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Berquin Department of Cancer Biology, Wake Forest School of Medicine, Medical Center Blvd, Winston-Salem, NC 27157, USA Comprehensive Cancer Center, Wake Forest School of Medicine, Winston-Salem, NC, USA Iris J.
Edwards Department of Pathology, Wake Forest School of Medicine, Winston-Salem, NC, USA Comprehensive Cancer Center, Wake Forest School of Medicine, Winston-Salem, NC, USA Steven J.
Kridel Department of Cancer Biology, Wake Forest School of Medicine, Medical Center Blvd, Winston-Salem, NC 27157, USA Comprehensive Cancer Center, Wake Forest School of Medicine, Winston-Salem, NC, USA Yong Q.
Chen Department of Cancer Biology, Wake Forest School of Medicine, Medical Center Blvd, Winston-Salem, NC 27157, USA Comprehensive Cancer Center, Wake Forest School of Medicine, Winston-Salem, NC, USA Isabelle M.
Berquin, Department of Cancer Biology, Wake Forest School of Medicine, Medical Center Blvd, Winston-Salem, NC 27157, USA; Comprehensive Cancer Center, Wake Forest School of Medicine, Winston-Salem, NC, USA; Polyunsaturated fatty acids PUFA play important roles in the normal physiology and in pathological states including inflammation and cancer.
While much is known about the biosynthesis and biological activities of eicosanoids derived from ω6 PUFA, our understanding of the corresponding ω3 series lipid mediators is still rudimentary.
The purpose of this review is not to offer a comprehensive summary of the literature on fatty acids in prostate cancer but rather to highlight some of the areas where key questions remain to be addressed.
These include substrate preference and polymorphic variants of enzymes involved in the metabolism of PUFA, the relationship between de novo lipid synthesis and dietary lipid metabolism pathways, the contribution of cyclooxygenases and lipoxygenases as well as terminal synthases and prostanoid receptors in prostate cancer, and the potential role of PUFA in angiogenesis and cell surface receptor signaling.
Since ω3 and ω6 PUFA cannot be synthesized de novo, they are essential fatty acids and must be taken in from the diet.
However, PUFA elongation to longer chain species shares malonyl-CoA as a common substrate with узнать больше novo fatty acid synthesis.
Bioactive metabolites of ω6 PUFA generated by COXs and LOXs eicosanoids have been extensively investigated and play various roles in inflammation, cancer cell proliferation, and metastasis.
Overall, metabolites of ω3 PUFA oppose these actions, but their generation is still poorly understood.
In this review, we highlight the interplay between dietary PUFA intake, elongation, β-oxidation, storage, and eicosanoid synthesis and de novo fatty acid synthesis.
We further discuss the potential roles of PUFA and their metabolites in prostate cancer, with an emphasis on angiogenesis and cell surface receptors, and contrast the wealth of information available on ω6 PUFA metabolism to the relative scarcity of knowledge on ω3 PUFA metabolism.
Linoleic acid LA, 18:2n-6 is an ω6 PUFA found in abundant supply in vegetable oils; it is metabolized primarily to arachidonic acid AA, 20:4n-6 through a series of alternating oxidative desaturation and elongation steps.
In the ω3 series, alpha linolenic acid α-LNA, 18:3n-3found at moderate levels in most terrestrial plants, is not converted efficiently to long-chain ω3 PUFA such as eicosapentaenoic acid EPA, 20:5n-3 and docosahexaenoic acid DHA, 22:6n-3; see below.
Therefore, in humans the main source for these long-chain ω3 PUFA is through dietary intake of fish or supplementation with fish oil.
During ω6 PUFA conversion, fatty acid desaturase 2 FADS2 or delta-6 desaturase converts LA to gamma linolenic acid γ-LNA, 18:3 n-6.
The first of these is condensation of the fatty acyl chain with malonyl-CoA, catalyzed by an enzyme encoded by the ELOVL5 gene elongation of very long-chain fatty acids, family member 5.
This is followed by a reduction reaction mediated by 3-ketoacyl-CoA reductase KAR, also known as HSD17B12a dehydration reaction catalyzed by 3-hydroxyacyl-CoA dehydratase HACDand finally a second reduction reaction нажмите чтобы узнать больше by trans-2,3-enoyl-CoA reductase TECR.
After chain elongation, fatty acid desaturase 1 FADS1 or delta-5 desaturase converts DGLA to AA.
Conversion of ω6 and ω3 series PUFA by metabolic enzymes and interaction with de novo fatty acid synthesis.
The main dietary ω6 and ω3 PUFA LA, 18:2 n-6 and αLNA, 18:3 n-3 undergo a series of desaturation FADS2, FADS1 and elongation ELOVL5, KAR, HACD, TECR steps converting them to AA and EPA, respectively.
Long-chain PUFA are converted to prostaglandins PG and thromboxanes TX by cyclooxygenases COX1— 2 or to leukotrienes LT and hydroxyeicosatetraenoic acids HETE by lipoxygenases LOX.
EPA can be further elongated and desaturated to DHA in a pathway involving β-oxidation in the peroxisome.
In the presence of aspirin, COX2 metabolizes EPA and DHA to resolvins.
The various products play important roles in inflammation, cell proliferation and apoptosis, and angiogenesis.
In the de novo lipid synthesis pathway, acetyl-CoA and malonyl-CoA can be interconverted by acetyl-CoA carboxylase ACC1 and malonyl-CoA decarboxylase MLYCD.
Acetyl-CoA and malonyl-CoA are used as substrates by fatty acid synthase FASN to generate long-chain saturated fatty acids, which can be elongated further ELOVL6 or desaturated SCD to form monounsaturated fatty acids.
Malonyl-CoA is also required for elongation of ω6 and ω3 PUFA The same enzymes are involved in ω3 PUFA conversion.
However, conversion of α-LNA to DHA in humans appears to be very inefficient.
Instead of being further anabolized, most of the ingested α-LNA is subject to β-oxidation to provide energy and only a small fraction is converted to EPA.
From kinetic analyses of fatty acid conversion, it was estimated that conversion of α-LNA to EPA might be as low as 0.
Therefore, the overall amount of DPA and DHA made from α-LNA would only represent 0.
These data suggest that FADS2, the first enzyme in the conversion sequence, is rate-limiting.
Approximately 207 single-nucleotide polymorphisms SNPs were identified on FADS1, 610 SNPs on FADS2, and 246 SNPs on FADS3.
One SNP rs174561 is present within the miRNA, and two additional SNPs rs73487465 and rs75810419 flank it.
Whether these SNPs have an effect on hsa-mir-1908 expression is currently unclear.
FADS polymorphisms may affect both ω3 and ω6 PUFA desaturation—elongation.
An intriguing question is whether this polymorphic 5, if confirmed, has an impact on the effect of ω3 and ω6 PUFA on cancer risk among different populations.
This is evidenced by high expression levels of enzymes in the pathway in multiple types of cancer, including prostate cancer.
In addition, the pathway is driven by the same processes that drive prostate cancer.
Collectively, these findings strongly suggest that that the de novo pathway of fatty acid synthesis is not only required for prostate cancer but may have a role in promoting disease progression.
There are other enzymes upstream of FASN that are involved in fatty acid synthesis.
To generate the substrates for fatty acid synthesis, several enzymatic steps are required.
Generation of malonyl-CoA is the rate-limiting step of fatty acid synthesis.
FASN also synthesizes the 14-carbon fatty acid myristate and the 18-carbon fatty acid stearate, albeit to lesser degrees.
Palmitate can undergo a series of modifications before it is utilized in the cells.
It can be elongated by two carbons to stearate using malonyl-CoA as the elongation substrate, just as 5 is for PUFA.
Palmitate and stearate can also be desaturated by stearoyl-CoA desaturase-1 to form the monounsaturated palmitoleate and oleate, respectively.
Thus, the fatty acid synthesis pathway generates the saturated fatty acid component of the cell but also provides the precursor for the monounsaturated component of the cell.
Because of the cellular dependence on fatty acid synthesis to facilitate membrane biogenesis and other aspects of cell biology, fatty acid synthesis impacts on virtually every aspect of cellular activity.
Some portion of the increased demand can be attributed to increased proliferation of tumor cells compared to normal cells.
It may also be possible that dietary and de novo fatty acids are subject to different fates in a cell.
In such a case, it may be that dietary fatty acid is unable to meet to demands of the tumor cell.
The fate of newly synthesized fatty acid in a tumor cells has been well defined.
Blockade of the pathway has little effect on phosphatidylserine, phosphatidylethanolamine, and phosphatidylinositol.
It is tempting to speculate that dietary fat is required to support the non-PC portion of tumor cell membranes.
This is consistent with the finding that lipid rafts are rich in lipids containing saturated fatty acid.
It also suggests that fatty acid synthesis supports signaling functions that are associated with lipid rafts.
Although the expression and activity of enzymes in the fatty acid synthesis pathway is highly correlated with cancer, there are several examples of normal biology in which the pathway is active.
Similarly, Acc1-deficient embryos display lethality at around day 8.
It is interesting to note that placing pregnant mothers on a diet enriched in saturated fatty acid is not sufficient to protect embryos from the effects of Fasn deletion.
Whether this is because узнать больше здесь differential utilization of dietary fat compared to synthesized fat or from having to cross the placenta is unknown.
The liver and adipose tissue are two other examples in which the fatty acid synthesis pathway is active.
In these tissues, fatty acid is generated and, following excessive caloric consumption, stored as triglyceride for future energy.
Of note, this lipid is among the most abundant of all lipid species.
That a high-fat diet could not recapitulate the wild-type liver phenotype of the wild-type mice suggests that dietary fat may be utilized differently than de novo synthesized fat in cells.
Unlike what has been a demonstrated in vivo using total or tissue-specific knockout of Fasn, exogenous fatty acid is able to protect cells from the effects of inhibiting FASN and ACC1 in tumor cell lines in vitro.
As discussed Сменные лезвия Deonica, when tumor cell lines are treated with FASN and ACC1 inhibitors or transfected with siRNA against either of the two enzymes, cell cycle blockade and cell death ensue.
Many of the cellular effects can be delayed or ameliorated by supplementing cells with exogenous fatty acid in their culture medium.
Moreover, it appears that this mechanism has the potential to protect tumor cells from the effects of inhibitors of de novo fatty acid synthesis.
Although in vitro experimentation does not always adequately reflect in vivo biology, it is interesting to consider that dietary fat may have a different influence on tumor cells than on normal cells.
This could be related to the fact that tumor cells have an absolute requirement for the synthesis of saturated fatty acid.
Development of FASN, ACC1, and ACLY inhibitors is the subject of intense investigation.
Because PUFA elongation requires malonyl-CoA, one interesting possibility is that inhibition of ACC1 or ACLY could reduce cellular malonyl-CoA level and consequently diminish the LA to AA conversion.
Since elongation of dietary ω6 PUFA appears to be more efficient than that of ω3 PUFA, it is tempting to speculate that ACC1 and ACLY inhibitors may preferentially reduce the formation of AA and consequently that of the ω6-series eicosanoids.
During the last two centuries, however, the consumption of ω6 PUFA has increased dramatically due to the increased intake of vegetable oils.
Today, the ratio of ω6 and ω3 PUFA in western diets is approximately 30:1.
Three major groups of phospholipase A2 PLA2 enzymes have been identified: secreted PLA2 or sPLA2, cytosolic PLA2 or cPLA2, and calcium-independent PLA2 or iPLA2.
Therefore, the extent to which ω3 and ω6 PUFA are released from phospholipids would be expected to depend on the relative expression of the various phospholipases.
To date, it is unclear whether ω6 and ω3 PUFA are differently β-oxidized and how ω6 and ω3 PUFA are cycled in tumor cells.
Compared to cytosolic and secreted phospholipases, little is known about the expression and function of iPLA2 enzymes in читать статью cancer.
COXs catalyze the first reaction in the conversion of AA to prostaglandins PG G and H, which are further metabolized into other prostaglandins PGE, PGF, PGJprostacyclins PGIand thromboxanes TXA, TXBwhereas LOXs mediate the first step in the conversion of AA to leukotrienes and hydroxyeicosatetraenoic acids HETEs.
Cytochrome P450 oxygenases convert AA to HETEs by the action of omega-hydroxylase activity and to epoxyeicosatrienoic acids EETs by epoxygenase activity.
However, in contrast to ω6 PUFA, the metabolism of ω3 PUFA is not well understood.
A third isoform, COX3, appears to be a splice variant of the COX1 gene.
Due to its induction in inflammation and cancer, COX2 has been the object of intense study and proposed as a target for cancer therapy.
Due to the existence of multiple oxygenases, the role of specific enzymes in the development of prostate cancer has not been studied systematically in a single system or animal model.
In addition, studies performed in animals rarely take diet into account for the design and interpretation of the experiments.
For 5 reason, it is still unclear whether all oxygenases читать an important role or some oxygenases are more critical in the development of посмотреть еще cancer in animals consuming different diets.
To systematically assess the interaction between oxygenases and dietary PUFA in a single in vivo model of prostate cancer, we knocked out Cox1, Cox2, Lox5, Lox12, or Lox15 in prostate-specific Pten-null mice.
Preliminary results indicate that loss of Cox1 had significant effects on prostate tumor growth in a PUFA-dependent manner; namely, tumor growth was significantly increased in Cox1 knockout mice on ω3 diet compared to Pten-null, Cox1-positive mice on the same diet, essentially negating the protective effects of ω3 PUFA.
In other words, Cox1 appears to be required for the protective effects of ω3 PUFA, suggesting that ω3 metabolites of Cox1 reduce cancer formation.
On the other hand, tumor growth was decreased in mice on ω6 diet compared to Pten-null, Cox1-positive mice on the same diet, suggesting that ω6 metabolites of Cox1 e.
Loss of Cox2 reduced prostate tumor growth regardless of diet, suggesting that metabolites of Cox2 promote tumor growth and that suppressive effects of ω3 PUFA do not depend upon Cox2.
Loss of Lox5 reduced prostate tumor growth on ω6 diet but had no effect on ω3 diet, suggesting that ω6 metabolites of Lox5 promote tumor growth, and protective effects of ω3 PUFA are independent of Lox5.
Loss of Lox12 or Lox15 did not affect prostate tumor growth on either diet, suggesting that either PUFA metabolites are not generated from these two enzymes, or metabolites generated are not critical for prostate tumor in this animal model Chen et al.
It is clear 5 these studies that the interaction between diet and metabolic genes can play an important role in determining cancer risk and response of cancer to dietary PUFA.
Such reports are consistent with our animal studies, but the role of COX1 as well as specific polymorphisms of eicosanoid metabolic enzymes in human prostate cancer warrants further investigations.
In turn, PGH 2 is converted to other prostaglandins, prostacyclin, and thromboxanes by the action of several isomerases also called terminal synthases.
Three terminal synthases capable of producing PGE 2 from COX-derived PGH 2 have been reported: prostaglandin E synthase PTGES or microsomal PGES-1 mPGES-1PTGES2 or mPGES-2, and PTGES-3 or cPGES.
A prostaglandin D 2 synthase responsible for converting PGH 2 to PGD 2 has been described in the brain, whereas in immune cells this conversion is catalyzed by hematopoietic prostaglandin D synthase.
Prostaglandin I 2 prostacyclin synthase PTGIS is involved in the conversion of PGH 2 to PGI 2.
In platelets, thromboxane A synthase 1 TBXAS1 converts PGH 2 to TXA 2.
However, for many of these enzymes, the extent to which ω3 PUFA can serve as substrates is unclear.
Main enzymes and G protein-coupled receptors in the cyclooxygenase pathway.
Arachidonic acid is converted to PGG 2 by cyclooxygenase 1 or 2 and PGG 2 then undergoes conversion to PGH 2 through the peroxidase activity of COX.
Several isomerases convert PGH 2 to other 2-series prostaglandins, prostacyclins or thromboxanes, which act in part by binding to specific prostanoid receptors green.
EPA is thought to serve as a substrate for the same set of enzymes to generate three-series eicosanoids PGH 3, PGE 3, etc.
Some prostanoids have also been shown to bind to PPARs not shown.
Official protein symbols are shown in red for enzymes and in green for receptors, with common abbreviations in parenthesis.
PTGS1—2 prostaglandin-endoperoxide synthase 1—2, PTGDS PGD 2 synthase brainHPGDS hematopoietic PGD synthase, PTGES1—3 PGE synthase 1—3, PTGIS PGI 2 prostacyclin synthase, TBXAS1 TXA synthase 1, PTGDR PGD 2 receptor, PTGER1—4 PGE receptor 1—4 subtype EP1—4PTGFR PG F receptor, PTGIR PGI 2 prostacyclin receptor, TBXA2R TXA 2 receptor mPGES-1 is a microsomal glutathione-dependent prostaglandin E synthase that can be induced by LPS, the proinflammatory cytokine interleukin 1 beta, by tumor suppressor protein TP53, as well as in pathological conditions such as cancer.
One report showed that mPGES-1 is expressed at high levels in DU145 human prostate cancer cells and in human prostate cancer tissues compared with benign hyperplasia.
Short hairpin RNA-mediated mPGES-1 knockdown in DU145 decreased clonogenic survival and increased sensitivity to adriamycin-induced apoptosis, which could be rescued by exogenous PGE 2.
The role of prostacyclin and PTGIS in prostate cancer is less clear.
Thromboxane A 4 synthase TBXAS1 is overexpressed in a number of cancers and has been proposed to contribute to tumor development and progression by modulating tumor growth, angiogenesis, thrombosis, invasion, and metastasis and by inhibiting apoptosis.
In addition, migration of PC-3 cells, which express high levels of TBXAS1, was reduced by inhibition of this enzyme, whereas motility of TBXAS1-negative DU145 cells was stimulated by its overexpression.
Nine prostanoid receptors LOMOND Пленка прозрачная для цветной струйной печати 100 мкм, A3, 50 листов been identified, which belong to the G protein-coupled receptor family and are conserved from mouse to human.
In mouse prostate cells, expression of Ep1, Ep2, and Ep4 is detectable Chen et al.
However, much remains to be learnt about the expression of these prostanoid receptors and their activation by ω6 and, especially, ω3 prostanoids in cancer cells.
Here we will focus on the potential role of PUFA in angiogenesis and cell surface receptor signaling.
Effects of ω3 PUFA on in vivo models of VEGF-induced angiogenesis are inconsistent.
Both EPA and DHA inhibited VEGF expression and reduced microvessels in tumors arising from HT-29 colon cancer cell transplants in nude mice.
A 45% reduction in the ω6 to ω3 PUFA ratio in serum was accompanied by a significant страница in VEGF following the Mediterranean diet phase.
PDGF is another agree, Емкость эвл-т 100 синий are regulator of angiogenesis.
Similar studies have yet to be conducted with cancer patients.
FGF8 has also emerged as an important promoter of angiogenesis.
They play a major role in defense against pathogens, particularly at mucosal surfaces.
Although the biological consequences of these polymorphisms are not understood, they are consistent with a major role of inflammation in prostate cancer and suppression of TLR activity may be one of the anti-inflammatory roles of ω3 PUFA.
Effects of ω3 PUFA on prostate cancer cell TLRs remain to be determined.
The syndecan family https://megapixels.ru/100/zharoprochniy-oktoboks-mingxing-front-diffuser-95-sm-bowens.html cell surface proteoglycans consists of four members with a shared structure of small conserved cytoplasmic and transmembrane domains and larger, distinct ectodomains.
Syndecan-1 is the most widely studied in relation to cancer, but its role is complex and far from clear.
Its heparan sulfate chains interact with a variety of extracellular matrix components, growth factors, cytokines, and enzymes to facilitate a role in regulation of cell proliferation, apoptosis, adhesion, and migration.
This may result in changes in the fine structure of syndecan-1 that lead to altered function.
Syndecan-1 has not been 5 studied in prostate cancer.
Moreover, in human and mouse prostate cancer cells lines, syndecan-1 was upregulated by DHA but not EPA.
New evidence points to an important role for syndecan-1 as a negative regulator of angiogenesis and suggests that ω3 PUFA modulation of angiogenesis may involve syndecan-1.
In a mouse model of lung injury, binding of the chemokine CXCL1 to syndecan-1 was shown to induce enzymatic shedding of the ectodomain-CXCL1 complex by MMP-7.
Critical experiments confirming a role for syndecan-1 in ω3 PUFA suppression of angiogenesis have 5 to be conducted.
Much of the knowledge is derived from the study of ω6 Https://megapixels.ru/100/igrushka-zvezda-svetitsya-v-temnote-22-h-18-h-5-sm.html />Relatively little is known about ω3 PUFA metabolism.
Moreover, the interplay between dietary fat and de novo synthesis is not fully understood, especially in cancer.
We will end this review by posing a series of questions, which we believe are some of the key challenges in the field of PUFA research.
Contributor Information Isabelle M.
нажмите сюда, Department of Cancer Biology, Wake Forest School of Medicine, Medical Center Blvd, Winston-Salem, NC 27157, USA.
Comprehensive Cancer Center, Wake Forest School of Medicine, Winston-Salem, NC, USA.
Edwards, Department of Pathology, Wake Forest School of Medicine, Winston-Salem, NC, USA.
Comprehensive Cancer Center, Wake Forest School of Medicine, Winston-Salem, NC, USA.
Kridel, Department of Cancer Biology, Wake Forest School of Medicine, Medical Center Blvd, Winston-Salem, NC 27157, USA.
Comprehensive Cancer Center, Wake Forest School of Medicine, Winston-Salem, NC, USA.
Chen, Department Стаканчик силиконовый складной 100 мл.

розовый Cancer Biology, Wake Forest School of Medicine, Medical Center Blvd, Winston-Salem, NC 27157, USA.
Comprehensive Cancer Center, Wake Forest School of Medicine, Winston-Salem, NC, USA.
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