Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.4.3 (phospholipase C)
 18,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The ability of Listeria monocytogenes to move within the cytosol of infected cells and their ability to infect adjacent cells is important in the development of infection foci leading to systemic disease. Interaction with the host cell microfilament system, particularly actin, appears to be the basis for propelling the bacteria through the host cell cytoplasm to generate the membraneous protrusions whereby cell-to-cell spread occurs. The actA locus of L.monocytogenes encodes a 90 kDa polypeptide that is a key component of bacterium-host cell microfilament interactions. Cloning of the actA gene allowed the identification of its gene product and permitted construction of an isogenic mutant strain defective in the production of the ActA polypeptide. Sequencing of the region encoding the actA gene revealed that it was located region encoding the actA gene revealed that it was located between the metalloprotease (mpl) and phosphatidylcholine-specific phospholipase C (plcB) genes. Within the cytoplasm of the infected cells, the mutant strain grew as microcolonies, was unable to accumulate actin following escape from the phagocytic compartment and was incapable of infecting adjacent cells. It was also dramatically less virulent, demonstrating that the capacity to move intracellularly and spread intercellularly is a key determinant of L.monocytogenes virulence. Like all other virulence factors described for this microorganism, expression of the ActA polypeptide is controlled by the PrfA regulator protein. The primary sequence of this protein appeared to be unique with no extended homology to known protein sequences. However, an internal repeat sequence showed strong regional homology to a sequence from within the hinge region of the cytoskeletal protein vinculin.
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PMID:A novel bacterial virulence gene in Listeria monocytogenes required for host cell microfilament interaction with homology to the proline-rich region of vinculin. 158 25

Pseudomonas aeruginosa is an opportunistic pathogen whose adaptability, ubiquitousness, and pathogenicity are closely related. Both cell-associated and extracellular products of P. aeruginosa contribute to its virulence. Surface structures, including pili and the polysaccharide capsule or glycocalyx, appear to mediate the initial attachment of P. aeruginosa to its prospective host, thus permitting colonization. Extracellular enzymes such as alkaline protease, elastase, phospholipase C, and exotoxin A degrade infected tissues and promote bacterial invasion. When dissemination occurs, systemic disease results, often with fatal consequences. Although extracellular enzymes of P. aeruginosa figure prominently in local disease processes, exotoxin A and endotoxin are primarily responsible for systemic disease. The most protective antibodies presently known are directed toward the nontoxic portions of P. aeruginosa lipopolysaccharides that serve no known virulence function per se. However, there is preliminary evidence that the protective activity of these opsonic antibodies may be augmented by toxin-neutralizing antibodies directed toward the lipid A moiety of endotoxin and exotoxin A.
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PMID:The virulence of Pseudomonas aeruginosa. 644 64

Phosphoinositide-specific phospholipase C (PLC) is a key enzyme in signal transduction. We have previously demonstrated that a PLC isozyme is abnormally accumulated in the brain tissue in Alzheimer's disease (AD). AD has been suggested to be a systemic disease in which the expression of abnormalities is most prominent in neuronal tissues. In a recent study, we have revealed the increase of the cytosolic protein kinase C (PKC) concentration in platelets of AD patients, suggesting the change of PLC, which is upstream to PKC in phosphoinositide metabolism. In this study, we examined phosphatidylinositol-specific PLC activity in platelets from patients with AD and age-matched controls by measuring the formation of radioactive inositol phosphate. The PLC activity was significantly lower in the AD platelets than in the controls. These findings suggest that aberrant phosphoinositide metabolism is present in nonneuronal tissues as well as the brain in AD.
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PMID:Reduction of platelet phospholipase C activity in patients with Alzheimer disease. 874 10