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

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Query: EC:3.1.1.79 (hormone-sensitive lipase)
2,163 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A lectin like haemagglutinin (Human Seminal Lectin - HSL) is present in human seminal plasma. Partial purification and characterization of HSL has been achieved. HSL was shown to be almost completely inactivated at 100 degree C within 15 min. HSL was stable within a pH range of 5 to 10 for one hour, was resistant to trypsin, mercaptoethanol and dithiothreitol and has a molecular weight of about 57 000 daltons and an iso-electric point of about 6.8. HSL activity did not depend on either the incubation temperature or on the availability of free divalent cations such as Ca++,Mg++,or Mn++.
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PMID:Human seminal lectin. II. Properties of a lectin like factor in the human seminal plasma. 679 Apr 48

In Pseudomonas aeruginosa, many exoproduct virulence determinants are regulated via a hierarchical quorum-sensing cascade involving the transcriptional regulators LasR and RhlR and their cognate activators, N-(3-oxododecanoyl)-L-homoserine lactone (3O-C12-HSL) and N-butanoyl-L-homoserine lactone (C4-HSL). In this paper, we demonstrate that the cytotoxic lectins PA-IL and PA-IIL are regulated via quorum sensing. Using immunoblot analysis, the production of both lectins was found to be directly dependent on the rhl locus while, in a lasR mutant, the onset of lectin synthesis was delayed but not abolished. The PA-IL structural gene, lecA, was cloned and sequenced. Transcript analysis indicated a monocistronic organization with a transcriptional start site 70 bp upstream of the lecA translational start codon. A lux box-type element together with RpoS (sigma(S)) consensus sequences was identified upstream of the putative promoter region. In Escherichia coli, expression of a lecA::lux reporter fusion was activated by RhlR/C4-HSL, but not by LasR/3O-C12-HSL, confirming direct regulation by RhlR/C4-HSL. Similarly, in P. aeruginosa PAO1, the expression of a chromosomal lecA::lux fusion was enhanced but not advanced by the addition of exogenous C4-HSL but not 3O-C12-HSL. Furthermore, mutation of rpoS abolished lectin synthesis in P. aeruginosa, demonstrating that both RpoS and RhlR/C4-HSL are required. Although the C4-HSL-dependent expression of the lecA::lux reporter in E. coli could be inhibited by the presence of 3O-C12-HSL, this did not occur in P. aeruginosa. This suggests that, in the homologous genetic background, 3O-C12-HSL does not function as a posttranslational regulator of the RhlR/C4-HSL-dependent activation of lecA expression.
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PMID:The Pseudomonas aeruginosa lectins PA-IL and PA-IIL are controlled by quorum sensing and by RpoS. 1105 84

Posttranscriptional control is known to contribute to the regulation of secondary metabolism and virulence determinants in certain gram-negative bacteria. Here we report the isolation of a Pseudomonas aeruginosa gene which encodes a global translational regulatory protein, RsmA (regulator of secondary metabolites). Overexpression of rsmA resulted in a substantial reduction in the levels of extracellular products, including protease, elastase, and staphylolytic (LasA protease) activity as well as the PA-IL lectin, hydrogen cyanide (HCN), and the phenazine pigment pyocyanin. While inactivation of rsmA in P. aeruginosa had only minor effects on the extracellular enzymes and the PA-IL lectin, the production of HCN and pyocyanin was enhanced during the exponential phase. The influence of RsmA on N-acylhomoserine lactone-mediated quorum sensing was determined by assaying the levels of N-(3-oxododecanoyl)homoserine lactone (3-oxo-C12-HSL) and N-butanoylhomoserine lactone (C4-HSL) produced by the rsmA mutant and the rsmA-overexpressing strain. RsmA exerted a negative effect on the synthesis of both 3-oxo-C12-HSL and C4-HSL, which was confirmed by using lasI and rhlI translational fusions. These data also highlighted the temporal expression control of the lasI gene, which was induced much earlier and to a higher level during the exponential growth phase in an rsmA mutant. To investigate whether RsmA modulates HCN production solely via quorum-sensing control, hcn translational fusions were employed to monitor the regulation of the cyanide biosynthesis genes (hcnABC). RsmA was shown to exert an additional negative effect on cyanogenesis posttranscriptionally by acting on a region surrounding the hcnA ribosome-binding site. This suggests that, in P. aeruginosa, RsmA functions as a pleiotropic posttranscriptional regulator of secondary metabolites directly and also indirectly by modulating the quorum-sensing circuitry.
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PMID:The global posttranscriptional regulator RsmA modulates production of virulence determinants and N-acylhomoserine lactones in Pseudomonas aeruginosa. 1167 39

Pseudomonas aeruginosa regulates the production of many exoproteins and secondary metabolites via a hierarchical quorum-sensing cascade through LasR and RhlR and their cognate signal molecules N-(3-oxododecanoyl)-L-homoserine lactone (3O-C12-HSL) and N-(butanoyl)-L-homoserine lactone (C4-HSL). In this study, we found that transcription of the quorum sensing-regulated genes lecA (coding for PA-IL lectin), lasB (coding for elastase), and rpoS appeared to be growth phase dependent and their expression could not be advanced to the logarithmic phase in cells growing in batch culture by the addition of exogenous C4-HSL and 3O-C12-HSL. To identify novel regulators responsible for this growth phase dependency, a P. aeruginosa lecA::lux reporter strain was subjected to random transposon mutagenesis. A number of mutants affected in lecA expression were found that exhibited altered production of multiple quorum sensing-dependent phenotypes. While some mutations were mapped to new loci such as clpA and mvaT and a putative efflux system, a number of mutations were also mapped to known regulators such as lasR, rhlR, and rpoS. MvaT was identified as a novel global regulator of virulence gene expression, as a mutation in mvaT resulted in enhanced lecA expression and pyocyanin production. This mutant also showed altered swarming ability and production of the LasB and LasA proteases, 3O-C12-HSL, and C4-HSL. Furthermore, addition of exogenous 3O-C12-HSL and C4-HSL to the mvaT mutant significantly advanced lecA expression, suggesting that MvaT is involved in the growth phase-dependent regulation of the lecA gene.
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PMID:Advancing the quorum in Pseudomonas aeruginosa: MvaT and the regulation of N-acylhomoserine lactone production and virulence gene expression. 1197 83

In Pseudomonas aeruginosa, diverse exoproduct virulence determinants are regulated via N-acylhomoserine lactone-dependent quorum sensing. Here we show that 2-heptyl-3-hydroxy-4(1H)-quinolone (PQS) is also an integral component of the quorum sensing circuitry and is required for the production of rhl-dependent exoproducts at the onset of stationary phase. Analysis of spent P. aeruginosa culture supernatants revealed that PQS is produced at the end of exponential phase in the parent strain and in the late stationary phase of a lasR mutant. Mutants defective in both PQS production (pqsR-) and response (pqsE-) produced substantially reduced levels of exoproducts but retained wild-type N-butanoyl homoserine lactone (C4-HSL) levels. In the wild type, provision of exogenous PQS at the time of inoculation significantly increased PA-IL lectin, pyocyanin and elastase production during early stationary phase and promoted biofilm formation. Exogenous PQS but not PQS derivatives lacking the 3-hydroxy group overcame the cell density but not growth phase-dependent production of exoproducts. PQS also overcame the transcriptional and post-transcriptional repression of lecA (which codes for the PA-IL lectin) mediated via the negative regulators MvaT and RsmA respectively. Increased expression of lecA in the presence of exogenous PQS can be explained partially by increases in RhlR, RpoS and C4-HSL levels. A refined model for quorum sensing in P. aeruginosa is presented.
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PMID:The Pseudomonas aeruginosa quinolone signal molecule overcomes the cell density-dependency of the quorum sensing hierarchy, regulates rhl-dependent genes at the onset of stationary phase and can be produced in the absence of LasR. 1450 61

Pseudomonas aeruginosa is a serious pathogen involved in nosocomial infections. Its pathogenicity is owed to rich production of virulence factors (VIFs) regulated by several complex hierarchical signal systems depending on environmental conditions, medium composition, and the presence of certain active compounds in it. Choline (Ch), which exists in patient tissues, and ethanol (Et), whose consumption aggravates infections, were reported to augment this microbe virulence. The goal of the present study was to show the effect of Et addition to P. aeruginosa cultures in two media (minimal culture medium [MM] and Eagon-Grelet medium [EGM]) in the absence or presence of Ch on its VIF levels. In MM, Et sharply repressed the basal and Ch-induced levels of the P. aeruginosa lectins PA-IL (galactose-specific) and PA-IIL (fucose/mannose-binding) and proteolytic activities, while increasing C(6)-HSL (autoinducer), hemolytic phospholipase C (PLC-H), and phosphatase levels. In EGM, it profoundly increased lectin, protease, pyocyanin, rhamnolipid (RhaL), autoinducer, and slightly phosphatase levels, but reduced Ch-induced protease, PLC-H, and acid phosphatase activities, except the short-chain HSL levels, which were increased by Et in combination with Ch. The presented results enlighten part of the complex molecular basis of Et-induced aggravation of P. aeruginosa infections due to increasing the bacterium virulence, which runs in parallel to suppression of the patient's immunity.
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PMID:Ethanol effects on Pseudomonas aeruginosa lectin, protease, hemolysin, pyocyanin, autoinducer, and phosphatase levels depending on medium composition and choline presence. 1730 40

A novel lectin was purified from the coelomic fluid of the sea cucumber Holothuria scabra (HSL), subjected to bacterial challenge. HSL is a monomeric glycoprotein of molecular mass 182 kDa. The lectin is highly thermostable as it retains full activity for 1 h at 80 degrees C. Further, the hemagglutination activity of HSL is unaffected by pH in the range 2-11. Unlike other lectins purified from marine invertebrates, the hemagglutination activity of HSL does not require any divalent metal ions. The affinity profile of HSL was studied by a combination of hemagglutination inhibition and fluorescence spectroscopy. HSL binds to desialylated glycoproteins, MealphaGal, T-antigen and T (alpha-ser)-antigen with a distinction between beta1-4 and beta1-3 linkages. Mealpha-T-antigen was a potent ligand having highest affinity (Ka 8.32 x 10(7)M(-1)). Monosaccharide binding is enthalphically driven while disaccharide binding involves both entropic and enthalpic contributions.
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PMID:Purification and characterization of a T-antigen specific lectin from the coelomic fluid of a marine invertebrate, sea cucumber (Holothuria scabra). 1828 68

In invertebrates, cellular and humoral components are evolved to maintain their body immunity and integrity. Both these factors respond to different antigens such as microorganisms, vertebrate erythrocytes and foreign proteins. In this article, we report a study of a lectin (HSL) involved in immune response in the echinoderm, sea cucumber (Holothuria scabra). Correlative studies indicate that the expression of this defensive lectin is induced by bacterial challenge, wherein cell wall glycoconjugates of bacteria are involved in lectin induction. HSL showed strong broad spectrum antibacterial activity against both gram-positive and gram-negative bacteria. Under in vitro conditions, purified HSL mediate agglutination of the test bacteria, there by indicating a possible mode of action in physiological situation.
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PMID:T-antigen binding lectin with antibacterial activity from marine invertebrate, sea cucumber (Holothuria scabra): possible involvement in differential recognition of bacteria. 1850 24

Pseudomonas aeruginosa is a free-living bacterium and an important opportunistic pathogen. The genes coding for virulence-associated traits are regulated at the level of transcription by the quorum-sensing response. In this response, the regulator LasR coupled with the autoinducer 3-oxo-dodecanoyl homoserine lactone (3O-C12-HSL) activates transcription of genes for several virulence factors. LasR/3O-C12-HSL also activates transcription of rhlR, the gene coding for the transcriptional regulator RhlR, and of rhlI that encodes the synthase that produces the autoinducer butanoyl-homoserine lactone (C4-HSL) that interacts with RhlR. Genes activated by RhlR/C4-HSL include those involved in rhamnolipids production (like the rhlAB operon) and lecA, coding for PA-I lectin. The molecular basis of LasR/3O-C12-HSL- and RhlR/C4-HSLDNA-binding specificity (at the so-called las-boxes) has not been clearly determined, and the aim of this work was to contribute to its understanding. Therefore, we analyzed the interaction of LasR and RhlR to variants of the rhlA-las-box that were constructed based on the comparison of this las-box to the las-box of lecA. We conclude that LasR and RhlR DNA-binding specificity is a complex multifactorial phenomenon in which both positive and negative effects are involved and that binding of these proteins does not necessarily result in gene activation.
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PMID:The effect of specific rhlA-las-box mutations on DNA binding and gene activation by Pseudomonas aeruginosa quorum-sensing transcriptional regulators RhlR and LasR. 2493 61

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