Diurnal changes in actin mRNA levels and incorporation of35S-methionine into actin in the rat hypothalamus

1990 ◽  
Vol 10 (2) ◽  
pp. 207-216 ◽  
Author(s):  
Juan Iovanna ◽  
Nelson Dusetti ◽  
Ezequiel Calvo ◽  
Daniel P. Cardinali
Keyword(s):  
Diurnal Changes ◽  
Mrna Levels ◽  
Rat Hypothalamus ◽  
Actin Mrna

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.

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

Multihormonal Control of Pre-Pro-Somatostatin mRNA Levels in the Periventricular Nucleus of the Male and Female Rat Hypothalamus

1990 ◽  
Vol 52 (5) ◽  
pp. 527-536 ◽  
Author(s):  
Ricardo Zorrilla ◽  
Jacques Simard ◽  
Eric Rhéaume ◽  
Fernand Labrie ◽  
Georges Pelletier
Keyword(s):  
Mrna Levels ◽  
Female Rat ◽  
Male And Female ◽  
Rat Hypothalamus ◽  
Periventricular Nucleus

Influences of Hypothyroidism on TRH Concentrations and PreproTRH mRNA Levels in Rat Hypothalamus: A Simple and Reliable Method to Detect PreproTRH mRNA Level

1992 ◽  
Vol 55 (3) ◽  
pp. 317-320 ◽  
Author(s):  
Masanobu Yamada ◽  
Teturo Satoh ◽  
Tuyoshi Monden ◽  
Masami Murakami ◽  
Tokuji Iriuchijima ◽  
...  
Keyword(s):  
Reliable Method ◽  
Mrna Level ◽  
Mrna Levels ◽  
Rat Hypothalamus

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).

Dexamethasone Decreases Somatostatin mRNA Levels in the Periventricular Nucleus of the Rat Hypothalamus

1993 ◽  
Vol 58 (3) ◽  
pp. 325-331 ◽  
Author(s):  
Karen S.L. Lam ◽  
Gopesh Srivastava ◽  
Sau-Ping Tam ◽  
Lap-Ping Chung ◽  
Sau-Fong Chan ◽  
...  
Keyword(s):  
Mrna Levels ◽  
Rat Hypothalamus ◽  
Periventricular Nucleus
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