Structural views of phosphoinositide-specific phospholipase C: signalling the way ahead

Williams, Roger L.; Katan, Matilda

doi:10.1016/s0969-2126(96)00146-3

Cited by 71 publications

(50 citation statements)

References 78 publications

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“…cells and was attributed to an endogenous phospholipase activity (Svetek et al, 1999). Cleavage of the GPI anchor by endogenous (glycosyl) phosphatidylinositol-specific phospholipases C or D, which are known to depend on divalent cations in other systems, is thus likely to be responsible for the shedding of both Sl3-MMP and arabinogalactan proteins (Bütikofer and Brodbeck, 1993;Li et al, 1994;Williams and Katan, 1996;Oxley and Bacic, 1999).…”

Section: Cloning Of Sl2-mmp and Sl3-mmpmentioning

confidence: 99%

Cell death control by matrix metalloproteinases in tomato

et al. 2016

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In contrast to mammalian matrix metalloproteinases (MMPs) that play important roles in the remodeling of the extracellular matrix in animals, the proteases responsible for dynamic modifications of the plant cell wall are largely unknown. A possible involvement of MMPs was addressed by cloning and functional characterization of Sl2-MMP and Sl3-MMP from tomato (Solanum lycopersicum). The two tomato MMPs were found to resemble mammalian homologs with respect to gelatinolytic activity, substrate preference for hydrophobic amino acids on both sides of the scissile bond, and catalytic properties. In transgenic tomato seedlings silenced for Sl2/3-MMP expression, necrotic lesions were observed at the base of the hypocotyl. Cell death initiated in the epidermis and proceeded to include outer cortical cell layers. In later developmental stages, necrosis spread, covering the entire stem and extending into the leaves of MMP-silenced plants. The subtilisin-like protease P69B was identified as a substrate of Sl2-and Sl3-MMP. P69B was shown to colocalize with Sl-MMPs in the apoplast of the tomato hypocotyl, it exhibited increased stability in transgenic plants silenced for Sl-MMP activity, and it was cleaved and inactivated by Sl-MMPs in vitro. The induction of cell death in Sl2/3-MMP-silenced plants depended on P69B, indicating that Sl2-and Sl3-MMP act upstream of P69B in an extracellular proteolytic cascade that contributes to the regulation of cell death in tomato.

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Section: Cloning Of Sl2-mmp and Sl3-mmpmentioning

confidence: 99%

Cell death control by matrix metalloproteinases in tomato

et al. 2016

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“…Crystallographic analysis also showed that the EF hand domain does not bind Ca 2ϩ but rather serves as a flexible link between the PH domain and the rest of the enzyme. 23,24 However, it was recently demonstrated that the EF hand domain of PLC-␦1 binds Ca 2ϩ and it is necessary for the efficient interaction of the PH domain with PIP 2 . 25 Thus, the 864G-A variant of PLC-␦1 found in this study seems to contribute to the altered enzyme activity induced by Ca 2ϩ .…”

Section: Nakano Et Al Phospholipase C-␦1 Variant In Coronary Spasm 2027mentioning

confidence: 99%

Enhanced Activity of Variant Phospholipase C-δ1 Protein (R257H) Detected in Patients With Coronary Artery Spasm

et al. 2002

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Background-We recently demonstrated that phospholipase C (PLC)-␦1 activity in cultured skin fibroblasts obtained from patients with coronary spastic angina (CSA) is enhanced. We tested the hypothesis that structural abnormality in PLC-␦1 isoform is a cause of the enhanced activity. Methods and Results-Sequence analysis of the cDNA coding for PLC-␦1 obtained from fibroblasts revealed that one conversion of guanine to adenine (A) was present at nucleotide position 864 in one CSA patient, resulting in the amino acid replacement of arginine 257 by histidine (R257H). The incidence of 864A/A in genomic DNA, analyzed by single-strand conformation polymorphism, was greater in patients with CSA than in male control subjects (6 of 57 patients with CSA versus 1 of 62 control subjects, PϽ0.05). The activity of the variant PLC-␦1 protein under free calcium concentration between 10 Ϫ8 and 10 Ϫ7 mol/L was 2-fold higher than that of the wild-type protein. Baseline intracellular calcium concentration ([Ca 2ϩ ] i ) in human embryonic kidney 293 cells transfected with the variant PLC-␦1 was higher than that in cells with the wild type. The peak increase in [Ca 2ϩ ] i in response to acetylcholine at 10 Ϫ6 and 10 Ϫ5 mol/L was greater in the cells with the variant PLC-␦1 than in those with the wild type. Conclusions-These findings indicate that the R257H variant in the PLC-␦1 gene detected in patients with CSA is associated with enhancement of enzyme activity, and they describe a novel mechanism for the enhanced coronary vasomotility in

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“…Phosphoinositide-specific phospholipase C (PLC) enzymes catalyze the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP 2 ) to inositol 1,4,5-triphosphate and diacylglycerol, key regulators of cellular responses (Williams and Katan, 1996). Overexpression of PLC in tumors with high receptor activity results in increased intracellular free Ca 2ϩ and cell proliferation (Piccolo et al, 2002;Wells and Grandis, 2003).…”

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confidence: 99%