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Thematische Bibliographien / Phospholipase A2 (sPLA2)

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Zeitschriftenartikel

Auswahl der wissenschaftlichen Literatur zum Thema „Phospholipase A2 (sPLA2)“

Autor: Grafiati

Veröffentlicht am 18. Mai 2024

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Zeitschriftenartikel zum Thema "Phospholipase A2 (sPLA2)"

1

Themsche, Céline Van, Michèle Jacob, and Christian Salesse. "Human retinal pigment epithelium secretes a phospholipase A2 and contains two novel intracellular phospholipases A2." Biochemistry and Cell Biology 79, no. 1 (2001): 1–10. http://dx.doi.org/10.1139/o00-088.

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The sensitivity of different phospholipase A2 (PLA2)-active fractions eluted from cation-exchange chromatography to para-bromophenacylbromide (pBPB), Ca2+-EGTA, DTT, heat, and H2SO4 indicates that human cultured retinal pigment epithelial (hRPE) cells probably contain two different intracellular PLA2 enzymes. Control experiments using "back-and-forth" thin-layer chromatography confirmed that, in our assay conditions, the generation of free fatty acids originated solely from PLA2 activity. Together with immunoblot experiments where no cross-reactivity was observed between the hRPE cytosolic PLA

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2

Rizzo, Maria Teresa, Elisabeth Nguyen, Marlene Aldo-Benson, and Gerard Lambeau. "Secreted phospholipase A2 induces vascular endothelial cell migration." Blood 96, no. 12 (2000): 3809–15. http://dx.doi.org/10.1182/blood.v96.12.3809.

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Abstract Secreted phospholipase A2 (sPLA2) regulates a variety of cellular functions. The present investigation was undertaken to elucidate the potential role of sPLA2 in endothelial cell (EC) migration. Bovine aortic endothelial cells (BAECs) exposed to sPLA2 placed in the lower compartment of a modified Boyden chamber displayed increased migration compared to cells exposed to vehicle. The effect of sPLA2 on EC migration was time and dose dependent. Migration of BAECs was observed at 30 minutes, increased over 1 to 2 hours, and declined thereafter. At 2 hours of stimulation, sPLA2 (0.01-2 μmo

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3

Rizzo, Maria Teresa, Elisabeth Nguyen, Marlene Aldo-Benson, and Gerard Lambeau. "Secreted phospholipase A2 induces vascular endothelial cell migration." Blood 96, no. 12 (2000): 3809–15. http://dx.doi.org/10.1182/blood.v96.12.3809.h8003809_3809_3815.

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Secreted phospholipase A2 (sPLA2) regulates a variety of cellular functions. The present investigation was undertaken to elucidate the potential role of sPLA2 in endothelial cell (EC) migration. Bovine aortic endothelial cells (BAECs) exposed to sPLA2 placed in the lower compartment of a modified Boyden chamber displayed increased migration compared to cells exposed to vehicle. The effect of sPLA2 on EC migration was time and dose dependent. Migration of BAECs was observed at 30 minutes, increased over 1 to 2 hours, and declined thereafter. At 2 hours of stimulation, sPLA2 (0.01-2 μmol/L) indu

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4

Shridas, Preetha, and Nancy R. Webb. "Diverse Functions of Secretory Phospholipases A2." Advances in Vascular Medicine 2014 (July 15, 2014): 1–11. http://dx.doi.org/10.1155/2014/689815.

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Phospholipase A2 enzymes (PLA2s) catalyze the hydrolysis of glycerophospholipids at their sn-2 position releasing free fatty acids and lysophospholipids. Mammalian PLA2s are classified into several categories of which important groups include secreted PLA2s (sPLA2s) and cytosolic PLA2s (cPLA2s) that are calcium-dependent for their catalytic activity and calcium-independent cytosolic PLA2s (iPLA2s). Platelet-activating factor acetylhydrolases (PAF-AHs), lysosomal PLA2s, and adipose-specific PLA2 also belong to the class of PLA2s. Generally, cPLA2 enzymes are believed to play a major role in the

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5

Wei, Yulong, Lesan Yan, Lijun Luo, et al. "Phospholipase A2 inhibitor–loaded micellar nanoparticles attenuate inflammation and mitigate osteoarthritis progression." Science Advances 7, no. 15 (2021): eabe6374. http://dx.doi.org/10.1126/sciadv.abe6374.

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Treating osteoarthritis (OA) remains a major clinical challenge. Despite recent advances in drug discovery and development, no disease-modifying drug for knee OA has emerged with any notable clinical success, in part, due to the lack of valid and responsive therapeutic targets and poor drug delivery within knee joints. In this work, we show that the amount of secretory phospholipase A2 (sPLA2) enzyme increases in the articular cartilage in human and mouse OA cartilage tissues. We hypothesize that the inhibition of sPLA2 activity may be an effective treatment strategy for OA. To develop an sPLA

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6

Taketomi, Yoshitaka, Yoshimi Miki, and Makoto Murakami. "Old but New: Group IIA Phospholipase A2 as a Modulator of Gut Microbiota." Metabolites 12, no. 4 (2022): 352. http://dx.doi.org/10.3390/metabo12040352.

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Among the phospholipase A2 (PLA2) superfamily, the secreted PLA2 (sPLA2) family contains 11 mammalian isoforms that exhibit unique tissue or cellular distributions and enzymatic properties. Current studies using sPLA2-deficient or -overexpressed mouse strains, along with mass spectrometric lipidomics to determine sPLA2-driven lipid pathways, have revealed the diverse pathophysiological roles of sPLA2s in various biological events. In general, individual sPLA2s exert their specific functions within tissue microenvironments, where they are intrinsically expressed through hydrolysis of extracellu

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7

Hite, R. Duncan, Michael C. Seeds, Randy B. Jacinto, R. Balasubramanian, Moseley Waite, and David Bass. "Hydrolysis of surfactant-associated phosphatidylcholine by mammalian secretory phospholipases A2." American Journal of Physiology-Lung Cellular and Molecular Physiology 275, no. 4 (1998): L740—L747. http://dx.doi.org/10.1152/ajplung.1998.275.4.l740.

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Hydrolysis of surfactant-associated phospholipids by secretory phospholipases A2 is an important potential mechanism for surfactant dysfunction in inflammatory lung diseases. In these conditions, airway secretory phospholipase A2(sPLA2) activity is increased, but the type of sPLA2 and its impact on surfactant function are not well understood. We examined in vitro the effect of multiple secretory phospholipases A2 on surfactant, including their ability to 1) release free fatty acids, 2) release lysophospholipids, and 3) increase the minimum surface tension (γmin) on a pulsating bubble surfactom

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8

Krizaj, Igor. "Roles of Secreted Phospholipases A2 in the Mammalian Immune System." Protein & Peptide Letters 21, no. 12 (2014): 1201–8. http://dx.doi.org/10.2174/0929866521666140819122624.

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Secreted phospholipase A2 (sPLA2) molecules constitute a family of proteins that are involved functionally in many biological processes. In particular, they participate in diverse pathophysiological settings as enzymes that release free fatty acids and lysophospholipids from phospholipids in biological membranes, or as ligands for various cellular receptors. In this review the confirmed or expected functions of sPLA2s in the mammalian immune system are surveyed. Some of the twelve mammalian sPLA2 molecules constitute part of the so-called innate immune system by virtue of their antibacterial,

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9

Wong, Dennis A., Yoshihiro Kita, Naonori Uozumi та Takao Shimizu. "Discrete Role for Cytosolic Phospholipase A2α in Platelets". Journal of Experimental Medicine 196, № 3 (2002): 349–57. http://dx.doi.org/10.1084/jem.20011443.

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Among several different types of phospholipase A2 (PLA2), cytosolic PLA2 (cPLA2)α and group IIA (IIA) secretory PLA2 (sPLA2) have been studied intensively. To determine the discrete roles of cPLA2α in platelets, we generated two sets of genetically engineered mice (cPLA2α−/−/sPLA2-IIA−/− and cPLA2α−/−/sPLA2-IIA+/+) and compared their platelet function with their respective wild-type C57BL/6J mice (cPLA2α+/+/sPLA2-IIA−/−) and C3H/HeN (cPLA2α+/+/sPLA2-IIA+/+). We found that cPLA2α is needed for the production of the vast majority of thromboxane (TX)A2 with collagen stimulation of platelets. In c

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10

Hite, R. Duncan, Michael C. Seeds, Anca M. Safta, et al. "Lysophospholipid generation and phosphatidylglycerol depletion in phospholipase A2-mediated surfactant dysfunction." American Journal of Physiology-Lung Cellular and Molecular Physiology 288, no. 4 (2005): L618—L624. http://dx.doi.org/10.1152/ajplung.00274.2004.

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Pulmonary surfactant's complex mixture of phospholipids and proteins reduces the work of breathing by lowering alveolar surface tension during respiration. One mechanism of surfactant damage appears to be the hydrolysis of phospholipid by phospholipases activated in the inflamed lung. Humans have several candidate secretory phospholipase A2 (sPLA2) enzymes in lung cells and infiltrating leukocytes that could damage extracellular surfactant. We considered two mechanisms of surfactant disruption by five human sPLA2s, including generation of lysophospholipids and the depletion of specific phospho

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