scholarly journals The molecular basis of phosphatidylcholine preference of human group-V phospholipase A2

2000 ◽  
Vol 348 (3) ◽  
pp. 643-647 ◽  
Author(s):  
Kwang Pyo KIM ◽  
Sang Kyou HAN ◽  
Mihae HONG ◽  
Wonhwa CHO
Keyword(s):  
Phospholipase A2 ◽  
Active Site ◽  
Molecular Basis ◽  
Mammalian Cells ◽  
Inflammatory Cells ◽  
Head Group ◽  
Human Group ◽  
Group V ◽  
Head Groups ◽  
Hydrolysis Of

Human group-V phospholipase A2 (hVPLA2) is a secretory phospholipase A2 (PLA2) that is involved in eicosanoid formation in such inflammatory cells as macrophages and mast cells. We showed that hVPLA2 can bind phosphatidylcholine membranes and hydrolyse phosphatidylcholine molecules much more efficiently than human group-IIa PLA2, which accounts for its high activity on the outer plasma membrane of mammalian cells. To understand the molecular basis of the high phosphatidylcholine specificity of hVPLA2, we mutated several residues (Gly-53, Glu-56 and Glu-57) that might be involved in interaction with an active-site-bound phospholipid molecule. Phospholipid head-group specificities of mutants determined using polymerized mixed-liposome substrates indicate that a small glycine residue in position 53 is important for accommodating a bulky choline head group. Also, results indicated that two anionic residues, Glu-56 and Glu-57, favourably interact with cationic head groups of phosphatidylcholine and phosphatidylethanolamine. Together, these steric and electrostatic properties of the active site of hVPLA2 allow for effective binding and hydrolysis of a bulky cationic choline head group of phosphatidylcholine, which is unique among mammalian secretory PLA2s.

scholarly journals The molecular basis of phosphatidylcholine preference of human group-V phospholipase A2

2000 ◽  
Vol 348 (3) ◽  
pp. 643 ◽  
Author(s):  
Kwang Pyo KIM ◽  
Sang Kyou HAN ◽  
Mihae HONG ◽  
Wonhwa CHO
Keyword(s):  
Phospholipase A2 ◽  
Molecular Basis ◽  
Human Group ◽  
Group V

scholarly journals Hydrolysis of three different head groups phospholipids by chicken group V phospholipase A2 using the monomolecular film technique

2020 ◽  
Vol 40 (1) ◽  
Author(s):  
Aida Karray ◽  
Madiha Bou Ali ◽  
Jallouli Raida ◽  
Bezzine Sofiane
Keyword(s):  
Phospholipase A2 ◽  
Hydrophobic Interactions ◽  
Electrostatic Potentials ◽  
Hydrolysis Rate ◽  
Head Group ◽  
Substrate Affinity ◽  
Head Groups ◽  
Surface Electrostatic Potentials ◽  
Hydrolysis Of ◽  
Long Chain

Abstract The kinetic aspects of lipolysis by pulmonary phospholipase A2 (ChPLA2-V), chicken intestinal phospholipase A2 (ChPLA2-IIA) and chicken pancreatic phospholipase A2 (ChPLA2-IB), from chicken have been compared using the monomolecular films technique, on short-chain phospholipids (with three different head groups) and on long-chain phospholipids. The main conclusions from our experimental data indicate that the maximum catalytic activities of ChPLA2-V on 1,2 phosphatidylcholine and 1,2 phosphatidylethanolamine reached 15.26 and 36.12 moles/cm2.min.mM, respectively, at a pressure of 15 and 35 dynes/cm, respectively. Whereas, those of ChPLA2-IB were 3.58 (at the pressure of 20 dynes/cm) and 4.9 moles/cm2.min.mM. However, hydrolysis of phosphatidylglycerol monolayers (C12PG), were very much higher compared with all the substrates tested with 122 moles/cm2.min. Surprisingly, the hydrolysis rate of ChPLA2-V on long-chain phosphatidylglycerol (C18PG) was very low (1.45 moles/cm2.min) compared with all tested substrates, even with the use of p-cyclodextrin. And thus, the fatty acid preference of ChPLA2-V was 2-decanoyl > 2-oleoyl with a PG head group. In order to gain significant correlations between enzyme’s structures and their relative functions, we tried to examine the surface electrostatic potentials of the various secreted phospholipase 2 (sPLA2) from chicken. In the present study, we detailed that the substrate affinity, specificity and the hydrolysis rates of sPLA2 at each interface is governed by the surface electrostatic potentials and hydrophobic interactions operative at this surface.

scholarly journals Group V Secreted Phospholipase A2 Is Upregulated by IL-4 in Human Macrophages and Mediates Phagocytosis via Hydrolysis of Ethanolamine Phospholipids

2015 ◽  
Vol 194 (7) ◽  
pp. 3327-3339 ◽  
Author(s):  
Julio M. Rubio ◽  
Juan P. Rodríguez ◽  
Luis Gil-de-Gómez ◽  
Carlos Guijas ◽  
María A. Balboa ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Group V ◽  
Human Macrophages ◽  
Secreted Phospholipase A2 ◽  
Hydrolysis Of

scholarly journals Mechanism of Human Group V Phospholipase A2(PLA2)-induced Leukotriene Biosynthesis in Human Neutrophils

2000 ◽  
Vol 276 (14) ◽  
pp. 11126-11134 ◽  
Author(s):  
Kwang Pyo Kim ◽  
John D. Rafter ◽  
Lenka Bittova ◽  
Sang Kyou Han ◽  
Yana Snitko ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Human Neutrophils ◽  
Human Group ◽  
Group V

scholarly journals Arginine 53 is involved in head-group specificity of the active site of porcine pancreatic phospholipase A2

1993 ◽  
Vol 213 (1) ◽  
pp. 517-522 ◽  
Author(s):  
Richard B. LUGTIGHEID ◽  
Maaike A. OTTEN-KUIPERS ◽  
Hubertus M. VERHEIJ ◽  
Gerard H. HAAS
Keyword(s):  
Phospholipase A2 ◽  
Active Site ◽  
Head Group ◽  
Pancreatic Phospholipase ◽  
Pancreatic Phospholipase A2 ◽  
Group Specificity

scholarly journals Group V and X secretory phospholipase A2 prevents adenoviral infection in mammalian cells

2005 ◽  
Vol 393 (1) ◽  
pp. 97-106 ◽  
Author(s):  
Michiko Mitsuishi ◽  
Seiko Masuda ◽  
Ichiro Kudo ◽  
Makoto Murakami
Keyword(s):  
Plasma Membrane ◽  
Phospholipase A2 ◽  
Mammalian Cells ◽  
Host Cells ◽  
Lung Fibroblasts ◽  
Secretory Phospholipase A2 ◽  
Group V ◽  
Adenoviral Infection ◽  
Secretory Phospholipase ◽  
Human Airway Epithelium

sPLA2 (secretory phospholipase A2) enzymes have been implicated in various biological events, yet their precise physiological functions remain largely unresolved. In the present study we show that group V and X sPLA2s, which are two potent plasma membrane-acting sPLA2s, are capable of preventing host cells from being infected with an adenovirus. Bronchial epithelial cells and lung fibroblasts pre-expressing group V and X sPLA2s showed marked resistance to adenovirus-mediated gene delivery in a manner dependent on their catalytic activity. Although adenovirus particles were insensitive to recombinant group V and X sPLA2s, direct addition of these enzymes to 293A cells suppressed both number and size of adenovirus plaque formation. Group V and X sPLA2s retarded the entry of adenovirus into endosomes. Moreover, adenoviral infection was suppressed by LPC (lysophosphatidylcholine), a membrane-hydrolytic product of these sPLA2s. Thus hydrolysis of the plasma membrane by these sPLA2s may eventually lead to the protection of host cells from adenovirus entry. Given that group V and X sPLA2s are expressed in human airway epithelium and macrophages and that the expression of endogenous group V sPLA2 is upregulated by virus-related stimuli in these cells, our present results raise the possibility that group V and X sPLA2s may play a role in innate immunity against adenoviral infection in the respiratory tract.

scholarly journals Roles of Trp31in High Membrane Binding and Proinflammatory Activity of Human Group V Phospholipase A2

1999 ◽  
Vol 274 (17) ◽  
pp. 11881-11888 ◽  
Author(s):  
Sang Kyou Han ◽  
Kwang Pyo Kim ◽  
Rao Koduri ◽  
Lenka Bittova ◽  
Nilda M. Munoz ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Membrane Binding ◽  
Human Group ◽  
Group V ◽  
Proinflammatory Activity
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