Regional and developmental variations of GFAP and actin mRNA levels in the CNS of jimpy and shiverer mutant mice

1993 ◽  
Vol 4 (2) ◽  
pp. 89-96 ◽  
Author(s):  
H. Chen ◽  
F. Cabon ◽  
P. Sun ◽  
E. Parmantier ◽  
P. Dupouey ◽  
...  
Keyword(s):  
Mutant Mice ◽  
Mrna Levels ◽  
Actin Mrna ◽  
Developmental Variations

Regulation of tubulin and actin mRNA production in rat brain: expression of a new beta-tubulin mRNA with development

1983 ◽  
Vol 3 (8) ◽  
pp. 1333-1342
Author(s):  
J F Bond ◽  
S R Farmer
Keyword(s):  
Rat Brain ◽  
Morphological Changes ◽  
In Vitro Translation ◽  
Brain Maturation ◽  
Cdna Clones ◽  
Mrna Levels ◽  
Beta Tubulin ◽  
Mrna Species ◽  
Tubulin Mrna ◽  
Actin Mrna

The expression of alpha-tubulin, beta-tubulin, and actin mRNA during rat brain development has been examined by using specific cDNA clones and in vitro translation techniques. During brain maturation (0 to 80 days postnatal), these mRNA species undergo a significant decrease in abundance. The kinetics of this decrease varies between the cerebrum and the cerebellum. These mRNAs are most abundant in both tissues during week 1 postnatal, each representing 10 to 15% of total mRNA activity. Both alpha- and beta-tubulin mRNA content decreases by 90 to 95% in the cerebrum after day 11 postnatal, and 70 to 80% decreases in the cerebellum after day 16. Actin sequences also decrease but to a lesser extent in both tissues (i.e., 50%). These decreases coincide with the major developmental morphological changes (i.e., neurite extension) occurring during this postnatal period. These studies have also identified the appearance of a new 2.5-kilobase beta-tubulin mRNA species, which is more predominant in the cerebellar cytoplasm. The appearance of this form occurs at a time when the major 1.8-kilobase beta-tubulin mRNA levels are declining. The possibility that the tubulin multigene family is phenotypically expressed and then this expression responds to the morphological state of the nerve cells is discussed.

Flavin-Containing Monooxygenase mRNA Levels are Up-Regulated in ALS Brain Areas in SOD1-Mutant Mice

2010 ◽  
Vol 20 (2) ◽  
pp. 150-158 ◽  
Author(s):  
Stella Gagliardi ◽  
Paolo Ogliari ◽  
Annalisa Davin ◽  
Manuel Corato ◽  
Emanuela Cova ◽  
...  
Keyword(s):  
Mutant Mice ◽  
Mrna Levels ◽  
Brain Areas ◽  
Sod1 Mutant

Actin mRNA Levels and Actin Synthesis During the Encystation of Entamoeba invadens

1994 ◽  
Vol 41 (4) ◽  
pp. 360-365 ◽  
Author(s):  
REBECA MANNING-CELA ◽  
MARCO A. MERAZ ◽  
J. MANUEL HERNANDEZ ◽  
ISAURA MEZA
Keyword(s):  
Mrna Levels ◽  
Actin Mrna ◽  
Entamoeba Invadens

β-Adrenergic regulation of β-actin mRNA abundance in mouse parotid glands by a post-transcriptional mechanism

1991 ◽  
Vol 6 (1) ◽  
pp. 79-86 ◽  
Author(s):  
S. G. E. Roberts ◽  
G. H. Cope ◽  
C. J. McDonald
Keyword(s):  
Single Injection ◽  
Actin Gene ◽  
Mrna Levels ◽  
Parotid Glands ◽  
Adrenergic Agonist ◽  
Adrenergic Regulation ◽  
Subsequent Change ◽  
Actin Mrna ◽  
And Function ◽  
Actin Protein

ABSTRACT In the first 24 h after a single injection of the β-adrenergic agonist isoprenaline to mice, the level of β-actin mRNA in the parotid glands increased significantly above that observed in untreated mice. The increase was transient, reaching 11 times the normal level 18 h after treatment and declining thereafter. Repeated daily doses of isoprenaline did not result in any further increase in β-actin mRNA. Nuclear transcription experiments showed that there was no increase in the transcription rate of the β-actin gene 8 h after an injection of isoprenaline, although β-actin mRNA levels were increasing at this time. Immunoblotting revealed an increase in β-actin protein in parotid gland samples after isoprenaline treatment, although the increase was not to the same extent as the mRNA, perhaps indicating that degradation of β-actin had also increased. Using immunocytochemistry it was found that β-actin was located mainly in the apical cortex of the normal acinar cell. There was a significant decrease in cortical β-actin 24 h after isoprenaline treatment, suggesting that the β-actin was under the process of redistribution. From these data we propose that isoprenaline caused an increase in β-actin synthesis by a post-transcriptional mechanism and a redistribution of β-actin in preparation for the well-known subsequent change in morphology and function of the parotid glands.

scholarly journals Arterial smooth muscle cells in vivo: relationship between actin isoform expression and mitogenesis and their modulation by heparin.

1988 ◽  
Vol 107 (5) ◽  
pp. 1939-1945 ◽  
Author(s):  
A W Clowes ◽  
M M Clowes ◽  
O Kocher ◽  
P Ropraz ◽  
C Chaponnier ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Muscle Cells ◽  
In Vitro Translation ◽  
In Vivo Model ◽  
Growth Fraction ◽  
Mrna Levels ◽  
Actin Isoforms ◽  
Actin Mrna

Quiescent smooth muscle cells (SMC) in normal artery express a pattern of actin isoforms with alpha-smooth muscle (alpha SM) predominance that switches to beta predominance when the cells are proliferating. We have examined the relationship between the change in actin isoforms and entry of SMC into the growth cycle in an in vivo model of SMC proliferation (balloon injured rat carotid artery). alpha SM actin mRNA declined and cytoplasmic (beta + gamma) actin mRNAs increased in early G0/G1 (between 1 and 8 h after injury). In vivo synthesis and in vitro translation experiments demonstrated that functional alpha SM mRNA is decreased 24 h after injury and is proportional to the amount of mRNA present. At 36 h after injury, SMC prepared by enzymatic digestion were sorted into G0/G1 and S/G2 populations; only the SMC committed to proliferate (S/G2 fraction) showed a relative slight decrease in alpha SM actin and, more importantly, a large decrease in alpha SM actin mRNA. A switch from alpha SM predominance to beta predominance was present in the whole SMC population 5 d after injury. To determine if the change in actin isoforms was associated with proliferation, we inhibited SMC proliferation by approximately 80% with heparin, which has previously been shown to block SMC in late G0/G1 and to reduce the growth fraction. The switch in actin mRNAs and synthesis at 24 h was not prevented; however, alpha SM mRNA and protein were reinduced at 5 d in the heparin-treated animals compared to saline-treated controls. These results suggest that in vivo the synthesis of actin isoforms in arterial SMC depends on the mRNA levels and changes after injury in early G0/G1 whether or not the cells subsequently proliferate. The early changes in actin isoforms are not prevented by heparin, but they are eventually reversed if the SMC are kept in the resting state by the heparin treatment.

scholarly journals Regulation of actin mRNA levels and translation responds to changes in cell configuration.

1983 ◽  
Vol 3 (2) ◽  
pp. 182-189 ◽  
Author(s):  
S R Farmer ◽  
K M Wan ◽  
A Ben-Ze'ev ◽  
S Penman
Keyword(s):  
Protein Synthesis ◽  
Total Protein ◽  
Cdna Probe ◽  
Rapid Recovery ◽  
Mrna Levels ◽  
Culture Dish ◽  
Tissue Culture Dish ◽  
Cell Configuration ◽  
Surface Contact ◽  
Actin Mrna

The role of cell configuration in regulating cell metabolism has been studied, using a system in which cell shape and surface contact can easily be manipulated. The suspension of anchorage-dependent mouse fibroblasts in Methocel results in a coordinate decrease of DNA, RNA, and protein synthesis. These processes are restored upon reattachment of cells to a solid surface. This recovery process has two or more components: a rapid recovery of protein synthesis requiring only surface contact, and a slower restoration of nuclear events which is dependent upon extensive cell spreading (A. Ben-Ze'ev, S.R. Farmer, and S. Penman, Cell 21:365-372, 1980). In the present study, we examined 3T3 cells while in suspension culture and after attachment to a tissue culture dish surface to study cell configuration-dependent expression of specific cytoskeleton protein genes. The 3T3 line of fibroblasts used here shows these responses much more dramatically compared with 3T6 cells previously studied. We demonstrate that whereas total protein synthesis was strongly inhibited upon suspension, actin synthesis was preferentially inhibited, decreasing from 12% of total protein synthesis in control cells to 6% in suspended cells. This occurred apparently at the level of translation of actin mRNA, since the amount of actin mRNA sequences in the cytoplasm was unchanged. Reattachment initiated the rapid recovery of overall protein synthesis which was accompanied by a dramatic, preferential increase in actin synthesis reaching peak values of 20 to 25% of total protein synthesis 4 to 6 h later, but then declining to control values by 24 h. Translation in vitro and hybridization of mRNA to a cloned actin cDNA probe revealed that the induction of actin synthesis was due to increased levels of translatable mRNA sequences in the cytoplasm. These results imply a close relationship among cell cytoarchitecture, expression of a specific cytoskeletal protein gene, and growth control. The expression of the actin gene appears to be regulated at both the level of translation (during suspension) and mRNA production (during recovery).

Loss of Foxo3 Reduces Erythroblast Apoptosis and Enhances RBC Production in Beta-Thalassemic Mice

Blood ◽  
2015 ◽  
Vol 126 (23) ◽  
pp. 756-756 ◽  
Author(s):  
Raymond Liang ◽  
Genís Campreciós ◽  
Carolina L. Bigarella ◽  
Saghi Ghaffari
Keyword(s):  
Oxidative Stress ◽  
Bone Marrow ◽  
Double Mutant ◽  
Molecular Mechanisms ◽  
Mutant Mice ◽  
Mrna Levels ◽  
Wild Type ◽  
Erythroid Progenitors ◽  
Ineffective Erythropoiesis ◽  
Qrt Pcr

β-thalassemia arises as a result of mutations in the β-globin gene. As a consequence erythropoiesis, the process that insures the daily generation of billions of red blood cells (RBCs), becomes disrupted. Ineffective erythropoiesis is a major contributor to the β-thalassemic anemia and is partially due to aberrant apoptosis during late stages of erythroid maturation. Despite the importance of apoptosis, the underlying molecular mechanisms regulating this process in β-thalassemia erythroblasts are not fully elucidated. One potential mechanism involves the transcription factor Foxo3, which under specific contexts can act as a positive regulator of apoptosis, but is also an essential transcriptional regulator of terminal erythroblast maturation. Foxo3 has a range of outputs that it can execute from sustaining cellular integrity by mitigating oxidative stress to inducing apoptosis under conditions of overwhelming stress. Given these functions, we sought to determine if Foxo3 played a role in maintaining RBC maturation in β-thalassemic mice. To address this, we used Hbbth3/+ (th3/+) mice that display a phenotype similar to β-thalassemia intermedia, and produced double mutant Foxo3-/-/Th3/+ mice. The th3/+ mice display a mild erythroblast apoptotic phenotype. We hypothesized that loss of Foxo3 may exacerbate the β-thalassemic phenotype. On the contrary, we found that loss of Foxo3 in a β-thalassemic background improved RBC numbers and hemoglobin concentration (by 1g/dl, n=10 mice) in double mutant mice compared to th3/+ mice. Furthermore, double mutant mice had a statistically significant lower frequency of apoptosis (2 fold less) during bone marrow erythroblast maturation as measured by flow cytometry analysis of annexin V-binding and 7AAD staining in distinct erythroblast stages resolved by TER119, CD44 and cell size (n=3 mice per genotype). We predicted that high levels of oxidative stress may prematurely activate FOXO3 during erythroblast maturation in β-thalassemic mice. In turn, activated FOXO3 may potentially promote apoptosis in these cells. To evaluate this, we examined FOXO3 levels by qRT-PCR and immunofluorescence in FACS sorted populations of erythroblasts (TER119+,CD44,FSC) or erythroid progenitors (TER119-,c-KIT+,CD71HI) acquired from bone marrow of at least 3 mice per genotype. Our data show increased mRNA levels of Foxo3 in early erythroblasts, corresponding to increased FOXO3 protein expression in erythroid progenitors from β-thalassemic mice relative to wild-type mice. We also examined the activation status of p53, as it is also a major regulator of apoptosis that can be triggered by oxidative stress. Nuclear p53 levels were greater in β-thalassemic as compared to wild-type erythroid progenitors based on immunofluorescence analysis of sorted cells from bone marrow of 3 mice per genotype. These results suggest a higher level of active p53 in β-thalassemic erythroid progenitors. Our results provide evidence that FOXO3, a factor normally critical for erythroblast maturation, may cooperate with aberrantly active p53 to induce apoptosis in β-thalassemic erythroblasts. In support of this, downstream p53 targets including Gadd45a and p21 that are also Foxo3 targets were significantly upregulated in β-thalassemic erythroblasts relative to wild-type erythroblasts as determined by qRT-PCR of cDNA produced from 3 mice per genotype. To more closely examine the mechanism of decreased apoptosis in double mutant Foxo3-/-/Th3/+ erythroblasts, we compared the expression of multiple genes involved in apoptosis by qRT-PCR of sorted erythroblast populations from at least 3 mice per genotype. We found multiple pro-apoptotic genes including, Cycs, Tnfsf10, Puma, and Bim expressed at significantly lower levels at various erythroblast stages in double mutant compared to β-thalassemic erythroblasts. Together, our data suggests Foxo3 becomes inappropriately and prematurely activated in erythroid progenitors and early erythroblasts in the context of β-thalassemia and cooperates with p53 to promote apoptosis. These findings raise the possibility that cooperation of Foxo3 and p53 in β-thalassemic erythroblasts might contribute to the ineffective erythropoiesis of β-thalassemic mice. They also suggest the possibility that as a homeostatic maintaining factor, Foxo3 behaves differently in the context of disease. Disclosures No relevant conflicts of interest to declare.

Alpha-skeletal actin messenger RNA increases in acute right ventricular hypertrophy

1990 ◽  
Vol 258 (4) ◽  
pp. L173-L178 ◽  
Author(s):  
P. R. Bakerman ◽  
K. R. Stenmark ◽  
J. H. Fisher
Keyword(s):  
Pulmonary Hypertension ◽  
Right Ventricular ◽  
Hypobaric Hypoxia ◽  
Ventricular Hypertrophy ◽  
Right Ventricular Hypertrophy ◽  
Hypoxic Exposure ◽  
Mrna Levels ◽  
Severe Pulmonary Hypertension ◽  
Cardiac Actin ◽  
Actin Mrna

Newborn calves exposed to hypobaric hypoxia develop severe pulmonary hypertension. Right ventricular hypertrophy and failure occur as a consequence of the increased pressure load. Alterations in right ventricular myocyte performance or differentiation could be reflected by the changes in the expression of contractile protein genes. We studied expression of contractile actin isotypes by measuring mRNA levels in total cellular RNA purified from right (RV) and left ventricles (LV) of calves with severe pulmonary hypertension after a 2-wk exposure to hypobaric hypoxia and age-matched controls. alpha-Skeletal actin mRNA was increased greater than 10-fold in the RV of hypertensive animals, whereas alpha-cardiac actin mRNA did not appear to change. alpha-Skeletal actin mRNA and alpha-cardiac actin mRNA did not increase in the LV of any of the hypoxic animals. After a 2-wk hypoxic exposure, calves were removed from the chamber. Two days later, RV alpha-skeletal actin mRNA decreased dramatically but was apparently elevated above that of an age-matched control. Thirty days after hypoxia, there appeared to be a persistent increase in RV alpha-skeletal actin mRNA. Although the physiological significance of these changes are unknown, an alteration in the RV myocyte phenotype has occurred.

scholarly journals Altered beta-actin gene expression in phorbol myristate acetate-treated chondrocytes and fibroblasts.

1985 ◽  
Vol 5 (6) ◽  
pp. 1425-1433 ◽  
Author(s):  
L C Gerstenfeld ◽  
M H Finer ◽  
H Boedtker
Keyword(s):  
Steady State ◽  
Type I Collagen ◽  
Type Ii Collagen ◽  
Tumor Promoter ◽  
Type I ◽  
Mrna Levels ◽  
Collagen Mrna ◽  
Beta Actin ◽  
Steady State Levels ◽  
Actin Mrna

Phorbol-12-myristate-13-acetate (PMA), a potent tumor promoter, was shown to have opposite effects on the cellular morphology and steady-state levels of beta-actin mRNA in embryonic chicken muscle fibroblasts and sternal chondrocytes. When fibroblasts were treated with PMA, they formed foci of densely packed cells, ceased to adhere to culture plates, and had significantly reduced levels of beta-actin mRNA and protein. Conversely, when treated with PMA, floating chondrocytes attached to culture dishes, spread out, and began to accumulate high levels of beta-actin mRNA and proteins. In the sternal chondrocytes the stimulation of the beta-actin mRNA production was accompanied by increased steady-state levels of fibronectin mRNAs and protein. These alterations were concomitant with a fivefold reduction in type II collagen mRNA and a cessation in its protein production. After fibronectin and actin mRNAs and proteins reached their maximal levels, type I collagen mRNA and protein synthesis were turned on. Removal of PMA resulted in reduced beta-actin mRNA levels in chondrocytes and in a further alteration in the cell morphology. These observed correlations between changes in cell adhesion and morphology and beta-actin expression suggest that the effect of PMA on cell shape and adhesion may result in changes in the microfilament organization of the cytoskeleton which ultimately lead to changes in the extracellular matrix produced by the cells.

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