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:3.1.30.2 (endonuclease)
18,621 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The kininogen (KGN) gene status was examined in 4 families with both high molecular weight (HMW) and low molecular weight (LMW) KGM deficiency and one family with only HMW-KGN deficiency reported in Japan. No abnormal HMW-KGN or LMW-KGN was detected in those with these deficiencies by immunoblot analysis using monoclonal antibodies (HKG-H12, HKG-L7, HKG-L17) for human HMW-KGN. HMW-DNA prepared from peripheral blood leucocytes was digested with endonuclease, EcoRI, Bam HI, Hind III, Sca I, Bg1II, Xba I, Msp I, Pst I, Hpa I, PvuII, HaeIII, Rsa I, Alu I, or Taq I, and studied by Southern blot analysis with human LMW prekininogen cDNA (phKG 36) as a probe. A gross deletion or insertion of the KGN gene was not detected in those with both HMW- and LMW-KGN deficiencies. On the other hand, partial defect in intron 7 (G) was found in those with only HMW-KGN deficiency, suggesting that this defect might be related to abnormality of the alternative RNA splicing events for HMW-prekininogen mRNA.
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PMID:[DNA analysis for the kininogen gene of patients with kininogen deficiency in Japan]. 259 35

The gene deletions responsible for isolated partial deficiency of fetal human chorionic somatomammotropin (hCS) production were characterized by restriction endonuclease analysis of genomic DNA prepared from the leukocytes of an affected child. The phenotypically normal child was the product of a 38-week pregnancy characterized by peak maternal hCS levels of 1.1 micrograms/microliter (normal, 3-9.2 micrograms/ml) and normal levels of other pregnancy-associated hormones. Two genes, termed hCS-A and hCS-B, specify the same mature hCS peptide and are responsible for fetal hCS production. Digestion of the child's DNA with the enzymes Hind III, Eco RI, Bam HI, Bgl II, Hinc II and Msp I disclosed absence of the restriction fragments that normally contain the hCS-A gene. However, the hCS-B gene was present in the child's DNA. The child's DNA digests contained an abnormally large Eco RI fragment of 10.0 kb containing the hCS-L gene. This abnormal fragment is a marker for a deletion that is responsible for complete deficiency of hCS when present in the homozygous state. The child's DNA restriction patterns were consistent with heterozygosity for two different deletions involving hCS genes. The paternal hGH gene cluster lacked the hCS-A, human GH variant, and hCS-B genes, while the maternal cluster lacked only the hCS-A gene. Thus, the child's DNA contained only one of the normal complement of four functional hCS genes per diploid genome. Material hCS levels approximately one fourth as great as those present at comparable stages of normal pregnancies indicated that there was no compensatory increase in expression of the remaining hCS gene.
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PMID:An effect of gene dosage on production of human chorionic somatomammotropin. 298 39

We have examined Blym expression in 11 human tumor cell lines. Increased Blym expression was observed in one of three osteosarcoma cell lines relative to nontransformed human foreskin fibroblasts. In addition, enhanced Blym expression was observed in a melanoma cell line and in 2 of 6 squamous carcinoma cell lines relative to nontransformed, low passage human epithelial cells. We found no evidence of gene amplification or rearrangements of Blym sequences in any of the cell lines we have examined. We further analyzed the state of methylation of the Blym gene in several of the tumor cell lines by Msp I/Hpa 11 restriction endonuclease digestion. All cell lines examined had similar Msp I digestion patterns. However, the different tumor cell lines had different Hpa 11 digestion patterns. Therefore, our results indicate that the Blym gene is differentially expressed and methylated in human tumor cell lines.
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PMID:Expression and methylation of the Blym gene in human tumor cell lines. 303 38

Restriction endonuclease digestion using Hind III and Msp I and Southern blot analysis of DNA from the liver of three inbred rat strains and one outbred strain using cDNA probes yields two banding patterns for the alphafetoprotein and albumin genes. Buffalo and Fischer DNA have one pattern whereas ACI had a different pattern for both genes. Sprague Dawley DNA contains fragments of both patterns suggesting heterozygosity in some individuals of this strain. These polymorphisms do not appear to be associated with any structural or biological differences in the proteins resulting from expression of these genes.
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PMID:Polymorphism of rat alphafetoprotein and albumin genes. 608 1

The expression of three c-onc genes (c-erb, c-myc, c-myb) was investigated in five cell lines established from fibrosarcomas induced with 20-methylcholanthrene (MCA) of Japanese quails. These cell lines showed low levels of the three c-onc genes, with the exception of two cell lines that accumulated moderate (MCAQ 1-4) and large amounts (MCAQ3-5) of c-myc RNA. Molecular cloning and restriction endonuclease analyses indicated that expression of c-myc in these two cell lines were not associated with detectable rearrangements in the c-myc locus, that the size of the c-myc transcript (2.7 kb) in MCAQ 3-5 was similar to that of the normal c-myc messenger RNAs (mRNA) and that the transcriptional activation observed in MCAQ 3-5 was not mediated by the LTR (long terminal repeat) of a proximate ALV (avian leukosis virus) provirus. Finally, when analysed with the restriction enzymes Msp I and Hpa II, the c-myc locus of MCAQ 3-5 and MCAQ 1-4 was found hypomethylated as compared with that of the other cell lines tested that show low levels of c-myc transcripts. Our results suggest that one of the ways methylcholantrene could mediate transformation is by inducing an abnormal regulation of the c-myc gene.
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PMID:Increased transcription of the c-myc oncogene in two methylcholanthrene-induced quail fibroblastic cell lines. 609 23

Human apoprotein(apo) CI and apo AII cDNA probes have been used to analyze the segregation of the human genes in panels of human-mouse hybrids. The apo CI (APOCI) gene segregates with chromosome 19 and the apo AII (APOA2) gene with chromosome 1. Somatic cell hybrids containing chromosome translocations were used to map the apo AII gene to the 1p21-1qter region. Human APOA2 is polymorphic for the restriction endonuclease Msp I. Comparison of human and mouse chromosome 1 reveals a conserved group including apo AII, renin and peptidase genes and suggests that APOA2 will be found distal to this group on human chromosome 1. The mouse apo AII gene is closely linked with genes that regulate HDL structure. Similar HDL regulatory genes will probably be found near human APOA2.
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PMID:Chromosomal localization of the human apoprotein CI gene and of a polymorphic apoprotein AII gene. 609 40

Type II restriction endonucleases cleave duplex DNA at nucleotide sequences displaying 2-fold symmetry. Our data show that Msp I cleaves single strand oligonucleotides, d(G-A-A-C-C-G-G-A-G-A) and d(T-C-T-C-C-G-G-T-T) at 4 degrees, 25 degrees, and 37 degrees C reaction temperatures. The rate of cleavage of d(G-A-A-C-C-G-G-A-G-A) is several-fold faster than that of d(T-C-T-C-C-G-G-T-T). Single strand phi X174 DNA is also, cleaved by Msp I endonuclease giving well defined fragments. 5'-Nucleotide analysis of the fragments generated from single strand and replicating form DNA suggest that cleavage occurs at the recognition sequence d(C-C-G-G). The data show that Msp I endonuclease cleaves single strand oligonucleotides and prefers a recognition sequence surrounded by purine nucleotides. A general model for endonuclease cleavage of single strand and duplex DNA is presented.
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PMID:Cleavage of single strand oligonucleotides and bacteriophage phi X174 DNA by Msp I endonuclease. 615 56

In a rat hepatoma cell line, H4-IIE-C3, a 10-fold excess of 18S and 28S rRNA genes has been found in amplified chromosome regions. Antibodies to 5-methylcytidine bound extensively to the DNA of these regions, indicating a high level of DNA methylation. Most of the amplified rRNA genes were transcriptionally inactive, as shown by their failure to stain with silver. DNAs from the tumor cells and control rat hepatocytes grown with L-[methyl-14C]methionine were digested with restriction endonuclease EcoRI; the DNA fragments were separated by agarose gel electrophoresis, denatured, transferred to nitrocellulose filters, and hybridized to 32P-labeled rRNA or cDNA. Fragments containing the 18S or 28S rRNA coding sequences occurred in three major size classes; all three were rich in 5-methylcytosine. Analysis of EcoRI fragments of DNA from the tumor and control cells after digestion with Hpa II or Msp I endonuclease indicated that the 5'-C-C-G-G-3' sequences in most of the amplified rRNA genes were methylated. Analysis of the fragments produced by digestion with Hha I endonuclease indicated a high degree of methylation within its recognition sequence in the amplified rRNA genes as well. The association of hypermethylation with restricted transcriptional activity suggests that DNA methylation may regulate the activity of the rRNA genes.
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PMID:Amplified ribosomal RNA genes in a rat hepatoma cell line are enriched in 5-methylcytosine. 616 93

Expression of the mouse alpha-fetoprotein gene in embryonic, adult, and neoplastic tissues was assessed by RNA dot hybridization using 32P-labeled alpha-fetoprotein cDNA as probe, alpha-fetoprotein mRNA was present in high levels in total RNA from yolk sac endoderm, fetal liver, and an alpha-fetoprotein-producing hepatoma. In contrast, this mRNA was greatly depleted in total RNA from yolk sac mesoderm and essentially absent in brain, adult liver, and a non-alpha-fetoprotein-producing hepatoma. These results indicated that alpha-fetoprotein gene expression was controlled primarily at the transcriptional level. The presence of the modified base, 5-methylcytosine, in the alpha-fetoprotein gene was studied by comparing hybridization patterns obtained by Southern blot analysis of DNA cleaved with the restriction endonuclease isoschizomers Msp I and Hpa II. The gross sequence organization and reiteration frequency of the alpha-fetoprotein gene were invariant among the DNA samples, whereas, in each case, there was a positive correlation between hypomethylation of six CCGG (Hpa II) sites in the alpha-fetoprotein gene and expression of this gene. These Hpa II sites were distributed throughout a large portion of the alp]a-fetoprotein gene. Patterns of cytosine methylation in this gene were established before day 15 of gestation in yolk sac endoderm and mesoderm.
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PMID:Expression and methylation of the mouse alpha-fetoprotein gene in embryonic, adult, and neoplastic tissues. 617 46

The 5-methylcytosine (m5C) content of DNAs from Morris hepatomas of varying growth rates and from normal liver was analyzed. DNA methylation in all hepatomas studied was found to be 20-45% less than in normal liver. This result was confirmed independently by restriction endonuclease (Hpa II and Msp I) analysis. While these results agreed with recent literature data suggesting hypomethylation of DNA from some neoplastic sources, no correlation was observed between the extent of DNA hypomethylation and the growth rates of the tumors.
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PMID:DNA hypomethylation in Morris hepatomas. 619 2


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