Multiple forms of phosphoinositide-specific phospholipase C and different modes of activation

Rhee, Sue Goo; Kim, Hyun; Suh, Pann‐Ghill; Choi, Won Chul

doi:10.1042/bst0190337

Cited by 98 publications

(66 citation statements)

References 3 publications

(3 reference statements)

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“…The PLC g family consists of PLC g 1 and g 2 . PLC g 1 is ubiquitously expressed (Rhee et al, 1991), whereas PLC g 2 expression is confined to the spleen and thymus (Emori et al, 1989). PLC g is regulated by receptors and nonreceptor tyrosine kinases (Rhee, 2001 Figure 2 Representative Western blots of PLC isozymes in membrane and cytosol fractions of the frontal cortex obtained from group C rats (given inescapable shock on day 1 and tested for escape latency on day 2; rats were again given shock on day 7 and tested for escape latency on day 8, and re-tested on day 14), comprised of TC, NLH, and LH rats.…”

Section: Discussionmentioning

confidence: 99%

Single and Repeated Stress-Induced Modulation of Phospholipase C Catalytic Activity and Expression: Role in LH Behavior

Dwivedi

Mondal

Rizavi

et al. 2004

Neuropsychopharmacol

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PI-PLC, a critical enzyme of the phosphoinositide (PI) signaling pathway, mediates many physiological functions in the brain, including cellular plasticity. Stress-induced learned helplessness (LH) in animals serves as a model of behavioral depression. Recently, we observed that repeated stress prolongs the duration of LH behavior in rats, enabling us to compare neurobiologic abnormalities in acute and chronic depression. Here we examine whether LH behavior is associated with alterations in phospholipase C (PLC), and whether repetition of inescapable shock has similar or dissimilar effects on PLC to those of the single-stress paradigm. Rats were exposed to inescapable shock either once on day 1, or twice, on days 1 and 7. Rats were tested for escape latency on days 2 and 4 after day 1 inescapable shock or on days 2, 8, and 14 after day 1 and 7 inescapable shock. PI-PLC activity and mRNA and protein expression of three different PLC isozymes were determined in the frontal cortex and hippocampus. Higher escape latencies were observed in LH rats tested on day 2 after single inescapable shock and on day 14 after repeated inescapable shock. Single inescapable shock reduced PI-PLC activity in the frontal cortex and hippocampus of LH rats. On the other hand, repeated inescapable shock not only reduced PI-PLC activity in these brain areas of LH rats but also selectively decreased the expression of PLC b 1 and PLC g 1 isozymes. Our results suggest different responsiveness at the level of PI-PLC after single vs repeated stress, and that reductions in PLC may be critical in the pathophysiology of depression and other stress-related disorders.

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Section: Discussionmentioning

confidence: 99%

Single and Repeated Stress-Induced Modulation of Phospholipase C Catalytic Activity and Expression: Role in LH Behavior

Dwivedi

Mondal

Rizavi

et al. 2004

Neuropsychopharmacol

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“…The mammalian PLC family comprises a related group of complex, modular, multi-domain enzymes that cover a broad spectrum of regulatory interactions, including direct binding to G protein subunits, small GTPases from Rho and Ras families, receptor and non-receptor tyrosine kinases, and lipid components of cellular membranes (11). PLC enzymes are thirteen isoforms classified on the basis of the amino acid sequence, domain structure, and mech-in testes and spermatic cell lines (12,13).…”

Section: Introductionmentioning

confidence: 99%

Comparison of Phosphoinositide-Specific Phospholipase C Expression Panels of Human Osteoblasts Versus MG-63 and Saos Osteoblast-Like Cells

Vasco¹,

Leopizzi²,

d’Abusco³

et al. 2016

Avicenna J Med Biochem

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Background: A large number of phospholipase C (PLC) enzymes, both mRNA transcripts and proteins, have been detected in osteoblasts, corroborating the importance of calcium regulation in bone tissue. MG-63 and SaOS-2 human osteosarcoma cell lines are actually considered osteoblast-like cells, and are therefore widely used as experimental models for osteoblasts. Objectives: Our aim was to verify whether MG-63 or SaOS-2 cells might also represent appropriate experimental osteoblast models for signal transduction studies, with special regard to the phosphoinositide (PI) pathway. We analyzed the expression and the subcellular distribution of enzymes related to calcium signal transduction (the PI-specific PLC family), which are known to possess high cell/tissue specificity. Materials and Methods:The expression of PLC genes was analyzed by performing RT-PCR experiments. The presence of PLC enzymes and their subcellular distribution within the cells was analyzed with immunofluorescence experiments. Results: Osteoblasts, MG-63 cells, and SaOS-2 cells have expression panels similar to those of PLC enzymes. However, slight differences were found in the expression of enzymes belonging to the PLCη subfamily. Conclusions: MG-63 and SaOS-2 osteosarcoma cell lines might not represent appropriate experimental models for studies that aim to analyze signal transduction in osteoblasts.

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“…2). Mo~t living cells contain several isozymes of PLC which differ in their structure and activity [1,2,4]. Three species of PLC were previously detected by gel filtration of neutrophil cytosol [28].…”

Section: Discussionmentioning

confidence: 99%

“…4) and was compatible with the size of/3 or y isozymes of PLC. PLC), I which undergoes phosphorylation on tyrosyl residues by the growth factor-stimulated kinase activity of the receptor has been detected in most living cells [4]. Moreover, in the promyelocytie leukemia HL-60 cells, which upon appropriate induction undergo maturation into cells that resemble neutrophils, PLCy and PLC/3 forms have been identified [4,27].…”

Section: Discussionmentioning

confidence: 99%

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Human neutrophil cytosolic phospholipase C: partial characterization

Faber¹,

Aviram²

1992

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metaboli

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The activity of n0utrophil cytosolic phospholipase C on PIP, and P! was compared employing ['~H]inositol-labeled heat-inactivated membranes of differentiated HL-60 cells, into which tracer ['~2P]PIP, was incorporated. Hydrolysis of PIP 2 did not require Ca -~+ and was stimulated when the content of PIP, in the i~embrane was increased by incorporation of unlabeled inositoi lipid. At equal concentrations of PI and PIP, in the membrane, hydrolysis of PIP~ was faster and no evidence of competition between the two substrates was obtained. Incorporation of P! into PE-[ "~-" P]PIP, vesicles, accelerated PIP e hydrolysis also at conditions that favor hydrolysis of PI. Partial purification of neutrophil cytosolic PLC on Q Sepharose, phenyl Sepharose and heparin-Agarose columns is described. From heparin-Agarose column, two PLC activity peaks exhibiting different substrate spccificities were elutcd. The elution profile of the main PLC species from Superose 12 gel filtration column was compatible with an approx. 150 kDa protein.

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Multiple forms of phosphoinositide-specific phospholipase C and different modes of activation

Cited by 98 publications

References 3 publications

Single and Repeated Stress-Induced Modulation of Phospholipase C Catalytic Activity and Expression: Role in LH Behavior

Single and Repeated Stress-Induced Modulation of Phospholipase C Catalytic Activity and Expression: Role in LH Behavior

Comparison of Phosphoinositide-Specific Phospholipase C Expression Panels of Human Osteoblasts Versus MG-63 and Saos Osteoblast-Like Cells

Human neutrophil cytosolic phospholipase C: partial characterization

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