Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.26.9 (ribonuclease)
6,589 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The seco-steroid hormone 1,25-dihydroxyvitamin D3 is known to induce the expression of a calcium binding protein termed calbindin-D28K in a variety of target tissues. In order to comprehend the mechanism of induction we have cloned and sequenced the chicken calbindin-D28K gene. The gene spans some 18.5 kilobases (kb) of chromosomal DNA from the putative Cap site to the polyadenylation site of the 2.8 kb mRNA. It is split into 11 coding exons by 10 intervening sequences. The promoter region of this gene is markedly G + C-rich (60-80%) extending from -225 to +400. Within this region we find 70 CpG dinucleotides, four G-C boxes, and numerous known promoter regulatory signals. These putative regulatory signals include a TATA box (ATAAATA) at -30 and a CAT box (CCAAT) at -326. Ten additional variant CAT boxes are found in the upstream promoter region (-218 to -770) of this gene. Furthermore we have identified a glucocorticoid-like responsive element at -410 (TCTACACACTGTTCC) and this element overlaps a metal responsive element (TGCACTC) and a variant CAT box (CCAAAT) and juxtaposes an enhancer-like core element (AAATGGT) on its 3'-side. In addition, the calbindin-D28K promoter is composed of a variety of simple repeated sequences, some of which are components of putative regulatory signals. All splice junctions were found to conform to the GT-AG rule. A consensus sequence of the 5'-splice junction reads AG/GTAAG-TTATA. A consensus sequence of the 3'-splice site consists of two elements: a pyrimidine track (mainly T) followed by ACAG/G-T. A two-dimensional model of calbindin-D28K was constructed which projects the existence of 6 alpha-helix-loop-alpha-helix regions characteristic of calcium binding domains. The 3'-end of the gene consists of a single large (2039 base pair) uninterrupted exon, an organizational feature common to other members of the calcium binding protein gene family which include calmodulin, parvalbumin, Spec I, myosin light chains, etc. Another feature common to the gene family is the presence of the repeated sequence ATTT or TTTA located in the 3'-untranslated exons. These simple repeat sequences could be involved in regulating mRNA degradation by serving as a ribonuclease recognition signal.
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PMID:Molecular structure of the chicken vitamin D-induced calbindin-D28K gene reveals eleven exons, six Ca2+-binding domains, and numerous promoter regulatory elements. 296 15

Isolated pancreatic acini from streptozocin-induced diabetic rats were used to study the role of insulin on the synthesis of specific cellular proteins. When acini were incubated with 0-100 nM insulin for 2 h and then pulsed with [35S]methionine, a dose-dependent increase in [35S]methionine incorporation into total cellular proteins was observed. When acinar cell lysates were subjected to gel electrophoresis, 12 major newly synthesized protein bands were resolved. Insulin (100 nM) increased the incorporation of [35S]methionine into all bands but with significantly different rates, varying from 84 to 216% of control. Next, specific antibodies to amylase, trypsin, ribonuclease, myosin, and lactate dehydrogenase (LDH) were used to evaluate the biosynthesis of known proteins. Insulin stimulated labeled amino acid incorporation into amylase by 148% over control. Insulin stimulated the synthesis of trypsinogen to a similar degree, but ribonuclease synthesis showed a significantly smaller increase of 53% over control. Insulin stimulated myosin and LDH synthesis by 169 and 184%, respectively. A differential pattern of protein synthesis was also observed when acini were treated with two other stimulators of protein synthesis, cholecystokinin and hemin. Both of these stimulators had a reduced effect on ribonuclease synthesis compared with amylase and trypsinogen synthesis but failed to increase myosin synthesis. When the RNAs extracted from control acini and acini treated with 100 nM insulin were translated in vitro, the proteins synthesized were quantitatively similar. This study therefore indicates that insulin has translational effects on acinar protein synthesis, and these effects are nonparallel for various specific acinar cell proteins.
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PMID:Insulin and other stimulants have nonparallel translational effects on protein synthesis. 330 74

The first results are reported with a magnetic suspension instrument for determination of the viscosity and density concurrently on small volumes (0.2 ml) of protein solution. Reasonable agreement was obtained with literature values for the intrinsic viscosities and specific volumes (partial or isopotential) of serum albumin and ribonuclease in native solvents, and in 6 M guanidinium chloride with or without 2-mercaptoethanol. Turnip Yellow Mosaic virus and myosin were also studied, the results with the virus being related to hydration and structure data and those with myosin to the dissociative character of the protein. The possibility of using this approach to follow the time course of viscosity and density changes during reactions is shown.
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PMID:Simultaneous determination of viscosity and density of protein solutions by magnetic suspension. 450 95

In the companion paper (M. D. Peterson and M. S. Mooseker (1993). J. Cell Sci. 105, 445-460) we describe a method for modeling brush border assembly in the Caco-2BBe clones. In this study we have examined the molecular changes accompanying cell contact-induced brush border assembly. A subset of brush border proteins was tracked throughout brush border assembly by immunoblotting and by immunofluorescent localization using laser scanning confocal microscopy. Actin, fodrin, villin and presumptive unconventional myosin immunogens were distributed at the periphery of depolarized cells. All proteins partitioned primarily with the membrane fraction upon differential sedimentation of depolarized cell lysates; the fractionation patterns were comparable to those of confluent cells. After a monolayer had formed, each protein showed a redistribution to the apical domain in a discrete sequence. Actin and villin began to shift apically at 2 d, while fodrin and the unconventional myosin immunogens did not redistribute until 3 d. Enterocyte-like localization was observed by 5 d for all proteins. Sucrase-isomaltase was not reliably detectable until 9 d by immunofluorescence, after brush border assembly was complete. Quantitative immunoblot analysis of total cell extracts demonstrated an average 10-fold increase in villin levels, while fodrin levels appeared to remain unchanged. Three putative unconventional myosin immunogens of 140 kDa, 130 kDa, and 110 kDa have been detected previously in the C2BBe cells with a head-specific monoclonal antibody to avian brush border myosin I (M. D. Peterson and M. S. Mooseker (1992) J. Cell Sci. 102, 581-600). Each of these immunogens displayed distinct expression patterns during brush border assembly. The 140 kDa species decreased by half, while the 130 kDa immunogen(s) did not change in any consistent fashion. The 110 kDa protein, presumed to be human brush border myosin I, rose on average 8-fold. A ribonuclease protection assay was also performed using a probe for human brush border myosin I. Equal amounts of total RNA from depolarized and confluent cells were assayed; the level of protected product was approximately 9-fold greater in the confluent cells. The expression patterns of the brush border proteins, coupled with the correlation to the ultrastructural features during brush border assembly in C2BBe cells, show that differentiation of the C2BBe cells closely resembles the changes that occur during human fetal intestinal differentiation.
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PMID:An in vitro model for the analysis of intestinal brush border assembly. II. Changes in expression and localization of brush border proteins during cell contact-induced brush border assembly in Caco-2BBe cells. 840 77

Myosin heavy chain (MHC) expression was studied in rat soleus and tibialis anterior (TA) at the mRNA and protein levels following reinnervation 8 and 32 wk after sciatic nerve injury. A sciatic nerve crush or transection injury was produced in the midthigh region of adult female Sprague-Dawley rats. A ribonuclease protection assay was developed to measure four of the adult MHCs (I, IIa, IIx, IIb) in a single sample. MHC mRNA and protein were measured and compared in the same muscles. Eight and thirty-two weeks after a crush injury, the MHC mRNA profiles were similar to control with the exception of soleus MHC IIa and TA MHC IIb, which were significantly less than control at both time points. In contrast, reinnervation of the soleus following a sciatic nerve transection injury resulted in an MHC isoform shift characterized by increases in the relative amounts of fast myosin (IIa and IIx) and a decrease in slow myosin. As expected, significant changes first occurred at the mRNA level followed by changes in protein expression. Thirty-two weeks after transection injury and repair, the primary MHC mRNA isoform in the soleus was MHC IIx. Moreover, at 32 wk, MHC IIb mRNA was detected in 50% of the reinnervated soleus following a transection injury. Reinnervation of the TA following sciatic nerve transection led to replacement of the MHC IIb isoform with MHC IIx.
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PMID:Altered expression of myosin mRNA and protein in rat soleus and tibialis anterior following reinnervation. 899 4

The skeletal rat myoblast omega (RMo) cell line forms myotubes that exhibit spontaneous contractions under appropriate conditions in culture. We examined if the RMo cells would provide a model for studying atrophy and muscle contraction. To better understand how to obtain contractile cultures, we examined levels of contraction under different growing conditions. The proliferation medium and density of plating affected the subsequent proportion of spontaneously contracting myotubes. Using a ribonuclease protection assay, we found that exponentially growing RMo myoblasts contained no detectable myogenin or herculin mRNA, while differentiating myoblasts contained high levels of myogenin mRNA but no herculin mRNA. There was no increase in myogenin mRNA concentration in either primary chick or RMo myotubes whose contractions were inhibited by depolarizing concentrations of potassium (K+). Thus, altered myogenin mRNA concentrations are not involved in atrophy of chick myotubes. Depolarizing concentrations of potassium inhibited spontaneous contractions in both RMo cultures and primary chick myotube cultures. However, we found that the myosin concentration of 6-d-old contracting RMo cells fed medium plus AraC was 11 +/- 3 micrograms myosin/microgram DNA, not significantly different from 12 +/- 4 micrograms myosin/microgram DNA (n = 3), the myosin concentration of noncontracting RMo cells (treated with 12 mM K+ for 6 d). Resolving how RMo cells maintained their myosin content when contraction is inhibited may be important for understanding atrophy.
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PMID:Effect of atrophy and contractions on myogenin mRNA concentration in chick and rat myoblast omega muscle cells. 911 27

To investigate specific effects of androgens on whole body metabolism, we studied six healthy lean men (mean +/- SEM age, 23.2 +/- 0.5 yr) before and after gonadal steroid suppression with a GnRH analog (Lupron), given twice, 3 weeks apart. Primed infusions of [13C]leucine, indirect calorimetry, isokinetic dynamometry, growth factor measurements, and percutaneous muscle biopsies were performed at baseline (D1) and after 10 weeks of treatment (D2); each subject served as his own control. Testosterone concentrations were markedly suppressed after 10 weeks of treatment (D1, 535 +/- 141 ng/dL; D2, 31 +/- 9). Leucine's rate of appearance (index of proteolysis) was markedly suppressed after 10 weeks of hypogonadism (-13%; P = 0.01) as well as the nonoxidative leucine disposal, an index of whole body protein synthesis (-13%; P = 0.01) without any changes in plasma amino acid concentrations. All subjects studied after 10 weeks showed a decrease in fat-free mass, as measured by skinfold calipers and dual emission x-ray absortiometry scans (D1, 56.5 +/- 2.9 kg; D2, 54.4 +/- 2.5; P = 0.005), and an increase in percent fat mass (D1, 19.2 +/- 2.5%; D2, 22.2 +/- 2.5; P = 0.001). Rates of lipid oxidation decreased (-31%; P = 0.05) after treatment, with parallel changes in resting energy expenditure (-9%; P = 0.05). Mean and peak GH concentrations (measured every 10 min for 6 h) and GH production rates did not decrease after testosterone deficiency, with an actual increase in basal secretion (P < 0.02). Plasma insulin-like growth factor I (IGF-I) concentrations did not change significantly after 10 weeks of treatment (D1, 227 +/- 44 micrograms/L; D2, 291 +/- 60; P = 0.08). Isokinetic dynamometry of leg extensors at 60 degrees and 180 degrees/s was also decreased after 10 weeks of hypogonadism. Total ribonucleic acid (RNA) was isolated from muscle biopsy samples, and ribonuclease protection assays were performed using human complementary DNA clones for IGF-I, IGF-binding protein-4, myosin, and actin. Ten weeks after Lupron treatment, messenger RNA (mRNA) concentrations of IGF-I decreased significantly, whereas there was a trend toward higher IGF-binding protein-4 concentrations, with no change in myosin or actin mRNA concentrations. In conclusion, testosterone deficiency in young men is associated with a marked decrease in measures of whole body protein anabolism, decreased strength, decreased fat oxidation, and increased adiposity. These effects of testosterone deficiency are independent of changes in peripheral GH production and IGF-I concentrations, even though im IGF-I mRNA concentrations decrease. These data suggest a direct effect of androgens on whole body lipid and protein metabolism.
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PMID:Testosterone deficiency in young men: marked alterations in whole body protein kinetics, strength, and adiposity. 962 14

In the present study, the mechanisms and importance of the Fc portion of immunoglobulin in experimental giant cell myocarditis were examined. Giant cell myocarditis was induced in rats by immunization of porcine cardiac myosin. Human intact immunoglobulin (1 g. kg(-1). d(-1)) or F(ab')(2) fragments of human immunoglobulin (1 g. kg(-1). d(-1)) were administered intraperitoneally daily on days 1 to 21. Intact immunoglobulin administration significantly ameliorated myocarditis, but F(ab')(2) fragments did not. The ribonuclease protection assay revealed that therapy with intact immunoglobulin, but not F(ab')(2) fragments, suppressed the mRNA expressions of inflammatory and proinflammatory cytokines. Immunohistochemical analysis showed that therapy with intact immunoglobulin, but not F(ab')(2) fragments, suppressed dendritic cell (DC) expression during both the early and the subsequent fulminant phases. Moreover, the early treatment of intact immunoglobulin until the 11th day or 14th day, when the expression of DCs was completely suppressed, ameliorated myocarditis. However, the late treatment of intact immunoglobulin beginning on day 15, when the expression of DCs had already been completed, failed to ameliorate the condition. An in vitro study showed that intact immunoglobulin, but not F(ab')(2) fragments, suppressed the lipopolysaccharide-induced interleukin-1beta production associated with the downregulation of CD32 antigen (Fcgamma receptor II) expression. Thus, intact immunoglobulin therapy markedly suppressed myocarditis as a result of Fc receptor-mediated anti-inflammatory action, and the suppression of the disease was associated with the suppression of DCs, ie, the suppression of the initial antigen-priming process in experimental giant cell myocarditis.
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PMID:Fc receptor-mediated inhibitory effect of immunoglobulin therapy on autoimmune giant cell myocarditis: concomitant suppression of the expression of dendritic cells. 1155 42

The effects of various neutral salts on the temperature of the thermally-induced denaturation of the globular protein ribonuclease are described and compared with the effects of these salts on helix-coil transition temperatures in other macromolecules. These agents affect the stability of the native form of macromolecules as diverse as ribonuclease, collagen, DNA, and myosin in very similar ways; salts such as KSCN and CaCl(2) serve as very potent general structural destabilizers or denaturants, while salts such as (NH(4))(2)SO(4) and K(2)HPO(4) strongly stabilize the native conformation. The effectiveness of the neutral salts as ribonuclease destabilizers is compared with that of urea and the guanidinium salts.
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PMID:NEUTRAL SALTS: THE GENERALITY OF THEIR EFFECTS ON THE STABILITY OF MACROMOLECULAR CONFORMATIONS. 1416 81

Chromatography, on diethylaminoethyl cellulose, of leg muscle extracts from older chick embryos yields three myosin-containing fractions, whereas material from muscle extracts of 11-day embryos cannot be eluted under the same conditions. A major fraction having the adenosine triphosphotase activity characteristic of myosin can be eluted when 11-day-old embryo muscle extracts are given prior treatment with ribonuclease.
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PMID:CHROMATOGRAPHY OF RIBONUCLEASE-TREATED MYOSIN EXTRACTS FROM EARLY EMBRYONIC CHICK MUSCLE. 1419 55


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