Inhibition of the phosphatidylinositol-specific phospholipase C from Bacillus cereus by a monoclonal antibody binding to a region with sequence similarity to eukaryotic phospholipases

Kuppe, A; Hedberg, Karen K.; Volwerk, Johannes J.; Griffith, O. Hayes

doi:10.1016/0005-2760(90)90258-y

Cited by 10 publications

(6 citation statements)

References 19 publications

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“…Moreover, the inhibition of the enzyme activity by anti-PLC antibodies totally disappears in competitive experiments when polyclonal PLC ␤1 and PLC ␤2 antibodies and the antigens they were raised against are used but not when the antigens corresponding to the other PLCs are used. This type of enzyme inhibition by selective antibodies against phosphoinositide-specific PLC has also been demonstrated in fresh bovine erythrocytes (34). One explanation of the noninhibiting effects of the other anti-PLC antibodies on the increase in [Ca 2ϩ ] i induced by the steroids may be that most antibodies do not classically inhibit enzyme activity.…”

Section: Effects Of Pertussis Toxin On the Intracellular Calcium Respmentioning

confidence: 88%

Phospholipase C β and Membrane Action of Calcitriol and Estradiol

Mellay

Grosse

Lieberherr

1997

Journal of Biological Chemistry

161

115

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We have shown that estrogens and calcitriol, the hormonally active form of vitamin D, increase the concentration of intracellular calcium ([Ca 2؉ ] i ) within 5 s by mobilizing calcium from the endoplasmic reticulum and the formation of inositol 1,4,5-trisphosphate and diacylglycerol. Because the activation of effectors as phospholipase C (PLC) coupled to G-proteins is the early event in the signal transduction pathway leading to the inositol 1,4,5-trisphosphate formation and to [Ca 2؉ ] i increase, we described different PLC isoforms (␤1, ␤2, ␥1, and ␥2, but not ␤4) in female rat osteoblasts using Western immunoblotting. The data showed that phospholipase C ␤ was involved in the mobilization of Ca 2؉ from the endoplasmic reticulum of Fura-2-loaded confluent osteoblasts by calcitriol and 17␤ estradiol, and PLC ␥ was ineffective. The data also showed that only a PLC ␤1 linked to a Pertussis toxin-insensitive G-protein and a PLC ␤2 coupled to a Pertussis toxin-sensitive G-protein are involved in the effects of calcitriol and 17␤ estradiol on the mobilization of Ca 2؉ from intracellular Ca 2؉ stores. In conclusion, these results may be an important step toward understanding membrane effects of these steroids and may be an additional argument in favor of membrane receptors to steroid hormones.An increase in the turnover of inositol lipids in response to receptor is one of the most important molecular mechanisms used by cells for transmembrane signaling. The initial event is the hydrolysis of phosphatidylinositol 4,5-bisphosphate, a reaction catalyzed by a phosphoinositide-specific phospholipase C (PLC), 1 which generates two intracellular second messengers, inositol 1,4,5-trisphosphate and 1,2-diacylglycerol (1-4). Inositol 1,4,5-trisphosphate binds to specific receptors on the endoplasmic reticulum (5) and mobilizes intracellular calcium, whereas diacylglycerol activates protein kinase C (6), which results in increased phosphorylation of cellular proteins.Molecular cloning has revealed at least three major families of PLC, ␤, ␥, and ␦ (7-9). Each of these families occurs in a number of isoforms. The enzymes are classified on the basis of their size and their immunological and structural similarities. The PLC isoforms have two highly conserved domains, X and Y, which form the active site of the protein. PLC ␦ and PLC ␥ proteins differ from PLC ␤ in that they have shorter C-terminal extensions past the end of the Y domain (9). This diversity among the PLC isoforms also extends to distinct mechanisms of regulation and function for the three PLC families. PLC ␥ is regulated via the phosphorylation of tyrosine residues between the X and Y domains by receptor tyrosine kinases (10 -12). PLC ␤ enzymes, of which there are four isoforms, PLC ␤1-4, are regulated via heterotrimeric G-proteins in response to an agonist binding to a receptor (13-15). The way in which PLC ␥ is regulated is not yet known, but enzyme activity is not affected by either the G-protein subunits or by receptor tyrosine kinases (16).The activat...

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Section: Effects Of Pertussis Toxin On the Intracellular Calcium Respmentioning

confidence: 88%

Phospholipase C β and Membrane Action of Calcitriol and Estradiol

Mellay

Grosse

Lieberherr

1997

Journal of Biological Chemistry

161

115

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“…PC-preferring and sphingomyelinase-encoding genes form a gene cluster (tandemly located) (59), which is not positioned in close proximity to the gene encoding phosphatidylinositol-specific PLC (59,96). The PCpreferring enzyme has structural homology to the C. perfringens alpha-toxin (103), while the phosphatidylinositol-specific enzyme has stretches of sequence homology to other eukaryotic phospholipases (97).…”

Section: Bacterial Phospholipasesmentioning

confidence: 99%

“…Interestingly, three regions surrounding these amino acids are also conserved in PLBs from fungi. The deduced amino acid sequence of caPLB2 contains the motifs SGGGX 97 RA(M/L), GL 133 SG(G/ S), and 381 D(S/G)G(E/L)XXXN, which may have a catalytic function (188).…”

Section: Phospholipases Of Candida Albicansmentioning

confidence: 99%

Potential Role of Phospholipases in Virulence and Fungal Pathogenesis

Ghannoum

2000

Clinical Microbiology Reviews

535

411

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“…There was 41% homology if conservative changes were considered. Moreover, this region involves a part of the X region, which is highly conserved among bacterial and eukaryotic PI-PLCs (36). The X region is supposedly involved in substrate binding.…”

Section: S Chromofuscus Pld Activity Towardmentioning

confidence: 99%

Activation of Phospholipase D by Phosphatidic Acid

Geng

Chura

Roberts

1998

Journal of Biological Chemistry

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The activity of bacterial phospholipase D (PLD), a Ca 2؉ -dependent enzyme, toward phosphatidylcholine bilayers was enhanced 7-fold by incorporation of 10 mol % phosphatidic acid (PA) in the vesicle bilayer. Addition of other negatively charged lipids such as phosphatidylinositol, phosphatidylmethanol, and oleic acid either inhibited or had no effect on enzyme activity. Only negatively charged lipids with a free phosphate group, phosphatidylinositol 4-phosphate and lyso-PA, had the same effect as PA on enzyme activity. Changes in vesicle curvature and fusion were not the reason for PA activation; rather, a metal ion-induced lateral segregation of PA in the vesicle bilayer correlated with PLD activation. Significant PA activation was also observed with monomer phosphatidylcholine substrate upon the addition of PA vesicles. The PA activation was caused by Ca 2؉ ⅐PA interacting with PLD at an allosteric site other than active site.

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Inhibition of the phosphatidylinositol-specific phospholipase C from Bacillus cereus by a monoclonal antibody binding to a region with sequence similarity to eukaryotic phospholipases

Cited by 10 publications

References 19 publications

Phospholipase C β and Membrane Action of Calcitriol and Estradiol

Phospholipase C β and Membrane Action of Calcitriol and Estradiol

Potential Role of Phospholipases in Virulence and Fungal Pathogenesis

Activation of Phospholipase D by Phosphatidic Acid

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