Evaluation of Intracellular Level of Thiols

2021 ◽  
pp. 127-131
Author(s):  
Pauline Brousseau ◽  
Yves Payette ◽  
Helen Tryphonas ◽  
Barry Blakley ◽  
Herman Boermans ◽  
...  
Keyword(s):  
Intracellular Level

Abnormal Intracellular Level of Bax in CD3 + Cells from Untreated B-Cell Chronic Lymphocytic Leukemia Patients

2006 ◽  
Vol 12 (4) ◽  
pp. 187-192
Author(s):  
F. Scamardella ◽  
M. Maconi ◽  
L. Albertazzi ◽  
B. Gamberi ◽  
L. Gugliotta ◽  
...  
Keyword(s):  
Chronic Lymphocytic Leukemia ◽  
B Cell ◽  
Lymphocytic Leukemia ◽  
Intracellular Level ◽  
Cell Chronic Lymphocytic Leukemia

scholarly journals Role of Small Envelope Protein in Sustaining the Intracellular and Extracellular Levels of Hepatitis B Virus Large and Middle Envelope Proteins

Viruses ◽  
2021 ◽  
Vol 13 (4) ◽  
pp. 613
Author(s):  
Jing Zhang ◽  
Yongxiang Wang ◽  
Shuwen Fu ◽  
Quan Yuan ◽  
Qianru Wang ◽  
...  
Keyword(s):  
Envelope Proteins ◽  
Full Length ◽  
M Protein ◽  
Intracellular Level ◽  
S Protein ◽  
L Protein ◽  
M Proteins ◽  
B Virus ◽  
Subviral Particle ◽  
Genotype A

Hepatitis B virus (HBV) expresses co-terminal large (L), middle (M), and small (S) envelope proteins. S protein drives virion and subviral particle secretion, whereas L protein inhibits subviral particle secretion but coordinates virion morphogenesis. We previously found that preventing S protein expression from a subgenomic construct eliminated M protein. The present study further examined impact of S protein on L and M proteins. Mutations were introduced to subgenomic construct of genotype A or 1.1mer replication construct of genotype A or D, and viral proteins were analyzed from transfected Huh7 cells. Mutating S gene ATG to prevent expression of full-length S protein eliminated M protein, reduced intracellular level of L protein despite its blocked secretion, and generated a truncated S protein through translation initiation from a downstream ATG. Truncated S protein was secretion deficient and could inhibit secretion of L, M, S proteins from wild-type constructs. Providing full-length S protein in trans rescued L protein secretion and increased its intracellular level from mutants of lost S gene ATG. Lost core protein expression reduced all the three envelope proteins. In conclusion, full-length S protein could sustain intracellular and extracellular L and M proteins, while truncated S protein could block subviral particle secretion.

Extracellular regulation of BMP signaling: welcome to the matrix

2017 ◽  
Vol 45 (1) ◽  
pp. 173-181 ◽  
Author(s):  
Georg Sedlmeier ◽  
Jonathan P. Sleeman
Keyword(s):  
Extracellular Matrix ◽  
Physical Properties ◽  
Bone Morphogenetic Protein ◽  
Bmp Signaling ◽  
Intracellular Level ◽  
Morphogenetic Protein ◽  
The Matrix ◽  
Mechanical Barrier

Given its importance in development and homeostasis, bone morphogenetic protein (BMP) signaling is tightly regulated at the extra- and intracellular level. The extracellular matrix (ECM) was initially thought to act as a passive mechanical barrier that sequesters BMPs. However, a new understanding about how the ECM plays an instructive role in regulating BMP signaling is emerging. In this mini-review, we discuss various ways in which the biochemical and physical properties of the ECM regulate BMP signaling.

Contribution from local conversion of thyroxine to 3,5,3'-triiodothyronine to intracellular 3,5,3'-triiodothyronine in several organs in hypothyroid rats at isotope equilibrium

1982 ◽  
Vol 101 (3) ◽  
pp. 386-396 ◽  
Author(s):  
J. van Doom ◽  
F. Roelfsema ◽  
D. van der Heide
Keyword(s):  
Cerebral Cortex ◽  
Pituitary Gland ◽  
Subcellular Fractions ◽  
Thigh Muscle ◽  
Intracellular Level ◽  
Carrier Free ◽  
Tissue Homogenates ◽  
Isotope Equilibrium ◽  
Layer Chromatography ◽  
The Brain

Abstract. The intracellular conversion of T4 to T3 was investigated in various tissues of hypothyroid rats after continuous iv infusion of radiolabelled T3 and T4. Two groups of 4 thyroidectomized rats were infused with carrier-free 125I-labelled T4 as well as 131I-labelled T3 until isotope equilibrium was achieved. Plasma, various tissue homogenates (liver, kidney, pituitary, thigh muscle, cerebral cortex and cerebellum) and subcellular fractions (nuclei, mitochondria, microsomes, cytoplasm) from liver, kidney and the pituitary gland were extracted for thin layer chromatography. The [125I]T3/[131I]T3 ratios were determined and the extra contribution of [125I]T3 derived from local conversion of [125I]T4 to the total [125I]T3 was calculated in percent. In addition to the [125I]T3 derived from plasma, [125I]T3 derived from locally converted [125I]T4 was present in all tissues investigated. There was substantially more, although in varying quantities, in the cerebral cortex (79 ± 2%), the cerebellum (68 ± 4%) and the pituitary gland (53 ± 1%) than in the liver (10 ± 6%), the kidney (11 ± 5%) and thigh muscle (17 ± 6%); in the latter tissues most of the 125I-labelled T3 is derived directly from plasma. These results indicate that in the brain of severe hypothyroid rats there is pronounced conversion of T4 to T3 and effective binding of the T3 produced whereas the T3 in the liver, kidney, and muscle is predominantly derived from plasma. At the intracellular level, within the investigated tissues, the locally formed T3 was distributed equally over the subcellular fractions.

Effects of adenosine 5′-monophosphate and adenosine 3′,5′-cyclic monophosphate on l cells

1975 ◽  
Vol 19 (2) ◽  
pp. 305-313
Author(s):  
J. Taylor-Papadimitriou ◽  
T. Karemfyllis ◽  
A. Eukarpidou ◽  
G. Karamanlidou
Keyword(s):  
Cyclic Amp ◽  
Adenine Nucleotides ◽  
Inhibitory Effect ◽  
S Phase ◽  
Breakdown Product ◽  
Intracellular Level ◽  
Effective Inhibitor ◽  
Growth Inhibitory Effect ◽  
L Cells ◽  
Growth Inhibitory

The adenine nucleotides, 5′-AMP and 3′,5′-cyclic AMP block L cells in the S-phase of the cell cycle. The intracellular level of cyclic AMP is reduced after incubation of cells with 5′-AMP, and rates of uridine transport are increased after incubation with either 5′-AMP or cyclic AMP. On the contrary, cyclic AMP levels are increased and uridine transport decreased in cells treated with an inhibitor of the cyclic AMP phosphodiesterase. This inhibitor partially reverses the growth-inhibitory effect of cyclic AMP, indicating that a breakdown product is the effective inhibitor of growth. The inhibition of cell growth induced by the adenine nucleotides is prevented by uridine, suggesting that the block in S is due to a lack of availability of pyrimidines.

scholarly journals The Elevation of Adenosine-Triphosphate Levels in Human Erythrocytes

Blood ◽  
1973 ◽  
Vol 42 (4) ◽  
pp. 637-648 ◽  
Author(s):  
Elizabeth M. Warrendorf ◽  
David Rubinstein
Keyword(s):  
Inorganic Phosphate ◽  
Adenine Nucleotides ◽  
Lactic Dehydrogenase ◽  
Human Erythrocytes ◽  
Intracellular Level ◽  
Normal Cells ◽  
Atp Level ◽  
Atp Formation ◽  
Intracellular Phosphate ◽  
Glucose 6 Phosphate Dehydrogenase

Abstract It has previously been possible to double the level of ATP in human erythrocytes by incubation of the cells at 37° for 10 hr with glucose and adenine. The present study describes a further increase in the ATP level and some of the possible mechanisms involved. Addition of 5 mM pyruvate to a medium containing 32 mM inorganic phosphate, glucose, and adenine elevated the level of ATP threefold during a 10-hr incubation. Pyruvate could be replaced by inosine but the presence of both limited the elevation of ATP to twice that of fresh cells. This limitation may be overcome by the use of 96 mM phosphate in the incubation medium, in which case the intracellular level of ATP is tripled within 2 hr. The conditions which limit the accumulation of ATP are associated with low intracellular phosphate concentrations and the accumulation of organic phosphates, especially, in the presence of inosine, 2,3-diphosphoglycerate. Utilizing 14C-glucose labeled in carbons 1, 2, or 6, it has been shown that when ATP is being rapidly elevated, the pentose moiety of the adenine nucleotides is mainly supplied (about 80%) by oxidation of carbon 1 of glucose, catalyzed by the dehydrogenases of the hexosemonophosphate shunt. In the presence of pyruvate this activity is doubled. Pyruvate reoxidizes NADPH formed by this pathway, since lactic dehydrogenase has some specificity towards the NADPH. The involvement of the dehydrogenases of the hexosemonophosphate shunt is illustrated by the use of erythrocytes deficient in glucose-6-phosphate dehydrogenase. Incubation of these cells for 5 hr with glucose and adenine results in only a slight increase in ATP formation, and pyruvate has no additional effect. Addition of inosine, however, leads to the same increment in ATP levels seen in normal cells. The ATP and 2,3-diphosphoglycerate levels in 6-wk preserved blood can also be increased to three times that of fresh cells by incubation with glucose, adenine, pyruvate, and inosine in a medium high in inorganic phosphate.

Role of acetylcholine in induction of repetitive activity in human atrial fibers

1989 ◽  
Vol 256 (1) ◽  
pp. H74-H84
Author(s):  
Z. Y. Hou ◽  
C. I. Lin ◽  
M. Vassalle ◽  
B. N. Chiang ◽  
K. K. Cheng
Keyword(s):  
Action Potential ◽  
Muscarinic Receptor ◽  
Action Potentials ◽  
Oscillatory Potentials ◽  
Contractile Force ◽  
Intracellular Level ◽  
Transmembrane Potentials ◽  
Rebound Increase

The actions of acetylcholine and its interactions with epinephrine were studied in human atrial tissues by recording transmembrane potentials and contractile force. Acetylcholine (0.55-5.5 microM) reduced force, shortened the duration and shifted to more negative values the plateau of action potentials, abolished phase 4 depolarization, and suppressed the activity of spontaneous fibers. During the recovery, often there was a rebound increase in some parameters of the action potential and in force. Epinephrine (0.3-2.8 microM) induced oscillatory potentials and aftercontractions and acetylcholine abolished them. However, during the washout of acetylcholine in the presence of epinephrine, the oscillatory potentials and aftercontractions were larger than before acetylcholine, and repetitive activity was often induced. The inhibitory and excitatory effects of acetylcholine were mimicked by methacholine (5.1 microM) and abolished by atropine (1.5 microM). The postacetylcholine rebound was also potentiated by theophylline (0.6-2 mM) but was not blocked by propranolol (1-3.4 microM), prazosin (1 microM), and diltiazem (0.1 microM). It is concluded that in human atrial fibers acetylcholine has inhibitory as well as excitatory effects that are exaggerated in the presence of epinephrine and are mediated by the activation of the muscarinic receptor. The interaction between acetylcholine and epinephrine involves an antagonism at an intracellular level.

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