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PubMed1978

Changes in hepatic levels of tyrosine aminotransferase messenger RNA during induction by hydrocortisone.

Messenger RNA specific for tyrosine aminotransferase was quantitated by microinjection into oocytes of Xenopus laevis. The heterologously translated enzyme was identified by specific immunoprecipitation and found to be identical with authentic aminotransferase by several criteria. The level of functional message present in rat liver increases during hydrocortisone induction, and this increase is directly proportional to the increased rate of synthesis of the enzyme. Kinetic analysis of the changes in tyrosine aminotransferase mRNA levels during induction and withdrawal indicates that the steroid does not affect the stability of the message, which has a half-life of approximately 1.2 h. Hydrocortisone, therefore, acts to increase the rate of synthesis of the specific messenger by stimulating either its transcription or processing to functional mRNA.

Animals↗

PubMed2000

Differential regulation of calmodulin content and calmodulin messenger RNA levels by acute and repeated, intermittent amphetamine in dopaminergic terminal and midbrain areas.

Repeated doses of psychoactive drugs often produce adaptive responses that differ from the initial drug application and additional adaptive processes occur following cessation of the drug. The relationship between alterations in calmodulin protein and messenger RNA produced by an initial versus a repeated dose of amphetamine was examined, as well as changes following drug cessation. Calmodulin protein and messenger RNA of the three individual calmodulin genes were measured in rat dopaminergic cell body and terminal areas following acute or repeated amphetamine. Rats were either injected once with 2.5mg/kg amphetamine or saline and decapitated after 3h, or given 10 injections of amphetamine three to four days apart and decapitated 3h after the final injection. Calmodulin messenger RNA and protein were also measured three and seven days after ceasing drug treatment. Acute amphetamine increased calmodulin 1.7-fold in the striatum and threefold in the ventral mesencephalon, with corresponding elevations in calmodulin messenger RNAs. In response to the 10th dose of amphetamine, however, the degree of increase in calmodulin was diminished in the striatum and ablated in the ventral mesencephalon. Correspondingly, select species of calmodulin messenger RNA were decreased from control levels. In the frontal cortex or nucleus accumbens, calmodulin levels were basically unaltered by the first or 10th doses of amphetamine, but both calmodulin and its messenger RNA were altered with time upon cessation of the drug. Three days later, both calmodulin protein and messenger RNA were decreased in select brain areas. By seven days after the 10th injection, calmodulin content was altered compared to saline controls in all areas, but the change in messenger RNA no longer paralleled the change in protein.Our findings demonstrate that both calmodulin protein and select species of calmodulin messenger RNA are altered by acute amphetamine, but this effect is attenuated after repeated, intermittent amphetamine. There are further time-dependent changes after cessation of repeated amphetamine, which may reflect compensatory neuronal responses. The alterations in calmodulin content and synthesis could contribute to changes in patterns or duration of behaviors that occur upon cessation of repeated amphetamine.

Amphetamine↗

PubMed1974

A new transfer RNA fragment reaction: Tp psi pCpGp bound to a ribosome-messenger RNA complex induces the synthesis of guanosine tetra- and pentaphosphates.

The tetranucleotide TpPsipCpGp, when bound to Escherichia coli 50S ribosomal subunits, can replace intact tRNA in the stringent factor-directed synthesis of guanosine tetra- and pentaphosphates. The TpPsipCpGp-dependent fragment reaction has a strict requirement for the 50S and 30S ribosomal subunits and synthetic or natural messenger RNA.

Bacterial Proteins↗

PubMed1971

An adenylic acid-rich sequence in messenger RNA of HeLa cells and its possible relationship to reiterated sites in DNA.

Messenger RNA from HeLa cells contains, as part of the polynucleotide chain, RNase-resistant sequences that are labeled by adenosine but not by uridine. Heterogeneous nuclear RNA also contains adenylate-rich RNase-resistant regions, but in lower proportion than messenger RNA. Hybridization to DNA of (32)P-labeled messenger RNA reveals that some of the adenylate-rich region is included in the rapidly-hybridizing fraction.

Adenine Nucleotides↗

PubMed1975

Isolation and in vitro translation of human placental lactogen messenger RNA from human term placenta.

A messenger activity for HPL was identified in normal human term placentas. The mRNA was translated in rabbit reticulocyte cell-free system. The HPL synthesized was quantified by a specific immunoprecipitation and further identified by electrophoresis on sodium dodecyl sulfate polyacrylamide gel. The HPL synthesized in the reticulocyte lysate exhibited a molecular weight between 20,000 and 22,000 daltons similar to the active hormone. The messenger RNA activity for HPL corresponded to a sedimentation coefficient of 11-12 S. Furthermore the messenger activity for HPL was preferentially associated with membrane bound polyribosomes than with free polyribosomes.

Cell Membrane↗

PubMed1995

Heterogeneity of melanized neurons expressing neurotensin receptor messenger RNA in the substantia nigra and the nucleus paranigralis of control and Parkinson's disease brain.

We have recently cloned the neurotensin receptor from human substantia nigra. Using in situ hybridization techniques, with an 35S-labeled antisense RNA probe complementary to this receptor complementary DNA, we studied the expression of the human neurotensin receptor in the brain from control and Parkinson's disease subjects. We also performed an analogous study with rat brain. Neurotensin receptor messenger RNA was present in high levels in melanized neurons of the substantia nigra pars compacta and the nucleus paranigralis (the ventral tegmental area for rat brain). Background levels of signals for neurotensin receptor messenger RNA were detected in the nucleus ruber, the colliculus inferior and the striatal subdivisions (the nucleus caudatus, the putamen and the nucleus accumbens) of both human and rat brain. All these areas, except the nucleus ruber and the collicus inferior, contain very high to high levels of neurotensin receptor binding sites. Additionally, Parkinson's disease brains had markedly fewer melanized (possibly dopaminergic) neurons, as expected, and correspondingly very low or background levels of messenger RNA for neurotensin receptor. We have also demonstrated heterogeneity among the melanized cells expressing messenger RNA encoding the neurotensin receptor in the substantia nigra and the nucleus paranigralis of human brain. The neurons in the nucleus paranigralis had lower melanin pigmentation and higher expression of neurotensin receptor messenger RNA. In general, the expression of the messenger RNA within the highly and evenly melanized neurons was lower than that found in low or unevenly pigmented neurons. The neurons in the nucleus paranigralis had lower melanin pigmentation and higher expression of neurotensin receptor messenger RNA. The low pigmented neurons in the ventral tier of the substantia nigra had relatively high expression. On the other hand, highly and evenly melanized neurons in these regions of the brain had low expression of neurotensin receptor messenger RNA. Together with the previous binding data, it is suggested that not only in rat brain, but also in human brain, melanized (possibly dopaminergic) neurons in the substantia nigra and the nucleus paranigralis (ventral tegmental area of rat brain) synthesize neurotensin receptors and express them in their perikarya and the terminal regions. Additionally, the heterogeneity of the melanized neurons in human brain may play a role in the normal function of dopaminergic systems and probably in the etiology of some neurological and psychiatric disorders.

Aged↗

PubMed2002

Preoperative evidence of circulating tumor cells by means of reverse transcriptase-polymerase chain reaction for carcinoembryonic antigen messenger RNA is an independent predictor of survival in non-small cell lung cancer: a prospective study.

OBJECTIVE: We conducted a prospective study of 103 consecutive patients with non-small cell lung cancer who underwent a curative lobectomy to test whether circulating tumor cells detected in the peripheral blood by means of reverse transcriptase-polymerase chain reaction of carcinoembryonic antigen messenger RNA is a prognostic indicator independent of tumor stage in patients with non-small cell lung cancer. METHODS: We assayed for carcinoembryonic antigen messenger RNA by means of reverse transcriptase-polymerase chain reaction in peripheral blood taken at the time of diagnosis before an operation and again 2 to 3 weeks after an operation from patients with non-small cell lung cancer who underwent a curative lobectomy between March 1996 and April 1998. We analyzed the prognostic value of carcinoembryonic antigen messenger RNA expression in the patients with non-small cell lung cancer in a univariate and multivariate manner. RESULTS: Patients with carcinoembryonic antigen messenger RNA in the preoperative blood samples had a poor survival when compared with those without carcinoembryonic antigen messenger RNA. Of these patients, the worst survival was seen in those with carcinoembryonic antigen messenger RNA in the postoperative blood samples. The multivariate stepwise analysis selected the preoperative carcinoembryonic antigen messenger RNA expression (P =.0004; relative risk, 0.21) and the pathologic stage of disease (P =.0002; relative risk, 1.43) as the independent prognostic factors for survival. CONCLUSIONS: The molecular detection of carcinoembryonic antigen messenger RNA in the preoperative peripheral blood is an independent prognostic factor in patients with non-small cell lung cancer who undergo a curative operation.

Adult↗

PubMed1975

Properties of sea urchin embryo messenger RNA containing and lacking poly(A).

Various properties of nonhistone messenger RNA species containing poly(A), [+A]mRNA, and lacking poly(A), [-A]mRNA, are described: the rates of turnover of these mRNA classes are not significantly different, as indicated by their similar rates of entry into and decay from the cytoplasm; each mRNA class is essentially entirely transcribed from unique DNA sequences; the ratio of [+A] to [-A] nonhistone mRNA increases with increase in size of free polyribosome, although the average molecular weights of these mRNAs are similar in each polysomal size class. These results indicate that the [+A]mRNA species tend to be more fully loaded with ribosomes than the nonhistone [-A]mRNA species.

Animals↗

PubMed1984

Molecular model for messenger RNA splicing.

A molecular model is presented for a messenger RNA (mRNA) "splice region." The model requires cation coordination to reduce backbone-backbone electrostatic repulsion and it allows for every base residue on the pre-mRNA to be stacked in A-form helical geometry with a recognition element on the intron or exon (or both) sides of the splice junction. The two nucleotides involved in the initial steps of the cleavage-ligation mechanism must adopt a non-A-form geometry, which ideally positions reactive groups on the pre-mRNA for the necessary catalytic chemistry. The model is also consistent with available biochemical data on splicing reactions.

Adenosine Triphosphate↗

PubMed1973

Messenger RNA for hepatic tryptophan oxygenase: its partial purification, its translation in a heterologous cell-free system, and its control by glucocorticoid hormones.

Messenger RNA from rat liver was partially purified by chromatography on cellulose on the basis of its poly(A) content. Microgram amounts of this RNA stimulate protein synthesis manyfold in a heterologous cell-free system, derived from Krebs ascites cells supplemented with reticulocyte initiation factors. The messenger RNA directs the initiation, synthesis, and release of a product that was identified as complete subunits of hepatic tryptophan oxygenase (EC 1.13.1.12) by immunoprecipitation with monovalent antibodies prepared against homogeneous tryptophan oxygenase and subsequent sodium dodecyl sulfate-polyacrylamide electrophoresis of the solubilized immunoprecipitate. This may represent the first complete translation in a heterologous system of a mammalian messenger RNA coding for an enzyme protein. Analysis of the messenger RNA content of the liver after glucocorticoid administration demonstrates that the hormonally enhanced rate of synthesis of tryptophan oxygenase is accompanied by an increased quantity of its corresponding messenger RNA.

Animals↗

PubMed1989

Regulation of HSP70 synthesis by messenger RNA degradation.

When Drosophila cells are heat shocked, hsp70 messenger RNA (mRNA) is stable and is translated at high efficiencies. During recovery from heat shock, hsp70 synthesis is repressed and its messenger RNA (mRNA) is degraded in a highly regulated fashion. Dramatic differences in the timing of repression and degradation are observed after heat treatments of different severities. The 3' untranslated region (UTR) of the hsp70 mRNA was sufficient to transfer this regulated degradation to heterologous mRNAs. Altering the translational efficiency of the message or changing its natural translation-termination site did not alter its pattern of regulation, although in some cases it changed the absolute rate of degradation. We have previously shown that hsp70 mRNA is very unstable when it is expressed at normal growth temperatures (from a metallothionein promoter). We report here that the 3' untranslated region of the hsp70 mRNA is responsible for this instability as well. We postulate that a mechanism for degrading hsp70 mRNA pre-exists in Drosophila cells, that it is inactivated by heat shock and that it is the reactivation of this mechanism that is responsible for hsp70 repression during recovery. This degradation system may be the same as that used by other unstable mRNAs.

Animals↗

PubMed1999

Dark rearing blocks the developmental down-regulation of brain-derived neurotrophic factor messenger RNA expression in layers IV and V of the rat visual cortex.

In this study, we describe the distribution of brain-derived neurotrophic factor messenger RNA in the binocular primary visual cortex of the rat during postnatal development, starting at postnatal day (P) 13. High-resolution non-isotopic in situ hybridization combined with Nissl staining were used to quantify the number of cells expressing brain-derived neurotrophic factor messenger RNA. At P13, most of the cells express brain-derived neurotrophic factor messenger RNA. After eye opening (P14-P15), the relative number of brain-derived neurotrophic factor messenger RNA-positive cells decreases by a factor of two in layer IV, i.e. that receiving the visual input, and in layer V. To verify the hypothesis that light could trigger this decrease, pups were kept in complete darkness from birth. At P22, pups reared in the dark were killed and the visual cortex processed for in situ hybridization and northern blotting. The results obtained in dark-reared animals prove that light deprivation can: (i) decrease the general levels of brain-derived neurotrophic factor messenger RNA, and (ii) increase the relative number of brain-derived neurotrophic factor messenger RNA-positive cells in layers IV and V with respect to control rats. Exposure to light for five days after the period of darkness restored the number of brain-derived neurotrophic factor messenger RNA-positive cells. We conclude that the expression of brain-derived neurotrophic factor messenger RNA in the rat primary visual cortex is regulated during development and that this process is under the control of visual input.

Animals↗

PubMed1997

Distribution of the messenger RNA for the extracellularly regulated kinases 1, 2 and 3 in rat brain: effects of excitotoxic hippocampal lesions.

Neurofibrillary tangles in Alzheimer's disease are composed of hyperphosphorylated forms of the microtubule-associated protein tau. Based on biochemical criteria, several enzymes have emerged as potential tau protein kinases, including the extracellularly regulated kinases 1, 2 and 3. In situ hybridization was used to map the messenger RNA distribution of extracellularly regulated kinase 1, 2 and 3 in the adult rat brain and their response to excitotoxic hippocampal lesions was examined. Extracellularly regulated kinase 1 messenger RNA was uniformly expressed by glia, but was also present in the dentate gyrus and some other neuronal populations. Extracellularly regulated kinase 2 was exclusively neuronal and concentrated within the cortical laminae and the CA subfields of the hippocampal formation. Extracellularly regulated kinase 3 messenger RNA expression was similar to extracellularly regulated kinase 2 and was also present in neurons but the level of expression was lower. Extracellularly regulated kinases 2 and 3 messenger RNA expression was lost following excitotoxic injury, further supporting a neuronal localization. Extracellularly regulated kinase 1 messenger RNA expression appeared unaltered, suggesting a non-neuronal localization and lack of responsiveness to lesion at the level of transcription. By contrast, messenger RNA of sgk, a recently described serine/threonine kinase, was up-regulated by glial cells following excitotoxic injury. Based on their messenger RNA distribution, cellular localization and response to lesion, it is clear that each kinase may function differently in various signaling pathways. Extracellularly regulated kinase 2, however, is the only kinase with the proper messenger RNA distribution to contribute to neurofibrillary tangle formation in Alzheimer's disease.

Animals↗

PubMed1999

Dopamine-opiate interaction in the regulation of neostriatal and pallidal neuronal activity as assessed by opioid precursor peptides and glutamate decarboxylase messenger RNA expression.

Neostriatal GABAergic neurons projecting to the globus pallidus synthesize the opioid peptide enkephalin, while those innervating the substantia nigra pars reticulata and the entopeduncular nucleus synthesize dynorphin. The differential control exerted by dopamine on the activity of these two efferent projections concerns also the biosynthesis of these opioid peptides. Using in situ hybridization histochemistry, we investigated the role of opioid co-transmission in the regulation of neostriatal and pallidal activity. The expression of the messenger RNAs encoding glutamate decarboxylase-the biosynthetic enzyme of GABA-and the precursor peptides of enkephalin (preproenkephalin) and dynorphin (preprodynorphin) were measured in rats after a sustained blockade of opioid receptors by naloxone (s.c. implanted osmotic minipump, eight days, 3 mg/kg per h), and/or a subchronic blockade of D2 dopamine receptors by haloperidol (one week, 1.25 mg/kg s.c. twice a day). The density of mu opioid receptors in the neostriatum and globus pallidus was determined by autoradiography. Naloxone treatment resulted in a strong up-regulation of neostriatal and pallidal mu opioid receptors that was not affected by the concurrent administration of haloperidol. Haloperidol alone produced a moderate down-regulation of neostriatal and pallidal micro opioid receptors. Haloperidol strongly stimulated the expression of neostriatal preproenkephalin and preprodynorphin messenger RNAs. This effect was partially attenuated by naloxone, which alone produced moderate increases in preproenkephalin and preprodynorphin messenger RNA levels. In the neostriatum, naloxone did not affect either basal or haloperidol-stimulated glutamate decarboxylase messenger RNA expression. A strong reduction of glutamate decarboxylase messenger RNA expression was detected over pallidal neurons following either naloxone or haloperidol treatment, but concurrent administration of the two antagonists did not result in a further decrease. The amplitude of the variations of mu opioid receptor density and of preproenkephalin and preprodynorphin messenger RNA levels suggests that the regulation of neostriatal and pallidal micro opioid receptors is more susceptible to a direct opioid antagonism, while the biosynthesis of opioid peptides in the neostriatum is more dependent on the dopaminergic transmission. The down-regulation of mu opioid receptors following haloperidol represents probably an adaptive change to increased enkephalin biosynthesis and release. The haloperidol-induced increase in neostriatal preprodynorphin messenger RNA expression might result from an indirect, intermittent stimulation of neostriatal D1 receptors. The haloperidol-induced decrease of pallidal glutamate decarboxylase messenger RNA expression suggests, in keeping with the current functional model of the basal ganglia, that the activation of the striatopallidal projection produced by the interruption of neostriatal dopaminergic transmission reduces the GABAergic output of the globus pallidus. The reduction of pallidal glutamate decarboxylase messenger RNA expression following opioid receptor blockade indicates an indirect, excitatory influence of enkephalin upon globus pallidus neurons and, consequently, a functional antagonism between the two neuroactive substances (GABA and enkephalin) of the striatopallidal projection in the control of globus pallidus output. Through this antagonism enkephalin could partly attenuate the GABA-mediated effects of a dopaminergic denervation on pallidal neuronal activity.

Animals↗

PubMed2001

Corticotropin-releasing hormone messenger RNA distribution and stress-induced activation in the thalamus.

Corticotropin-releasing hormone plays a critical role in mediating the stress response. Brain circuits hypothesized to mediate stress include the thalamus, which plays a pivotal role in distributing sensory information to cortical and subcortical structures. In situ hybridization revealed neurons containing corticotropin-releasing hormone messenger RNA in the posterior thalamic nuclear group and the central medial nucleus of the thalamus, which interfaces with the ventral posteromedial nucleus (parvicellular part). These regions are of interest because they process somatosensory and visceral information. In the first experiment, the effect of acute stress on thalamic corticotropin-releasing hormone messenger RNA levels was assessed. Rats restrained for 1 h and killed 1 h later were found to have increased corticotropin-releasing hormone messenger RNA in the posterior thalamic nuclear group. The time course of these changes was examined in a second experiment in which rats were killed immediately or 3 h after restraint. While no changes occurred in the thalamus immediately after restraint, 3 h after restraint, increases in corticotropin-releasing hormone messenger RNA occurred in both the posterior thalamic nuclear group and the central medial-ventral posteromedial nucleus (parvicellular part) of the thalamus. A different pattern of activation was observed in the paraventricular nucleus of the hypothalamus with increased corticotropin-releasing hormone messenger RNA immediately after restraint, but not 1 or 3 h later. In addition to the stress-induced changes, a prominent decrease in baseline thalamic corticotropin-releasing hormone messenger RNA was observed from 1000 to 1300 h. These results show that the thalamus contains corticotropin-releasing hormone messenger RNA that increases after restraint stress, indicating a role for thalamic corticotropin-releasing hormone systems in the stress response. Stress-induced changes in thalamic corticotropin-releasing hormone messenger RNA expression appears to be regulated differently than that in the paraventricular nucleus of the hypothalamus, and may be influenced by diurnal mechanisms.

Animals↗

PubMed1973

Maternal histone messenger RNA: detection by molecular hybridization.

A competition-hybridization assay has been developed for the majority of sequences present in embryonically synthesized histone messenger RNA. The assay permits the first direct demonstration of specific "maternal" messengers in unfertilized sea-urchin eggs. The molecular size of histone messenger RNA stored in the egg appears to be the same as that of histone messenger RNA synthesized by the embryo. Maternal histone messenger RNA is found in the soluble phase of egg homogenates, in the form of ribonucleoprotein particles, unassociated with ribosomes.

Animals↗

PubMed1990

Two domains of yeast U6 small nuclear RNA required for both steps of nuclear precursor messenger RNA splicing.

U6 is one of the five small nuclear RNA's (snRNA's) that are required for splicing of nuclear precursor messenger RNA (pre-mRNA). The size and sequence of U6 RNA are conserved among organisms as diverse as yeast and man, and so it has been proposed that U6 RNA functions as a catalytic element in splicing. A procedure for in vitro reconstitution of functional yeast U6 small nuclear ribonucleoproteins (snRNP's) with synthetic U6 RNA was applied in an attempt to elucidate the function of yeast U6 RNA. Two domains in U6 RNA were identified, each of which is required for in vitro splicing. Single nucleotide substitutions in these two domains block splicing either at the first or the second step. Invariably, U6 RNA mutants that block the first step of splicing do not enter the spliceosome. On the other hand, those that block the second step of splicing form a spliceosome but block cleavage at the 3' splice site of the intron. In both domains, the positions of base changes that block the second step of splicing correspond exactly to the site of insertion of pre-mRNA-type introns into the U6 gene of two yeast species, providing a possible explanation for the mechanism of how these introns originated and adding further evidence for the proposed catalytic role of U6 RNA.

Base Sequence↗

PubMed1982

alpha A-crystallin messenger RNA of the mouse lens: more noncoding than coding sequences.

The 14S messenger RNA (1300 to 1500 nucleotides) for the alpha A chain of alpha-crystallin of the mammalian lens is nearly three times larger than required to code for the polypeptide that contains 173 amino acids. As a means of accounting for this anomaly, a complementary DNA clone for the mouse alpha A-crystallin messenger RNA was constructed in pBR322 and sequenced. Derivation of the protein sequence from the nucleic acid sequence showed that mouse alpha A-crystallin is similar to that of other organisms. The messenger RNA contains 536 nucleotides located on the 3' side of the coding region, excluding the polyadenylate stretch. This 3' sequence does not encode any other crystallin and has multiple termination codons in the three possible reading frames.

Amino Acid Sequence↗