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:3.1.27.1 (RNase)
16,360 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The amino acid sequence of golden hamster pancreatic ribonuclease was determined by analysis of tryptic, chymotryptic, thermolytic, and CNBr peptides and by automatic sequence analysis of the intact protein. Like all RNases with an Asn-Met-Thr sequence at positions 34-36, hamster RNase is glycosylated at position 34 with a complex-type carbohydrated chain. Val-17, Ala-18, His-55, His-76 and Ala-90 have never been observed in other pancreatic RNases. Ala-90 replaces Ser-90, which had been invariant in all mammalian RNases studied so far. The amino acid sequence of hamster RNase differs at 15 positions from that of another Cricetidae rodent, the muskrat. The similarity between both ribonucleases was used to confirm a few less certain parts of the muskrat RNase sequence. The replacement rate of the RNases of the Cricetidae appeared to be higher than the average rate in the mammals, but much lower than the rate in another myomorph family, the Muridae (mouse and rat). Possibly, in many respects, the Cricetidae underwent less evolutionary change in recent times than the evolutionarily highly successful Muridae.
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PMID:The amino acid sequence of hamster pancreatic ribonuclease. 51 28

Oligonucleotide products of complete pancreatic or T1 RNase digestion or partial T1 RNase digestion of HeLa cell (human) and MPC-11 cell (mouse) 5.8S rRNA are identical with those obtained from Novikoff hepatoma (rat) 5.8S rRNA except for minor differences at the termini. pCp is the only major 5' terminus of both human and mouse RNAs; both pGp and pCp 5' termini were found in rat 5.8S RNA. Furthermore, HeLa cells contain C-U-U at the 3' end rather than the C-U terminus of mouse and rat. The results indicate that the nucleotide sequence has been highly conserved during the evolution of mammals and suggest that, as reported for 5S rRNA, this sequence is essentially constant throughout the Mammalia.
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PMID:Sequence homologies in mammalian 5.8S ribosomal RNA. 125 8

We describe here a protocol developed to detect specific mRNAs by in situ hybridization using tissue sections that were not treated to inactivate RNase and were stored in cryoprotectant solution for several years. Brains from rats, monkeys and humans were sectioned at 50 microns and stored free floating in an ethylene glycol based cryoprotective solution at -20 degrees C. Rat brain sections were kept in cryoprotective solution for 3 days, 1 month and 2 months. Control sections were cut and mounted immediately on gelatin-coated slides and stored at -80 degrees C. Monkey brain sections were stored in cryoprotective solution for up to 5 years. Human sections were tested after storage for one year. Oligonucleotide probes that were complementary to human preproenkephalin mRNA (amino acid sequences 130-145), rat preproenkephalin mRNA (sequences 388-435) and rat tyrosine hydroxylase mRNA (sequences 1441-1488) were labeled with 35S-dATP and terminal deoxynucleotidyl transferase. To prevent possible RNase contamination from mounting the tissue sections onto gelatin coated slides, the in situ hybridization was performed in sterile culture dishes. Following each step, solutions were aspirated out of the dish. The amount of probe necessary for each section was 45 microliters (rat), 450 microliters (monkey), and 350 microliters (human). Using this protocol, the detection of specific mRNAs in rat brain sections was more specific with less non-specific background as compared to control sections that were processed after they were mounted onto gelatin-coated sides. Excellent resolution was also obtained from monkey brain sections that were stored in cryoprotectant for up to 31 months and in human brain sections stored for 12 months.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:In situ hybridization histochemistry: a new method for processing material stored for several years. 135 96

The effects of hypophysectomy and hormonal replacement therapy on GH receptor (GH-R) gene expression was studied in rat adipose tissue with a cRNA probe corresponding to the amino-terminal of the hepatic GH-R. Male Sprague-Dawley rats, 50-65 days of age, were used. In all fat depots tested (epididymal, retroperitoneal, and sc), two transcripts with an estimated size of 4.0 and 1.2 kilobases (kb), respectively, were detected. An intermediate-size transcript (2.6 kb) was sometimes observed. Also, isolated adipocytes and adipocyte precursor cells from the epididymal fat pad expressed these GH-R transcripts. The pituitary dependance of GH-R gene expression was analyzed in epididymal fat. Hypophysectomies were performed at 50 days of age, and the rats were then given replacement therapy with L-T4 (10 micrograms/kg.day) and hydrocortisone (400 micrograms/kg.day). Hypophysectomy decreased the abundance of both the 4.0 and the 1.2-kb transcripts, an effect that in part was restored by GH treatment. A solution hybridization RNase protection assay was then used to further characterize the effect of GH treatment of hypophysectomized rats on GH-R gene expression. A single injection of human GH (100 micrograms/rat) increased GH-R mRNA levels within 1 h, and maximal levels were reached between 3-12 h after the injection. The increase in GH-R mRNA levels was dose dependent and was observed also after prolonged treatment (1 or 5 mg/kg.day for 6 days) with bovine GH. These results confirm that GH-R mRNAs are present in rat adipose tissue from different fat depots. GH-R transcripts of the same estimated size were detected in isolated adipocytes and adipocyte precursor cells. Furthermore, the results show that there is a rapid and GH-dependent regulation of GH-R mRNA levels in adipose tissue.
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PMID:Expression and regulation of growth hormone (GH) receptor messenger ribonucleic acid (mRNA) in rat adipose tissue, adipocytes, and adipocyte precursor cells: GH regulation of GH receptor mRNA. 171 28

In the kidney, 11 beta-dehydrogenase (11 beta-DH) converts the active steroid cortisol to inactive cortisone (corticosterone to 11-dehydrocorticosterone in the rat). In man, congenital and acquired deficiency of 11 beta-dehydrogenase are rare causes of hypertension in which cortisol acts as a potent mineralocorticoid. Observations from these clinical studies indicate that 11 beta-DH conveys specificity for the mineralocorticoid receptor in distal tubules and collecting ducts. However, while some studies do indicate 11 beta-DH activity in rat distal tubules and collecting ducts, immunohistochemical studies localize 11 beta-DH only to proximal tubules. to resolve this dilemma, we have performed in situ hybridization localization of 11 beta-DH mRNA in rat kidney tissue using 35S-labeled sense and antisense cRNA probes to rat 11 beta-DH. In contrast to our immunohistochemical studies in which 11 beta-DH protein was localized predominantly to proximal tubules in the inner cortex, 11 beta-DH mRNA was expressed in tubules in both the inner and outer cortex, most probably proximal and distal tubules, and in collecting ducts extending across the corticomedullary junction to the papillary tip. Weak hybridization was also seen in glomeruli, but no hybridization to the sense 11 beta-DH cRNA or to sections pretreated with RNase-A was observed. We conclude that renal 11 beta-DH is suitably located to prevent access of glucocorticoid to the MR in an autocrine and not a paracrine fashion. 11 beta-DH in proximal tubules may protect the glucocorticoid receptor.
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PMID:Localization of renal 11 beta-dehydrogenase by in situ hybridization: autocrine not paracrine protector of the mineralocorticoid receptor. 184 10

We, and others have recently demonstrated the ovary to be a site of interleukin-1 (IL-1) reception and action. Since IL-1 is an established mediator of inflammation and since ovulation may constitute an inflammatory-like reaction, consideration was given to the possibility that IL-1 may play an intermediary role in the ovulatory process. To begin to evaluate the above hypothesis, we have set out to evaluate rat ovarian IL-1 beta gene expression, to determine its cellular localization, and to study its modulation by key endocrine and autocrine regulatory signals. To this end, use was made of a solution hybridization/RNase protection assay in which rat ovarian total RNA (20 micrograms) was hybridized with a [32P]-labeled 272 base rat IL-1 beta antisense riboprobe. To assess rat ovarian IL-1 beta gene expression under in vivo circumstances, use was made of an established experimental model capable of simulating naturally-occurring follicular maturation, ovulation, and corpus luteum formation. Specifically, a single subcutaneous injection of PMSG (15IU/rat) was followed (48h) later by an ovulatory dose (15IU) of human chorionic gonadotropin (hCG). A faint protected fragment 222 bases long corresponding to the IL-1 beta message was detectable in whole ovarian material prior to gonadotropic stimulation. Treatment with PMSG for 48h resulted in a modest, albeit measurable increase in the densitometrically-quantified steady state levels of the ovarian IL-1 beta message. Most striking, however, were the increments noted in the relative abundance of ovarian IL-1 beta transcripts following a 6h exposure to hCG producing a 4 to 5-fold increase (P less than 0.05) over the untreated state at a time point approximately 6h prior to projected follicular rupture. Subsequent evaluation of ovarian IL-1 beta transcripts, 24 and 48h following hCG administration, revealed significant (P less than 0.05) decrements (relative to the 6h peak) to a level comparable to that seen at the conclusion of 48h of treatment with PMSG. Cellular localization studies revealed the gonadotropin-dependent IL-1 beta mRNA to be theca-interstitial cell-exclusive. To assess rat ovarian IL-1 beta gene expression under in vitro circumstances, we have set out to determine whether IL-1 itself may influence the relative level of its own message. Treatment of whole ovarian dispersates with rhIL-1 beta (10ng/ml) for 4 and 24h resulted in a marked (P less than 0.05) time-dependent increase (up to 12-fold) in the relative abundance of IL-1 beta transcripts when compared with untreated controls.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Endocrine- and autocrine-mediated regulation of rat ovarian (theca-interstitial) interleukin-1 beta gene expression: gonadotropin-dependent preovulatory acquisition. 195 17

Ribonucleases are found in considerable quantities in the pancreas of a number of mammalian taxa and a few reptiles. The ribonuclease content varies greatly in different species. Large quantities are found in ruminants and species that have a ruminant-like digestion and in a number of species with coecal digestion. This is a response to the necessity of digesting large amounts of RNA derived from the microflora of the stomach of ruminants or species with ruminant-like digestion or of the coecum of species with coecal digestion. The amino acid sequence of pancreatic ribonuclease from the chromosomal species 2n = 60 of the mole rat, superspecies Spalax Ehrenbergi was determined. From the comparison of the sequence with those of other mammalian species we found that Spalax diverged from the myomorph rodent branch before the divergence of the Muridae (mouse, rat) from the Cricetidae (hamster, muskrat). Spalax ribonuclease shares several amino acid residues with other myomorph rodent species. These are not or only rarely observed outside this rodent suborder. Although the ribonuclease content varies greatly in different mammalian species, the variation in content between individuals within a species is small. Spalax is an exception to this with ribonuclease contents varying over more than an order of magnitude in different individuals. Ribonucleases isolated from the chromosomal species 2n = 52, 2n = 58 and 2n = 60 have identical elution positions on reversed-phase HPLC. The enzyme from the 2n = 54 species, however, elutes at a slightly earlier elution position. No amino acid sequence differences have been found hitherto between the ribonucleases of the four chromosomal species of Spalax ehrenbergi occurring in Israel. However, due to lack of material we were unable to determine more than about 20% of the sequence of the enzyme from the 2n = 54 species, which is the oldest offshoot.
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PMID:Ribonuclease in different chromosomal species of the mole rat, superspecies Spalax ehrenbergi: concentration in the pancreas and primary structure. 230 13

Some of the enzymes and metabolites of the glycolytic pathway of an animal model for cystic fibrosis (the chronically reserpine-treated rat) were investigated. The activities of the enzymes phosphofructokinase (P less than 0.002), enolase (P less than 0.03), pyruvate kinase (P less than 0.005), and lactate dehydrogenase (P less than 0.009) were decreased whereas the activity of glycerol-3-phosphate dehydrogenase was unaffected in the submandibular glands of the treated animals. For metabolites, the reserpine treatment resulted in an increased concentration of glycogen (P less than 0.0002) and phosphoenolpyruvate (P less than 0.001) and a decreased concentration of pyruvate (P less than 0.005) and lactate (P less than 0.002) in the glands. The concentration of glucose and glycerate-2-phosphate was unaffected. The perchloric acid-soluble part of the proteins was also increased (P less than 0.0001) in the submandibular glands of the reserpine-treated animals, as was the activity of ribonuclease. These findings point to a disturbance in the metabolism of glucose and a possible acidosis in the submandibular glands of this animal model for cystic fibrosis.
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PMID:The chronically reserpinized rat: decreased glycolytic activity in the submandibular gland. 399 4

Plagemann, Peter G. W. (Western Reserve University, Cleveland, Ohio), and H. Earle Swim. Replication of mengovirus. I. Effect on synthesis of macromolecules by host cell. J. Bacteriol. 91:2317-2326. 1966.-The replication of mengovirus was studied in two strains of Novikoff (rat) hepatoma cells propagated in vitro. The replicative cycle in both strains required 6.5 to 7 hr. Infection resulted in a marked depression of ribonucleic acid (RNA) and protein synthesis by strain N1S1-63. Inhibition of RNA synthesis was reflected by a decrease in the deoxyribonucleic acid (DNA)-dependent RNA polymerase activity of isolated nuclei. Mengovirus had no effect on either protein or RNA synthesis or on the DNA-dependent RNA polymerase activity of a second strain, N1S1-67. The time course of viral-induced synthesis of RNA by cells was studied in cells treated with actinomycin D. It was first detectable between 2.5 and 3 hr after infection and continued until 6.5 to 7 hr. The formation of mature virus was estimated biochemically by measuring the amount of RNA synthesized as a result of viral infection which was resistant to degradation by ribonuclease in the presence of deoxycholate. Approximately 70% of the deoxycholate-ribonuclease-resistant RNA was located in mature virus, and the remainder was double-stranded. The formation of mature virus began about 45 min after viral-directed (actinomycin-resistant) synthesis of RNA was detectable in the cell, and only about 18 to 20% of the total RNA synthesized was incorporated into virus. Release of virus from cells began about 1 hr after maturation was first detectable. Release of virus from cells was accompanied by a loss of a large proportion of their cytoplasmic RNA and protein.
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PMID:Replication of mengovirus. I. Effect on synthesis of macromolecules by host cell. 428 85

Changes produced in ribosome populations by gamma irradiation of isolated livers (rat) are reported. The main effect was the increase in free ribosomes due to the liberation of membrane bound ribosomes. The radiation apparently injures the binding-site of the large ribosomal subunit, detaching its structural proteins. The disassembled ribosomes are rapidly catabolized by cell RNase. The amount in total and free ribosomes of the livers as a function of the radiation dose was assessed. The relative insensitivity to radiation of the free ribosome pool is discussed in terms of its implications for repair and transformation of the cells.
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PMID:Ribosome changes induced by irradiation of isolated rat liver in vitro. 630 23


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