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Major insights into action pathways of bacterial phospholipases have been provided during the last years.
2
Recovery of lung phospholipases occurred despite continuous treatment.
3
None of the deduced protein sequences contain N-terminal signal peptides, suggesting that these phospholipases are not secreted.
4
In particular, the PI-selective enzyme may represent a new member of the growing family of cytoplasmic phospholipases A2.
5
They are rapidly formed in response to a variety of stimuli via the activation of lipid kinases or phospholipases.
6
Therefore, when those enzymes are injected or secreted by the bacterium into the host cell they may mimic eukaryotic phospholipases.
7
In this system, the phospholipases C and A2 are coupled to two classes of muscarinic receptors that display a different sensitivity to pertussis toxin.
8
Reaction products of bacterial phospholipases may potentially influence many more host cell processes, such as cell respreading, lamellopodia formation, cell migration and membrane traffic.
9
Phospholipases play a dominant role in the biology of the lung pathogen Legionella pneumophila.
10
Phospholipases are a diverse class of enzymes produced both by eukaryotic hosts and their pathogens.
11
Phospholipases A and C were measured in lysosomal soluble fractions of lavaged lung and sonicated lung lavage cells.
12
Phospholipases C are known to be important regulators of cellular processes but may also act as virulence factors of pathogenic microbes.
13
These receptors were phospholipase C-coupled and had appropriate ligand affinity and specificity.
14
The phospholipase A2 molecules interact extensively with each other in the crystalline state.
15
Fluorescence microscopy with fura-2 revealed that phospholipase C increased systolic-free calcium.
16
Sphingosine did not activate phospholipase D activity significantly after 10 min.