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 mouse biliary glycoprotein 1 gene (bgp1) encodes several multifunctional glycoprotein isoforms. These glycoproteins represent members of the carcinoembryonic antigen (CEA) family which belongs to the immunoglobulin superfamily. The Bgp1 glycoproteins function as cell adhesion molecules and receptors for the mouse hepatitis viruses. In contrast to CEA, whose overexpression has been correlated with cancer progression, the human and mouse Bgp proteins are generally down-regulated upon tumor formation. In this study, we report on the mouse bgp1 gene organization and transcriptional activation. We have isolated phage and cosmid clones encompassing the entire bgp1 coding region. This gene consists of nine exons, some of which are subjected to alternative splicing producing a minimum of four splice variants. A comparison of the murine bgp1 proximal promoter with the human BGP and mouse cea10/bgp3 genes revealed sequence conservation of 66% and 95%, respectively. RNase protection assays and primer extension analyses indicated that the mouse bgp1 transcriptional start site is positioned 240 nucleotides upstream of the ATG translational initiation codon, which is 140 nucleotides further upstream than in any other CEA family member. The bgp1 promoter is transcriptionally active in reporter gene activation in vitro transfection studies and in vivo using a bgp1-containing cosmid clone. We identified three putative AP-2 or AP-2-like sites and an upstream stimulatory factor (USF) recognition sequence within the proximal mouse bgp1 promoter region at positions similar to those used by the human BGP promoter region. These data suggest that the regulation of the mouse and human BGP genes may follow some common spatial and temporal expression. Interestingly, the bgp1 proximal promoter and coding region are also well conserved throughout evolution.
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PMID:Characterization and transcriptional activity of the mouse biliary glycoprotein 1 gene, a carcinoembryonic antigen-related gene. 762 60

Lactoferrin is a 703-amino acid glycoprotein originally isolated from milk. Plasma lactoferrin is predominantly neutrophil derived but indications are that it may also be produced by other cells. Lactoferrin in body fluids is found in the iron-free form, the monoferric form and in the diferric form. Three isoforms of lactoferrin have been isolated, ie two with RNase activity (lactoferrin-beta and lactoferrin-gamma) and one without RNase activity (lactoferrin-alpha). Receptors for lactoferrin can be found on intestinal tissue, monocytes/macrophages, neutrophils, lymphocytes, platelets, and on certain bacteria. A wide spectrum of functions are ascribed to lactoferrin. These range from a role in the control of iron availability to immune modulation. More research is necessary however to obtain clarity with regard to the exact mechanism of action of lactoferrin.
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PMID:Lactoferrin: a general review. 767 21

We isolated 18 cDNA candidates that were expected to encode parts of the self-incompatibility-associated RNase of Lycopersicon peruvianum PI 126441 (S11a-plant) from a style cDNA library. Polymerase chain reaction was used with oligonucleotides derived from conserved amino acid sequences of RNases from fungi and S-associated RNases in other species of Solanaceae. Two of these clones (both do not have full length sequences) gave 826-bp and 730-bp sequences, and they had the same open reading frame, named ORF-1. Comparison of the deduced amino acid sequence of ORF-1 with S-associated RNase of other Solanaceous plants showed a high degree of similarity. mRNA encoding this ORF-1 was about 1000 bases long and detected only in the style tissue by Northern analysis. Using one of the cDNA clones as a probe, we detected sequence variability among three different S-genotypes of randomly chosen wild-type tomatoes by Southern analysis. From these results, it was concluded that ORF-1 encodes the self-incompatibility associated S-glycoprotein of L. peruvianum PI 126441 (S11a-plant).
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PMID:Identification of cDNA clones coding for the style specific S11a-glycoprotein gene associated with gametophytic self-incompatibility in tomato (Lycopersicon peruvianum). 768 79

The expression of the multidrug resistance-associated protein (MRP), a new glycoprotein involved in drug resistance, was investigated in tumour samples from 80 patients with chronic B-cell malignancies by a quantitative RNase protection assay. In B-cell chronic lymphocytic leukaemia (B-CLL) (n = 32), either treated (n = 18) or untreated (n = 14), a high percentage of patients (20/32: 63%) had relatively high expression levels of the MRP gene (25U or more). In addition, hyperexpression of the MRP gene was demonstrated in 4/10 (40%) untreated patients with B-cell prolymphocytic leukaemia (B-PLL). In contrast, low MRP mRNA expression levels were detected in hairy cell leukaemia (n = 7), non-Hodgkin's lymphoma (n = 13) and multiple myeloma (n = 18). Statistical analysis of MRP expression in untreated CLL (mean +/- SD 29.2 +/- 18.5 U) versus treated CLL (mean +/- SD 26.7 +/- 13.7 U) did not show significant differences in MRP expression between the two groups. Southern blot analysis did not reveal amplification of the MRP gene in the leukaemia samples with elevated MRP mRNA levels. We conclude that B-PLL and B-CLL frequently display high MRP expression and that this hyperexpression is probably due to transcriptional activation and/or increased mRNA stability.
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PMID:High expression of the multidrug resistance-associated protein (MRP) in chronic and prolymphocytic leukaemia. 780 81

Ribonuclease B has become a paradigm as a simple example of an N-linked glycoprotein. We have found that certain affinity-purified preparations of this enzyme demonstrated a pronounced tendency to lose activity if stored as dilute aqueous solutions. Such inactivation is accelerated by the presence of NaCl, but can be counteracted by inclusion of high (1 mol/l) concentrations of xylose. Enzyme activity cannot be restored by addition of xylose after storage of the enzyme. In marked contrast to alpha-methyl-mannoside, xylose does not prevent ribonuclease B from binding to concanavalin A and so may be used to stabilize the enzyme during purification by lectin affinity chromatography.
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PMID:Stabilization of ribonuclease B activity by concentrated xylose solutions. 785

Recombinant human interferon-gamma (IFN-gamma) glycoform populations produced by Chinese hamster ovary cells have been resolved by micellar electrokinetic capillary chromatography (MECC). Separations were performed in uncoated fused silica capillaries at alkaline pH in the presence of micellar concentrations of the anionic detergent sodium dodecyl sulfate (SDS). Maximum resolution was obtained reproducibly with high-ionic-strength borate/SDS electrophoresis buffer. Under the conditions described, glycoform migration time was inversely related to the amount of carbohydrate associated with the protein. Digestion of IFN-gamma with peptide-N-glycosidase F allowed virtual real-time monitoring of glycosidase digests by capillary electrophoresis. Analysis of other digestions with either neuraminidase or endoglycosidase H (endo H) showed most IFN-gamma glycoforms to be sialylated and a minor proportion of glycoforms to be associated with oligomannose structures. While both bovine pancreas ribonuclease B and horse-radish peroxidase glycoforms were separated by this technique, proteins glycosylated at multiple sites such as bovine serum fetuin and human alpha 1-acid glycoprotein were not well resolved by MECC.
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PMID:High-resolution separation of recombinant human interferon-gamma glycoforms by micellar electrokinetic capillary chromatography. 786 54

Simian varicella virus (SVV) causes a natural, varicella-like disease in nonhuman primates. The unique short region of the SVV genome contains four open reading frames (ORFs), two of which encode glycoproteins that exhibit extensive homology with varicella-zoster virus (VZV) gpIV (gI) and gpI (gE). Northern hybridization, primer extension, and RNase protection analyses were employed to define precisely the transcripts mapping to the SVV gpIV and gpI genes. A total of five transcripts composing two coterminal families of RNAs were mapped to the SVV gpIV and gpI ORF region. Based on transcriptional mapping and previous DNA sequence analysis, two transcripts 1.3 and 2.2 kb in size were assigned to the SVV gpIV and gpI genes, respectively. The transcriptional patterns described in this study for the SVV gpIV and gpI ORFs are analogous to those previously reported for the homologous glycoproteins genes encoding the herpes simplex virus type 1 Us7 (gI) and Us8 (gE) and VZV gpIV and gpI genes. In addition, the transcriptional start site for the VZV gpI RNA was determined. DNA alignments of the promoter regions for the SVV and VZV gpIV and gpI genes revealed a number of cis-acting elements which are conserved between the two viruses. The characterization of SVV glycoprotein genes will facilitate future studies to define their role in SVV pathogenesis and immunity and assist in the construction of recombinant vaccines which could be evaluated in the simian varicella model.
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PMID:Transcriptional analysis of two simian varicella virus glycoprotein genes which are homologous to varicella-zoster virus gpI (gE) and gpIV (gI). 797 31

Unlike other small animals, cytomegalovirus (CMV) infection of the guinea pig results in transplacental passage and intrauterine infection of the fetus. These features make the guinea pig model ideal for studying vaccine strategies designed to prevent congenital infection. Unfortunately, little is known about immunogenic guinea pig CMV gene products. In other animal cytomegaloviruses, a major target of the host immune response is the glycoprotein B (gB, gp UL 55) gene product. Using DNA probes containing human CMV gB sequences, the gB gene homolog of the guinea pig cytomegalovirus was identified, cloned, and sequenced. The gpCMV gB gene maps to a region spanning portions of the HindIII K, Q, and P fragments of the gpCMV genome. DNA sequence analysis identified an open reading frame of 2706 nucleotides capable of encoding a protein of 901 amino acids. Extensive similarity to the human and murine gB proteins was noted with 42% identity at the amino acid level. The predominant gpCMV gB mRNA is a 6.8-kb transcript with the expression kinetics of an early gene. RNase protection and primer extension analyses indicated that gB mRNAs were transcribed from two different initiation sites corresponding to distinct TATA elements. Polyclonal antisera prepared against a synthetic peptide derived from amino acid sequences within the ORF identified a 58-kDa virion-associated protein representing the cleaved COOH-terminus (gp 58) of the gpCMV gB molecule. The molecular characterization of gpCMV gB should facilitate studies of vaccine strategies in the guinea pig model of congenital CMV infection.
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PMID:Cloning and characterization of the guinea pig cytomegalovirus glycoprotein B gene. 800 31

Gametophytic self-incompatibility in the Solanaceae is controlled by a single, multiallelic locus, the S locus. We have recently described an allele of the S locus of Lycopersicon peruvianum that caused this normally self-incompatible plant to become self-compatible. We have now characterized two glycoproteins present in the styles of self-compatible and self-incompatible accessions of L. peruvianum: one is a ribonuclease that cosegregates with a functional self-incompatibility allele (S6 allele); the other cosegregates with the self-compatible allele (Sc allele) but has no ribonuclease activity. The derived amino acid sequences of the cDNAs encoding the S6 and Sc glycoproteins resemble sequences of other ribonucleases encoded by the S locus. The derived sequence for the Sc glycoprotein differs from the others by lacking one of the histidine residues found in all other S-locus ribonucleases. These findings demonstrate the essential role of ribonuclease activity in self-incompatibility and lend further weight to evidence that this histidine residue is involved in the catalytic site of the enzyme.
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PMID:Loss of a histidine residue at the active site of S-locus ribonuclease is associated with self-compatibility in Lycopersicon peruvianum. 802 14

Bovine respiratory syncytial virus (BRSV) is a very important pathogen of cattle and perhaps other ruminants. It is a major contributor to the incidence of respiratory tract disease in nursing beef and feedlot and dairy calves. The genome of respiratory syncytial viruses encodes 10 proteins translated from 10 unique mRNAs. The major glycoprotein (G), fusion protein (F), 1A protein and the 22K protein are components of the viral envelope. The nucleocapsid contains the nucleocapsid protein (N), the phosphoprotein (P), and the large protein (L). The matrix protein (M) forms a structural layer between the envelope and the nucleocapsid. Antibodies to all the structural proteins develop in convalescent calves. However, evidence suggests that immunity develops primarily as a result of the antigenic stimulus by the major glycoprotein G and the fusion glycoprotein F. It is known also that activated cytotoxic T cells interact with N and F protein antigens and helper T cells interact with N, F, and 1A protein antigens. With the exception of the major glycoprotein, the respective proteins of various respiratory syncytial viruses share major antigenic domains. Based on antigenic differences of the major glycoprotein, at least 3 subgroups of RSV are recognized; human A, human B, and bovine RSV. Indirect evidence suggests that a second subgroup of BRSV exists. However, we have identified only one BRSV subgroup based on our work with RNase mismatch cleavage analysis of the G protein gene from a limited number of strains. Furthermore, our data indicated that a caprine RSV isolate is closely related to the bovine strains, but an ovine isolate is not. The latter may constitute yet another subgroup of RSV. These data affect decisions on optimization of immunoprophylaxis since evidence suggests that protection against a homologous RSV subgroup virus is superior to that against a heterologous strain in immune subjects.
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PMID:Antigenic diversity of respiratory syncytial viruses and its implication for immunoprophylaxis in ruminants. 811 89


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