Vinconate, a cognitive enhancer, and PI turnover-phospholipase C systems in the brain

1997 ◽  
Vol 83 (1-2) ◽  
pp. 75-81
Author(s):  
Masashi Katsura ◽  
Toshiaki Iino ◽  
Jun Xu ◽  
Seitaro Ohkuma ◽  
Kinya Kuriyama
Keyword(s):  
Phospholipase C ◽  
Cognitive Enhancer ◽  
Pi Turnover ◽  
The Brain

scholarly journals High-Cholesterol Diet Decreases the Level of Phosphatidylinositol 4,5-Bisphosphate by Enhancing the Expression of Phospholipase C (PLCβ1) in Rat Brain

2020 ◽  
Vol 21 (3) ◽  
pp. 1161 ◽  
Author(s):  
Yoon Sun Chun ◽  
Sungkwon Chung
Keyword(s):  
Neurodegenerative Diseases ◽  
Rat Brain ◽  
Phospholipase C ◽  
Cultured Cells ◽  
Cell Interaction ◽  
High Cholesterol Diet ◽  
Cholesterol Diet ◽  
High Cholesterol ◽  
Amyloid Aβ ◽  
The Brain

Cholesterol is a critical component of eukaryotic membranes, where it contributes to regulating transmembrane signaling, cell–cell interaction, and ion transport. Dysregulation of cholesterol levels in the brain may induce neurodegenerative diseases, such as Alzheimer’s disease, Parkinson disease, and Huntington disease. We previously reported that augmenting membrane cholesterol level regulates ion channels by decreasing the level of phosphatidylinositol 4,5-bisphosphate (PIP2), which is closely related to β-amyloid (Aβ) production. In addition, cholesterol enrichment decreased PIP2 levels by increasing the expression of the β1 isoform of phospholipase C (PLC) in cultured cells. In this study, we examined the effect of a high-cholesterol diet on phospholipase C (PLCβ1) expression and PIP2 levels in rat brain. PIP2 levels were decreased in the cerebral cortex in rats on a high-cholesterol diet. Levels of PLCβ1 expression correlated with PIP2 levels. However, cholesterol and PIP2 levels were not correlated, suggesting that PIP2 level is regulated by cholesterol via PLCβ1 expression in the brain. Thus, there exists cross talk between cholesterol and PIP2 that could contribute to the pathogenesis of neurodegenerative diseases.

Two types of G proteins involved in regulation of phosphoinositide turnover in pulmonary endothelial cells

1991 ◽  
Vol 261 (4) ◽  
pp. 118-122 ◽  
Author(s):  
V. A. Tkachuk ◽  
T. A. Voyno-Yasenetskaya
Keyword(s):  
Endothelial Cells ◽  
Phospholipase C ◽  
G Proteins ◽  
Hormonal Regulation ◽  
Umbilical Vein ◽  
Dependent Manner ◽  
Hormone Regulation ◽  
Pi Turnover ◽  
Umbilical Vein Endothelial Cells ◽  
Stimulation Of

The involvement of G proteins in hormonal regulation of phospholipase C in bovine pulmonary arterial endothelial cells and human umbilical vein endothelial cells has been investigated. Histamine and bradykinin stimulated phosphoinositol (PI) turnover in a dose-dependent manner, and phorbol-myristate-acetate inhibited hormone-dependent activation of PI turnover, indicating a feedback control of this process. Activation of PI turnover by histamine and bradykinin is guanine nucleotide-dependent. Stimulation of the endothelial cell G proteins by guanosine 5'-0-(3-thiotriphosphate) leads to the potentiation of hormone-induced activation of PI turnover, whereas guanosine 5'-0-(2-thiodiphosphate), which inactivates G proteins, blocks the hormone-dependent PI turnover. Pertussis toxin blocked the histamine-dependent stimulation but did not affect the bradykinin-dependent stimulation of phospholipase C. By contrast, botulinurn toxin (C2 + C3 components) blocked the bradykinin-dependent stimulation of phospholipase C but did not affect the histamine-dependent stimulation of this enzyme. These data suggest that at least two different G proteins are involved in hormone-dependent stimulation of phospholipase C in endothelial cells. bacterial toxins; hormone regulation; phospholipase C

scholarly journals The Role of Phospholipase C in GABAergic Inhibition and Its Relevance to Epilepsy

2021 ◽  
Vol 22 (6) ◽  
pp. 3149
Author(s):  
Hye Yun Kim ◽  
Pann-Ghill Suh ◽  
Jae-Ick Kim
Keyword(s):  
Phospholipase C ◽  
Intracellular Signaling ◽  
Neuronal Development ◽  
Gabaergic Inhibition ◽  
Inhibitory Neurotransmitter ◽  
Intracellular Signaling Pathway ◽  
Key Enzyme ◽  
The Central Nervous System ◽  
Neuronal Functions ◽  
The Brain

Epilepsy is characterized by recurrent seizures due to abnormal hyperexcitation of neurons. Recent studies have suggested that the imbalance of excitation and inhibition (E/I) in the central nervous system is closely implicated in the etiology of epilepsy. In the brain, GABA is a major inhibitory neurotransmitter and plays a pivotal role in maintaining E/I balance. As such, altered GABAergic inhibition can lead to severe E/I imbalance, consequently resulting in excessive and hypersynchronous neuronal activity as in epilepsy. Phospholipase C (PLC) is a key enzyme in the intracellular signaling pathway and regulates various neuronal functions including neuronal development, synaptic transmission, and plasticity in the brain. Accumulating evidence suggests that neuronal PLC is critically involved in multiple aspects of GABAergic functions. Therefore, a better understanding of mechanisms by which neuronal PLC regulates GABAergic inhibition is necessary for revealing an unrecognized linkage between PLC and epilepsy and developing more effective treatments for epilepsy. Here we review the function of PLC in GABAergic inhibition in the brain and discuss a pathophysiological relationship between PLC and epilepsy.

Location-dependent role of phospholipase C signaling in the brain: Physiology and pathology

2020 ◽  
pp. 100771
Author(s):  
Isabella Rusciano ◽  
Maria Vittoria Marvi ◽  
Eric Owusu Obeng ◽  
Sara Mongiorgi ◽  
Giulia Ramazzotti ◽  
...  
Keyword(s):  
Phospholipase C ◽  
Brain Physiology ◽  
The Brain

Presence of pituitary adenylate cyclase-activating polypeptide 38-immuno-like material in the brain and ovary of the female crested newt, Triturus carnifex: its involvement in the ovarian synthesis of prostaglandins and steroids

1997 ◽  
Vol 152 (1) ◽  
pp. 141-146 ◽  
Author(s):  
A Gobbetti ◽  
M Zerani ◽  
A Miano ◽  
M Bramucci ◽  
O Murri ◽  
...  
Keyword(s):  
Adenylate Cyclase ◽  
Phospholipase C ◽  
Prostaglandin Synthesis ◽  
Prostaglandin E ◽  
Ovarian Steroidogenesis ◽  
Pituitary Adenylate Cyclase ◽  
Crested Newt ◽  
The Brain

Abstract The presence of pituitary adenylate cyclase-activating peptide (PACAP) 38-immuno-like material (PACAP 38-IL) in the brain and ovary of the crested newt, Triturus carnifex, and its action on ovarian steroidogenesis and prostaglandin synthesis were evaluated. The HPLC brain and ovary extract peaks that eluted like PACAP 38 were considered PACAP 38-like material. The concentrations of PACAP 38-IL in the HPLC extracts were measured by RIA. T. carnifex ovary was incubated with PACAP 38, brain and ovary PACAP 38-IL, and inhibitors of cyclooxygenase (COX), adenylate cyclase (AC) and phospholipase C (PLC) for 30 and 60 min. PACAP 38, and brain and ovary PACAP 38-IL increased prostaglandin E2 (PGE2) (30 and 60 min), and progesterone and corticosterone (60 min), but decreased oestradiol-17β (60 min). COX and PLC inhibitors counteracted the increases in PGE2, progesterone and corticosterone and the decrease in oestradiol-17β, and the AC inhibitor also counteracted them except for PGE2. These results suggest that PACAP 38-IL, present in T. carnifex brain and ovary, acts on PLC, inducing the increase of PGE2 which, in turn, acting on AC, induces increases in progesterone and corticosterone and a decrease in oestradiol-17β. Journal of Endocrinology (1997) 152, 141–146

Increased phospholipase C activity after experimental brain injury

1982 ◽  
Vol 56 (5) ◽  
pp. 695-698 ◽  
Author(s):  
Enoch P. Wei ◽  
Robert G. Lamb ◽  
Hermes A. Kontos
Keyword(s):  
Brain Injury ◽  
Phospholipase C ◽  
Prostaglandin Synthesis ◽  
Content Type ◽  
Free Arachidonic Acid ◽  
Membrane Bound ◽  
Cell Fractions ◽  
Cytidine Diphosphate ◽  
The Brain ◽  
Experimental Fluid

✓ Phospholipase C activity was measured in 1000 × G centrifuged cellular fractions isolated from cerebral cortical homogenates obtained from either control cats or cats subjected to experimental fluid-percussion brain injury. Phospholipase C activity was determined directly by measuring the Ca++-dependent conversion of membrane-bound, labeled phosphatidate to diacylglycerol or indirectly by measuring the diacylglycerol-dependent (brain diacylglycerol content) formation of phosphatidylcholine in the presence of labeled cytidine diphosphate (CDP) choline. Phospholipase C activity determined by either method was about two times greater in cell fractions isolated from animals subjected to brain injury than in controls (p < 0.01). The brain injury-induced rise in phospholipase C activity may be responsible, at least in part, for generating diacylglycerol that may be a source of free arachidonic acid that stimulates prostaglandin synthesis. These changes may account for the rise in brain prostaglandin levels that has been demonstrated earlier to occur after this type of brain injury.

scholarly journals Molecular cloning and characterization of a novel phospholipase C, PLC-η

2005 ◽  
Vol 389 (1) ◽  
pp. 181-186 ◽  
Author(s):  
Jong-Ik HWANG ◽  
Yong-Seok OH ◽  
Kum-Joo SHIN ◽  
Hyun KIM ◽  
Sung Ho RYU ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Phospholipase C ◽  
Neuronal Cell ◽  
Zona Incerta ◽  
Pleckstrin Homology Domain ◽  
Molecular Biological Analysis ◽  
Splicing Variants ◽  
The Brain

PLC (phospholipase C) plays an important role in intracellular signal transduction by hydrolysing phosphatidylinositol 4,5-bisphosphate, a membrane phospholipid. To date, 12 members of the mammalian PLC isoforms have been identified and classified into five isotypes β, γ, δ, ε and ζ, which are regulated by distinct mechanisms. In the present study, we describe the identification of a novel PLC isoform in the brains of human and mouse, named PLC-η, which contains the conserved pleckstrin homology domain, X and Y domains for catalytic activity and the C2 domain. The first identified gene encoded 1002 (human) or 1003 (mouse) amino acids with an estimated molecular mass of 115 kDa. The purified recombinant PLC-η exhibited Ca2+-dependent catalytic activity on phosphatidylinositol 4,5-bisphosphate. Furthermore, molecular biological analysis revealed that the PLC-η gene was transcribed to several splicing variants. Although some transcripts were detected in most of the tissues we examined, the transcript encoding 115 kDa was restricted to the brain and lung. In addition, the expression of the 115 kDa protein was defined in only nerve tissues such as the brain and spinal cord. In situ hybridization analysis with brain revealed that PLC-η was abundantly expressed in various regions including cerebral cortex, hippocampus, zona incerta and cerebellar Purkinje cell layer, which are neuronal cell-enriched regions. These results suggest that PLC-η may perform fundamental roles in the brain.

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