still significant even when the animals had been pre-treated with 100 μg act D 24 and 7 h before sacrifice. On the other hand, act D strongly decreased incorporation of 3H-uridine into RNA. Short-term regulation of thyroidal protein synthesis by TSH appears to be partly but not wholly dependent on neosynthesis of RNA. Hence regulation may partly occur at the translation level of protein synthesis.

INHIBITION OF THYROGLOBULIN BIOSYNTHESIS AND DEGRADATION BY EXCESS IODIDE. SYNERGISM WITH LITHIUM

1976 ◽  
Vol 81 (2) ◽  
pp. 495-506 ◽  
Author(s):  
A. Radvila ◽  
R. Roost ◽  
H. Bürgi ◽  
H. Kohler ◽  
H. Studer
Keyword(s):  
Protein Synthesis ◽  
Thyroid Gland ◽  
Inhibitory Action ◽  
Inhibit Protein Synthesis ◽  
Thyrotrophic Hormone ◽  
Thyroid Glands ◽  
Pre Treatment ◽  
Excess Iodide ◽  
Kidney Liver

ABSTRACT Lithium and excess iodide inhibit the release of thyroid hormone from preformed stores. We thus tested the hypothesis that this was due to an inhibition of thyroglobulin breakdown. Rats were pre-treated with propylthiouracil (PTU) for 3 weeks in order to deplete their thyroids of thyroglobulin. While the PTU was continued, lithium chloride (0.25 mEq./100 g weight) or potassium iodide (3 mg per rat) were injected every 12 h for 3 days. Thereafter the thyroglobulin content in thyroid gland homogenates was measured. PTU pre-treatment lowered the thyroglobulin content from 4.21 to 0.22 mg/100 mg gland. Lithium caused a marked re-accumulation of thyroglobulin to 0.60 mg/100 mg within 3 days. While iodide alone had only a borderline effect, it markedly potentiated the action of lithium and a combination of the two drugs increased the thyroglobulin content to 1.04 mg/100 mg. Thyroxine was injected into similarly pre-treated animals to suppress secretion of thyrotrophic hormone. This markedly inhibited the proteolysis of thyroglobulin and 1.3 mg/100 mg gland accumulated after 3 days. Excess iodide, given in addition to thyroxine, decreased the amount of thyroglobulin accumulated to 0.75 mg/100 mg gland. To study whether this could be explained by an inhibitory action of iodide on thyroglobulin biosynthesis, thyroid glands from animals treated with excess iodide were incubated in vitro in the presence of 0.2 mm iodide for 3 h. Iodide decreased the incorporation of radioactive leucine into total thyroidal protein and into thyroglobulin by 25 and 35 % respectively. Iodide did not inhibit protein synthesis in the kidney, liver or muscle tissue. Thus, large doses of iodide selectively inhibit thyroglobulin biosynthesis.

Sign in / Sign up

Export Citation Format

Share Document