Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.4.22.36 (
caspase-1
)
6,285
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The paper describes properties of proteases A and B isolated from the biological insecticide bitoxibacillin by sulphate precipitation and Sephadex G-75 gel filtration. Proteases A and B of bitoxibacillin belong to the neutral bacterial proteases. pH optimum was found to be 6.0 and 7.5 for detection of proteolytic activity of
protease A
and protease B, respectively. Thermal stability of proteases A and B was similar and increased by 25% upon addition of
CaCl2
. Both proteases were inhibited with EDTA. The molecular weight of proteases A and B was estimated to be 57,000 and 47,000, respectively.
...
PMID:[Partial purification and properties of proteases of bitoxibacillin]. 51 93
Calcium is involved in several steps of the apoptotic process. In nuclei, endonucleases are presumed to be the main targets of calcium; however, little is known about its role during the cytosolic phase of apoptosis. We used a cell-free system to address this question. Our results show that
CaCl2
triggered nuclear apoptosis (i.e. typical morphological change and DNA fragmentation) at concentrations of 5 mM. This concentration was lowered 10-fold by the co-incubation with cytosolic extracts from nonapoptotic cells. Apoptotic changes induced by the incubation of nuclei with
CaCl2
in the presence of these cytosols were strongly reduced in the presence of an inhibitor of caspase-3 and to a lesser extent by an inhibitor of
caspase-1
. We also show that calcium-induced apoptosis is affected by protease inhibitors such as N-tosyl-L-phenylalanine chloromethyl ketone, but not by calpain or several lysosomal protease inhibitors. The addition of
CaCl2
to the cell-free system increased a caspase-3 activity in nonapoptotic cytosols as shown by specific antibodies and an enzymatic assay. No activation of a caspase-3-like activity by the addition of cytochrome c was observed in these extracts under similar conditions. The enhanced caspase-3 activity induced by calcium was inhibited by protease inhibitors affecting morphological nuclear apoptosis except for those responsible for the degradation of lamin A. These results suggest that
CaCl2
could trigger, in normal cells, an apoptotic cascade through the activation of cytosolic caspase-3 activity.
...
PMID:Induction of a caspase-3-like activity by calcium in normal cytosolic extracts triggers nuclear apoptosis in a cell-free system. 965 49
