Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
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Query: EC:3.1.30.1 (
S1 nuclease
)
3,660
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The structural organization of the gene coding for human hepatocyte growth factor (hHGF) has been determined by seven overlapping lambda phage genomic clones including three clones that were previously characterized. The gene for hHGF spans about 70 kbp of DNA and consists of 18 exons separated by 17 introns. The coding sequence of hHGF consists of multiple putative domains that are homologous to those observed in plasminogen. These regions were found as separate exons in the gene, and the exon-intron arrangement was similar to that of plasminogen. These results suggest that the genes for hHGF and plasminogen have arisen through gene duplication events from an ancestral gene. The major transcription initiation site of the hHGF gene is located 76 bp upstream of the translational start codon as judged by
S1 nuclease
mapping and primer extension analyses. A TATA-like element was found 33 nucleotides upstream of the transcription initiation site. Two sequence elements, an
interleukin 6
response element (CTGGGA) and a potential binding site for NF-IL6 (TGAGGAAAG), are located near the transcription initiation site. These sequence elements might be involved in the regulation of HGF gene expression.
...
PMID:Structural organization and the transcription initiation site of the human hepatocyte growth factor gene. 183 56
We analyzed the effect of several growth factors and cytokines on the expression of amyloid beta protein precursor (APP) mRNAs in cultured mouse neuronal and glial cells. In neuronal cultures from embryonic day-15 brain. Northern blotting revealed that APP mRNAs increased by 1.3- to 2.6-fold when treated with nerve growth factor, basic fibroblast growth factor, interleukin 1, interleukin 2, interleukin 3,
interleukin 6
or granulocyte-macrophage colony-stimulating factor but not with tumor necrosis factor alpha. An
S1 nuclease
protection assay revealed that the enhanced APP mRNA in neuronal cultures was exclusively APP695 mRNA. On the other hand, astrocyte-enriched cultures prepared from postnatal day-2 brain did not show any significant alteration among these factors. We conclude that certain growth factors and cytokines could enhance APP 695 mRNA expression in neurons in vitro.
...
PMID:Effect of growth factors and cytokines on expression of amyloid beta protein precursor mRNAs in cultured neural cells. 847 81
Microglia rapidly respond to lipoplysaccharide (LPS) by transformation from resting to active states and secretion of several neuro- and immuno-regulators including tumour necrosis factor alpha (TNF-alpha), interleukin 1 beta (IL-1 beta), and
interleukin 6
(
IL-6
). With longer LPS treatment, microglia are converted to reactive or phagocytic states with characteristics similar to macrophages in inflammation and injury processes. We have investigated LPS-mediated changes in two myristoylated substrates of protein kinase C (PKC): MARCKS (myristoylated alaninerich C kinase substrate) and MRP (MARCKS-related protein). Within 6 hours of addition, LPS induced a twofold increase in [3H]myristoylated and immunoreactive MARCKS protein and a sevenfold increase in MRP. The differential effect of LPS on expression of MRP vs. MARCKS was even more dramatic at the level of transcription:
S1 nuclease
protection assays revealed a 40-fold increase in MRP mRNA levels (maximum at 4-6 hours), whereas a threefold increase was observed for MARCKS. TNF alpha and colony-stimulating factor 1 (CSF-1), two cytokines which are induced by LPS, did not reproduce the observed effect of LPS on MARCKS and MRP gene transcription. CSF-1 also induced differential transcription of MRP, but of lower magnitude (threefold) and more sustained than by LPS. Accordingly, these two substrates for PKC are differentially up-regulated by LPS, apparently independent of TNF alpha or CSF-1.
...
PMID:Lipopolysaccharide stimulates differential expression of myristoylated protein kinase C substrates in murine microglia. 872 62