Identification and purification of a novel serine proteinase inhibitor
We report the identification, purification, and partial amino acid sequence of a novel serine proteinase inhibitor which is present in extracts from human placentas and in the cytosolic fraction of the leukemic cell line K562. Extracts from these tissues exhibited time-dependent inhibition of the serine proteinase thrombin.
P B, Coughlin, T, Tetaz, H H, Salem
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Isolation, cloning and structural characterisation of boophilin, a multifunctional Kunitz-type proteinase inhibitor from the cattle tick. [PDF]
Inhibitors of coagulation factors from blood-feeding animals display a wide variety of structural motifs and inhibition mechanisms. We have isolated a novel inhibitor from the cattle tick Boophilus microplus, one of the most widespread parasites of farm ...
Sandra Macedo-Ribeiro +7 more
doaj +1 more source
Organization and sequence of the gene encoding the human acrosin-trypsin inhibitor (HUSI-II) [PDF]
A complete cDNA encoding the acrosin-trypsin inhibitor, HUSI-II, was used as a probe to isolate genomic clones from a human placenta library. Three clones which cover the entire HUSI-II gene were isolated and characterized.
Abelson +28 more
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Serine Proteinase Inhibitors Produced by Human Melanoma Cell Lines
The human melanoma cell lines M21 and MSM-M2 are shown to produce two similar competitive inhibitors of trypsin, a serine proteinase. These proteinase inhibitors inhibited the serine proteinases trypsin and kallikrein with similar efficiency but did not inhibit plasmin (a serine proteinase) or papain (a thiol proteinase).
D, Giacomoni, F, Najmabadi, S, Dray
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Os insetos podem causar perdas consideráveis aos seus hospedeiros, entretanto alguns deles habitam em plantas sem causar-lhes danos. Por exemplo, Thyrinteina leucoceraea, herbívoro da entomofauna brasileira, pode ser encontrado na goiabeira, hospedeiro ...
Jeanne Scardini Marinho +4 more
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Dietary regulation of serine proteinases that are resistant to serine proteinase inhibitors
Ingestion of Kunitz soybean trypsin inhibitor (STI) by larval Helicoverpa zea, Agrotis ipsilon, and Trichoplusia ni extended the retention time of food in the digestive tract and increased the level of activity of proteolytic enzymes that were not susceptible to inhibition by STI.
openaire +2 more sources
By dawn or dusk—how circadian timing rewrites bacterial infection outcomes
The circadian clock shapes immune function, yet its influence on infection outcomes is only beginning to be understood. This review highlights how circadian timing alters host responses to the bacterial pathogens Salmonella enterica, Listeria monocytogenes, and Streptococcus pneumoniae revealing that the effectiveness of immune defense depends not only
Devons Mo +2 more
wiley +1 more source
Processing of Neutrophil α-Defensins Does Not Rely on Serine Proteases In Vivo. [PDF]
The α-defensins, human neutrophil peptides (HNPs) are the predominant antimicrobial peptides of neutrophil granules. They are synthesized in promyelocytes and myelocytes as proHNPs, but only processed in promyelocytes and stored as mature HNPs in ...
Andreas Glenthøj +3 more
doaj +1 more source
Diabetic retinopathy: could the alpha-1 antitrypsin be a therapeutic option? [PDF]
Diabetic retinopathy is one of the most important causes of blindness. The underlying mechanisms of this disease include inflammatory changes and remodeling processes of the extracellular-matrix (ECM) leading to pericyte and vascular endothelial cell ...
Chuluyan, Hector Eduardo +3 more
core +1 more source
Crosstalk between the ribosome quality control‐associated E3 ubiquitin ligases LTN1 and RNF10
Loss of the E3 ligase LTN1, the ubiquitin‐like modifier UFM1, or the deubiquitinating enzyme UFSP2 disrupts endoplasmic reticulum–ribosome quality control (ER‐RQC), a pathway that removes stalled ribosomes and faulty proteins. This disruption may trigger a compensatory response to ER‐RQC defects, including increased expression of the E3 ligase RNF10 ...
Yuxi Huang +8 more
wiley +1 more source

