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101.
Ligtenberg AJ Veerman EC Nieuw Amerongen AV Mollenhauer J 《Biological chemistry》2007,388(12):1275-1289
Salivary agglutinin (SAG), lung glycoprotein-340 (gp-340) and Deleted in Malignant Brain Tumours 1 (DMBT1) are three names for identical proteins encoded by the dmbt1 gene. DMBT1/SAG/gp-340 belongs to the scavenger receptor cysteine-rich (SRCR) superfamily of proteins, a superfamily of secreted or membrane-bound proteins with SRCR domains that are highly conserved down to sponges, the most ancient metazoa. On the one hand, DMBT1 may represent an innate defence factor acting as a pattern recognition molecule. It interacts with a broad range of pathogens, including cariogenic streptococci and Helicobacter pylori, influenza viruses and HIV, but also with mucosal defence proteins, such as IgA, surfactant proteins and MUC5B. Stimulation of alveolar macrophage migration, suppression of neutrophil oxidative burst and activation of the complement cascade point further to an important role in the regulation of inflammatory responses. On the other hand, DMBT1 has been demonstrated to play a role in epithelial and stem cell differentiation. Inactivation of the gene coding for this protein may lead to disturbed differentiation, possibly resulting in tumour formation. These data strongly point to a role for DMBT1 as a molecule linking innate immune processes with regenerative processes. 相似文献
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To facilitate identification and characterization of genomic functional elements, we have developed a chromatin architecture alignment algorithm (ArchAlign). ArchAlign identifies shared chromatin structural patterns from high-resolution chromatin structural datasets derived from next-generation sequencing or tiled microarray approaches for user defined regions of interest. We validated ArchAlign using well characterized functional elements, and used it to explore the chromatin structural architecture at CTCF binding sites in the human genome. ArchAlign is freely available at http://www.acsu.buffalo.edu/~mjbuck/ArchAlign.html. 相似文献
104.
den Hertog AL van Marle J Veerman EC Valentijn-Benz M Nazmi K Kalay H Grün CH Van't Hof W Bolscher JG Nieuw Amerongen AV 《Biological chemistry》2006,387(10-11):1495-1502
The human cathelicidin peptide LL-37 and several truncated variants differ in their capability to transmigrate over the plasma membrane of Candida albicans. We investigated whether retention at the cell perimeter or membrane transmigration affects their membrane-disrupting activities and candidacidal properties. Using fluorescein-labeled peptides, we demonstrate that LL-37 and its C-terminally truncated peptide LL-31 remain permanently associated with the perimeter of the cell. The N-terminally truncated peptide RK-31 initially accumulated at the cell boundary, but transmigrated into the cytoplasm within 30 min. The C-terminally truncated peptide LL-25 transmigrated instantaneously into the cytoplasm. The ultrastructural effects on the plasma membrane were studied by freeze-fracture electron microscopy combined with filipin cytochemistry. All peptides, whether they transmigrated over the plasma membrane or not, induced phase separation in the plasma membrane. All peptides induced leakage of cell components, including nucleotides and proteins. Proteins were identified by SDS-PAGE in combination with mass spectrometry, which revealed that predominantly proteins smaller than 50 kDa had leaked out of C. albicans. 相似文献
105.
Gabriel M Nazmi K Veerman EC Nieuw Amerongen AV Zentner A 《Bioconjugate chemistry》2006,17(2):548-550
Modification of material surfaces aimed at bestowing them with antimicrobial properties is a promising approach in the development of new biomaterials. Antimicrobial peptides (AMPs) are an attractive alternative to conventional antibiotics because of lack of toxicity, inherently high selectivity, and absence of immune response. As the antimicrobial mode of action of the AMP cathelin LL37 is formation of pores and disruption of microbial membrane, the purpose of the present study was to develop and test a method of covalent immobilization of LL37 on titanium surface. The application of a flexible hydrophilic poly(ethylene glycol) spacer and selective N-terminal conjugation of LL37 resulted in a surface peptide layer which was capable of killing bacteria on contact. 相似文献
106.
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Behavioural responses were studied in mated and unmated females of a Dutch strain of the spider mite Tetranychus urticae which were destined to enter diapause. Observations were confined to the period between acquirement of the winter coloration by the females (a few days after the last moult) and their entering of artificial hibernation sites offered to the mites on the host leaves. Unmated females were found to stay longer on the leaf surface than mated females; they entered the hibernation sites significantly later than mated females. The delay in the search for hibernation sites shown by unmated females may be seen as a behavioural adaptation to enhance the chance of being fertilized before hibernation. Winter survival of mated and unmated diapausing females of the same strain of mites was studied both in the laboratory at a constant temperature of 2±1°C and outdoors under natural climatic conditions in Amsterdam during the winter of 1990–1991. Survival was high under both conditions for mated as well as unmated females; no significant differences in survival were found between both types of female. Observations on post-diapause females of Tetranychus atlanticus (a mite belonging to the T. urticae complex) sampled from strawberry fields near Moscow in spring, showed that at most 10% of the females of this natural spider mite population were unmated. Both mated and unmated females had survived winter temperatures of -28 to -30°C. 相似文献
108.
Coccia C Rinaldi AC Luca V Barra D Bozzi A Di Giulio A Veerman EC Mangoni ML 《European biophysics journal : EBJ》2011,40(4):577-588
Bombinins H are mildly cationic antimicrobial peptides isolated from the skin of the anuran genus Bombina, the fire-bellied toad. Some members of this peptide family coexist in skin secretions as diastereomers in which a single
d-amino acid (alloisoleucine or leucine) is incorporated as a result of the post-translational modification of the respective
gene-encoded l-amino acid. Here we report on the antimicrobial properties and membrane interactions of bombinins H2 and H4. The latter differs
from H2 by the presence of a d-alloisoleucine at the second N-terminal position. Specifically, we have evaluated the antimicrobial activity of H2 and H4
against a large panel of reference and clinical isolates of Gram-negative and Gram-positive bacteria; performed membrane permeation
assays on both intact cells and model membranes (lipid monolayers and liposomes) mimicking the composition of the plasma membrane
of Gram-negative/positive bacteria; used biochemical tools, such as trypsin-encapsulated liposomes and capillary electrophoresis,
to monitor the peptides’ ability to translocate through the membrane of liposomes mimicking Escherichia coli inner membrane. The results revealed interesting relationships between the presence of a single d-amino acid in the sequence of an antimicrobial peptide and its target microbial cell selectivity/membrane-perturbing activity. 相似文献
109.
Veerman JL 《PLoS medicine》2011,8(11):e1001114
110.