Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.27.5 (RNase)
 17,967 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Alpha-1 antitrypsin messenger RNA (A1AT mRNA) was determined in alveolar macrophages and in peripheral blood monocytes of healthy individuals using a sensitive RNase protection assay. Determinations were made of bacterial lipopolysaccharide (LPS) stimulated and unstimulated cells. We found that the amount of A1AT mRNA increased 7.3 and 14 times after 4 h of incubation with LPS for monocytes and macrophages, respectively (relative to total RNA). The increase was 12.3 and 14.8 times, respectively, when expressed as increase per cell. In both cell types there was wide interindividual variation in LPS response: 2-36 and 5-12 times for monocytes and macrophages, respectively. The possible significance of A1AT production of monocytes and macrophages may be the local control of granulocytic proteases such as elastase and cathepsin G.
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PMID:Alpha-1 antitrypsin response of stimulated alveolar macrophages. 142 67

Granzyme F belongs to a closely related family of seven murine serine proteases stored in cytoplasmic granules of lymphoid cell populations. In contrast to the murine granzymes A to E and G, granzyme F is exclusively expressed in the CD4-CD8+ subset of peripheral T cells. To characterize the genomic sequences responsible for its highly restricted expression, we isolated a cosmid clone and sequenced a 7.5-kb genomic fragment that contains the promoter region and all five exons of the murine granzyme F gene. A TATA box sequence is located at position -25 relative to the transcription initiation site, which was determined by RNase protection. The genomic organization of granzyme F is similar to that of granzyme B and granzyme C, leukocyte elastase, cathepsin G, rat mast cell protease II, and complement factor D (adipsin). By the use of two fluorochromes for simultaneous high resolution in situ hybridization, the granzyme F gene was localized in close proximity distally from the TCR alpha-chain locus on mouse chromosome 14.
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PMID:Genomic organization and subchromosomal in situ localization of the murine granzyme F, a serine protease expressed in CD8+ T cells. 186 Oct 68

Subunit rLMP7 of the multicatalytic proteinase (MCP), which has been associated with chymotrypsin-like proteinase activity, was examined in rat liver and hepatocyte-derived cell lines. rLMP7 was detected in both nucleus and cytosol in liver by immunohistochemistry and immunoblotting, using a peptide-specific anti-rLMP7 antibody. A M(r) 30,000 precursor protein was present only in cytosol, as was a minor component of M(r) 25,000. Mature rLMP7 (M(r) 23,000) was present in MCP in both nucleus and cytosol, although it was not detectable in the nuclear scaffold. Two rLMP7 cDNAs (designated rLMP7.1 and rLMP7.s) were identified by rapid amplification of 5' ends using RT/PCR, a result which was confirmed by Northern blot analysis and RNase protection assays. rLMP7.1 is 3-4x more abundant than rLMP7.s; it is 50 nt longer than the previously reported cDNA sequence and includes an upstream in-frame ATG within a consensus translation initiation sequence, which encodes the M(r) 30,000 rLMP7 precursor protein identified in vivo. rLMP7.s is 100 nt shorter than rLMP7.1 and does not contain the most 5' ATG. Transient transfection analyses with rLMP7.1 and rLMP7.s constructs coupled to green fluorescent protein showed that both transcripts were efficiently expressed in vivo. In vitro expression of these two rLMP7 cDNAs showed that rLMP7.1 produces the M(r) 30,000 precursor protein, whereas rLMP7.s produces two smaller peptides of M(r) 25,000 and 23,000. Purified 20S MCP preparations were able to proteolytically process the M(r) 30,000 precursor to the M(r) 25,000 product but not to the mature rLMP7 form. However, incorporation of this processed M(r) 25,000 product (or of either M(r) form produced from rLMP7.s) did not occur in vitro. In vitro processing and pulse-chase experiments suggested that the mature M(r) 23,000 subunit is derived, at least in part, from the M(r) 30,000 precursor. The M(r) 25,000 form may be a stable product produced directly from rLMP7.s.
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PMID:Studies on rLMP7, a beta-subunit of the multicatalytic proteinase. 922 75

Killer lymphocyte granzyme (Gzm) serine proteases induce apoptosis of pathogen-infected cells and tumor cells. Many known Gzm substrates are nucleic acid binding proteins, and the Gzms accumulate in the target cell nucleus by an unknown mechanism. In this study, we show that human Gzms bind to DNA and RNA with nanomolar affinity. Gzms cleave their substrates most efficiently when both are bound to nucleic acids. RNase treatment of cell lysates reduces Gzm cleavage of RNA binding protein targets, whereas adding RNA to recombinant RNA binding protein substrates increases in vitro cleavage. Binding to nucleic acids also influences Gzm trafficking within target cells. Preincubation with competitor DNA and DNase treatment both reduce Gzm nuclear localization. The Gzms are closely related to neutrophil proteases, including neutrophil elastase (NE) and cathepsin G. During neutrophil activation, NE translocates to the nucleus to initiate DNA extrusion into neutrophil extracellular traps, which bind NE and cathepsin G. These myeloid cell proteases, but not digestive serine proteases, also bind DNA strongly and localize to nuclei and neutrophil extracellular traps in a DNA-dependent manner. Thus, high-affinity nucleic acid binding is a conserved and functionally important property specific to leukocyte serine proteases. Furthermore, nucleic acid binding provides an elegant and simple mechanism to confer specificity of these proteases for cleavage of nucleic acid binding protein substrates that play essential roles in cellular gene expression and cell proliferation.
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PMID:Leukocyte protease binding to nucleic acids promotes nuclear localization and cleavage of nucleic acid binding proteins. 2477 51