Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.22.1 (DNase II)
 429 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

DNase II purified from porcine spleen (pDNase II) comprises alpha(1), alpha(2) and beta subunits. The three subunits are encoded by one cDNA, in the sequence alpha(1), beta, and alpha(2), and the peptides linking these subunits are presumably cleaved out post-translationally. To understand the relevance of post-translational cleavage to pDNase II, recombinant pDNase II (rpDNase II) was produced in human 293T cells by transfection with an expression plasmid containing pDNase II cDNA (pcDNaseII). An 11.5, a 35 and a 46.5 kDa protein were detected in the cell lysates, whereas only a 46.5 kDa protein was detected in the culture medium of the pcDNaseII-transfected cells. The 46.5 kDa rpDNase II secreted into the medium was purified to homogeneity and characterized. MALDI-TOF MS and N-terminal amino acid sequencing of the 46.5 kDa protein revealed a single contiguous polypeptide chain of pDNase II. Zymographic analysis showed that the 46.5 kDa protein digested DNA in acidic conditions and that the specific activity of this rpDNase II was about twice that of pDNase II purified from porcine spleen. Treatment with chloroquine, a lysosomal inhibitor, resulted in the accumulation of only the 46.5 kDa protein in the pcDNaseII-transfected cells. Treatments with cycloheximide 22 h after transfection led to accumulation of the processed enzyme and disappearance of the 46.5 kDa protein. These results suggest that the proteolytic processing of rpDNase II occurs in the lysosome, which is not involved in the activation of pDNase II.
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PMID:Proteolytic processing of porcine deoxyribonuclease II occurs in lysosomes but is not required for enzyme activation. 1929 69

Trichinella spiralis surface proteins are directly exposed to the host's immune system, making them the main target antigens which induce the immune responses and may play an important role in the larval invasion and development process. The analysis and characterization of T. spiralis surface proteins could provide useful information to elucidate the host-parasite interaction, identify the early diagnostic antigens and the targets for vaccine. The purpose of this study was to identify the surface proteins of T. spiralis muscle larvae by two-dimensional gel electrophoresis (2-DE) Western-blot analysis and mass spectrometry. The 2-DE results showed that a total of approximately 33 proteins spots were detected with molecular weights varying from 10 to 66 kDa and isoelectric point (pI) from 4 to 7. Fourteen protein spots were recognized by sera of mice infected with T. spiralis at 42 dpi or at 18 dpi, and 12 spots were successfully identified by MALDI-TOF/TOF-MS, which represented 8 different proteins of T. spiralis. Out of the 8 T. spiralis proteins, 5 proteins (partial P49 antigen, deoxyribonuclease II family protein, two serine proteases, and serine proteinase) had catalytic and hydrolase activity, which might be the invasion-related proteins and the targets for vaccine. The 4 proteins (deoxyribonuclease II family protein, serine protease, 53 kDa ES antigen and hypothetical protein Tsp_08444) recognized by infection sera at 18 dpi might be the early diagnostic antigens for trichinellosis.
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PMID:Identification of surface proteins of Trichinella spiralis muscle larvae using immunoproteomics. 2577 83