Analysis of expression of secreted phospholipases A2 in mouse tissues at protein and mRNA levels

Eerola, Leena I.; Surrel, Fanny; Nevalainen, Timo J.; Gelb, Michael H.; Lambeau, Gérard; Laine, V.

doi:10.1016/j.bbalip.2006.04.002

Cited by 47 publications

(51 citation statements)

References 82 publications

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“…Although several sPLA 2 s are present in mouse male reproductive organs (16), we did not detect mGIIA, mGIID, mGIIE, mGIIF, and mGV sPLA 2 proteins in mature mouse sperm, while the expression of mGX was very high, with several nanograms of mGX protein per million sperm. This value appears very high when compared with the level of mGX protein in various mouse tissues (56) and fits with the very high level of mGX mRNA in testis versus other tissues (57). Our finding is important, since there have been numerous biochemical reports during the past 40 years showing the presence of an sPLA 2 protein in sperm from several mammalian species, the molecular identity of which was never clarified (19,(27)(28)(29).…”

Section: Discussionsupporting

confidence: 78%

“…This result suggests that mGX is also present in the female tract and may compensate for the deficit of mGX in sperm. This view is supported by our preliminary data showing the presence of mGX sPLA 2 in the female reproductive tract, notably in the uterine epithelium (56). Similar observations have been made for iPLA 2 β-deficient mice, where crossings between iPLA 2 β-deficient males and females produced no offspring, while crossings between iPLA 2 β-deficient males and WT females did produce offspring, though at less than the normal rate (18).…”

Section: Figuresupporting

confidence: 86%

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Group X phospholipase A2 is released during sperm acrosome reaction and controls fertility outcome in mice

Escoffier¹,

Jemel²,

Tanemoto³

et al. 2010

J. Clin. Invest.

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100

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Ejaculated mammalian sperm must undergo a maturation process called capacitation before they are able to fertilize an egg. Several studies have suggested a role for members of the secreted phospholipase A 2 (sPLA 2 ) family in capacitation, acrosome reaction (AR), and fertilization, but the molecular nature of these enzymes and their specific roles have remained elusive. Here, we have demonstrated that mouse group X sPLA 2 (mGX) is the major enzyme present in the acrosome of spermatozoa and that it is released in an active form during capacitation through spontaneous AR. mGX-deficient male mice produced smaller litters than wild-type male siblings when crossed with mGX-deficient females. Further analysis revealed that spermatozoa from mGX-deficient mice exhibited lower rates of spontaneous AR and that this was associated with decreased in vitro fertilization (IVF) efficiency due to a drop in the fertilization potential of the sperm and an increased rate of aborted embryos. Treatment of sperm with sPLA 2 inhibitors and antibodies specific for mGX blocked spontaneous AR of wild-type sperm and reduced IVF success. Addition of lysophosphatidylcholine, a catalytic product of mGX, overcame these deficiencies. Finally, recombinant mGX triggered AR and improved IVF outcome. Taken together, our results highlight a paracrine role for mGX during capacitation in which the enzyme primes sperm for efficient fertilization and boosts premature AR of a likely phospholipid-damaged sperm subpopulation to eliminate suboptimal sperm from the pool available for fertilization.

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Section: Discussionsupporting

confidence: 78%

Section: Figuresupporting

confidence: 86%

Group X phospholipase A2 is released during sperm acrosome reaction and controls fertility outcome in mice

Escoffier¹,

Jemel²,

Tanemoto³

et al. 2010

J. Clin. Invest.

Self Cite

100

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“…However, these transgenic mice are artificial models with constitutive overexpression of sPLA2-IIA (36). Moreover, mice are known to exhibit no or very low sPLA2-IIA expression in the lung (37). Therefore, we used guinea pigs as animal model known to produce high pulmonary levels of sPLA2-IIA (18,30).…”

Section: Discussionmentioning

confidence: 99%

Staphylococcus aureus Adenosine Inhibits sPLA2-IIA–Mediated Host Killing in the Airways

Pernet

Brunet

Guillemot

et al. 2015

The Journal of Immunology

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Staphylococcus aureus is a common cause of bacterial infections in respiratory diseases. It secretes molecules to dampen host immunity, and the recently identified adenosine is one of these molecules. The type IIA secretory phospholipase A2 (sPLA2-IIA) is a host protein endowed with antibacterial properties, especially against Gram-positive bacteria such as S. aureus. However, the role of adenosine in sPLA2-IIA–mediated S. aureus killing by host is still unknown. The present studies showed that the S. aureus mutant lacking adenosine production (∆adsA strain) increased sPLA2-IIA expression in guinea pig airways and was cleared more efficiently, compared with the wild-type strain. S. aureus ∆adsA strain induced sPLA2-IIA expression by alveolar macrophages after phagocytic process via NOD2–NF-κB–dependent mechanism. However, S. aureus adenosine (wild-type and adsA-complemented strains) and exogenous adenosine downregulated S. aureus phagocytosis by alveolar macrophages, leading to inhibition of sPLA2-IIA expression. This occurred through inhibition of p38 phosphorylation via adenosine receptors A2a-, A2b-, and protein kinase A–dependent pathways. Taken together, our studies suggest that, in the airway, S. aureus escapes sPLA2-IIA–mediated killing through adenosine-mediated inhibition of phagocytosis and sPLA2-IIA expression.

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“…cPLA 2 is activated by infl ux of Ca 2+ into the cell ( 232 ) and is subject to glucose-mediated phosphorylation ( 235 ). A variety of sPLA 2 s (1B, IIC, IIF, XIIA/B) have also been described in whole pancreas ( 236 ), islets ( 233,234,237 ), and in ␤ -cell secretory granules ( 234,238,239 ) from which sPLA 2 -1B is co-released with insulin ( 236 ). When observations from these studies are taken together, a sequential participation of PLA 2 s in the insulin secretory process is suggested.…”

Section: +mentioning

confidence: 99%

Calcium-independent phospholipases A2 and their roles in biological processes and diseases

Ramanadham

Ali

Ashley

et al. 2015

Journal of Lipid Research

169

190

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The Ca 2+ -independent phospholipases A 2 (iPLA 2 s) are part of a diverse family of PLA 2 s that hydrolyze the sn -2 substituent from membrane phospholipids to release a free fatty acid and a lysolipid ( 1, 2 ). These enzymes are ubiquitously expressed, and in contrast to secretory PLA 2 s (sPLA 2 s) and cytosolic PLA 2 s (cPLA 2 s), do not require Ca 2+ for either translocation or activity. Some of the fi rst descriptions of iPLA 2 activity were in the mid-to late-1980s with the identifi cation of a plasmalogen-selective PLA 2 in Abstract Among the family of phospholipases A 2 (PLA 2 s) are the Ca 2+ -independent PLA 2 s (iPLA 2 s) and they are designated group VI iPLA 2 s. In relation to secretory and cytosolic PLA 2 s, the iPLA 2 s are more recently described and details of their expression and roles in biological functions are rapidly emerging. The iPLA 2 s or patatin-like phospholipases (PNPLAs) are intracellular enzymes that do not require Ca 2+ for activity, and contain lipase (GXSXG) and nucleotide-binding (GXGXXG) consensus sequences. Though nine PNPLAs have been recognized, PNPLA8 (membraneassociated iPLA 2 ␥ ) and PNPLA9 (cytosol-associated iPLA 2 ␤ ) are the most widely studied and understood. The iPLA 2 s manifest a variety of activities in addition to phospholipase, are ubiquitously expressed, and participate in a multitude of biological processes, including fat catabolism, cell differentiation, maintenance of mitochondrial integrity, phospholipid remodeling, cell proliferation, signal transduction, and cell death. As might be expected, increased or decreased expression of iPLA 2 s can have profound effects on the metabolic state, CNS function, cardiovascular performance, and cell survival; therefore, dysregulation of iPLA 2 s can be a critical factor in the development of many diseases. This review is aimed at providing a general framework of the current understanding of the iPLA 2 s and discussion of the potential mechanisms of action of the iPLA 2 s and related involved lipid mediators. -Ramanadham, S

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Analysis of expression of secreted phospholipases A2 in mouse tissues at protein and mRNA levels

Cited by 47 publications

References 82 publications

Group X phospholipase A2 is released during sperm acrosome reaction and controls fertility outcome in mice

Group X phospholipase A2 is released during sperm acrosome reaction and controls fertility outcome in mice

Staphylococcus aureus Adenosine Inhibits sPLA2-IIA–Mediated Host Killing in the Airways

Calcium-independent phospholipases A2 and their roles in biological processes and diseases

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