| Field | Specification |
|---|---|
| Target | |
| CAS no. | |
| Applications | |
| Molecular weight | |
| Molecular formula | C22H32O3 |
| Purity | |
| SMILES | |
| Form | Liquid |
| Storage | |
| Shipping | |
| Catalog no. (Mfr.) | |
| Main SKU |
Compound Overview
17-HDHA is a DHA-derived specialized pro-resolving mediator (SPM) that inhibits NF-κB activation by activating PPARγ and upregulating IκBα, targets FPR2 and Bcl-6, and serves as a precursor of RvD1 and PD1. It inhibits pulmonary artery smooth muscle cell proliferation, regulates expression of adiponectin, GLUT-4, and inflammatory cytokines, suppresses IgE production by B cells, and promotes antibody secretion. It also reduces adipose tissue inflammation, improves insulin sensitivity and glucose tolerance, eases pathological processes associated with pulmonary hypertension, and enhances antibody responses and virus-neutralizing activity against influenza HA, and can be used in research on obesity-associated inflammation, insulin resistance, glucose intolerance, pulmonary hypertension, and influenza virus infection[1][2][3][4][5][6]. It is supplied as a colorless to light yellow liquid (C22H32O3, MW 344.49) at 98.86% purity.
Physical & Chemical Properties
| CAS Number | 90780-52-2 |
|---|---|
| Molecular Formula | C22H32O3 |
| Molecular Weight | 344.49 g/mol |
| Purity | 98.86% |
| Appearance | Liquid |
| Color | Colorless to light yellow |
| SMILES | CC/C=C\CC(O)/C=C/C=C\C/C=C\C/C=C\C/C=C\CCC(O)=O |
| Target | PPARγ |
| Signaling Pathway | Metabolic Enzyme/Protease; Vitamin D Related/Nuclear Receptor; Cell Cycle/DNA Damage; NF-κB; Membrane Transporter/Ion Channel |
| Storage | Solution, -20°C, 2 years. |
| Shipping | Room temperature in continental US; may vary elsewhere. |
Literature Cited
Sources cited in this description and in the In Vitro & In Vivo Data tab. Peer-reviewed publications that used this product are listed under References.
Safety
For Research Use Only. Not for use in diagnostic or therapeutic procedures, and not for human or veterinary use. Handle in accordance with the Safety Data Sheet and your institution's chemical hygiene plan.
In Vitro
Proliferation of mouse pulmonary artery smooth muscle cells induced by PDGFbb is potently inhibited by 17-HDHA (10-20 nM)[2]. By activating formyl peptide receptor 2 (FPR2), 17-HDHA inhibits neutrophil adhesion and migration to monocytes/macrophages[2]. In mouse pulmonary artery smooth muscle cells, 17-HDHA (10 nM; 24 h) activates PPARγ nuclear translocation and inhibits Stat3 phosphorylation stimulated by PDGFbb[2]. Spontaneous and stimulus-induced IgE production is significantly reduced by 17-HDHA (10-100 nM; 6 days) in peripheral blood mononuclear cells taken from asthmatic patients who are not on oral corticosteroids[3]. When cells are pretreated with Dexamethasone, the inhibitory effect of 17-HDHA (10-100 nM; 6 days) on IgE production is blocked in peripheral blood mononuclear cells taken from asthmatic patients who are not on oral corticosteroids[3]. In purified CD19+ B cells from healthy donors, 17-HDHA (10-100 nM; 24-72 h) lowers IgE production along with levels of ε germline transcripts and mature IgE mRNA; pretreatment with Dexamethasone blocks these inhibitory effects[3]. Zileuton, through its 5-lipoxygenase inhibitory effect, blocks the reduction in IgE production that 17-HDHA (10-100 nM; 7 days) achieves in peripheral blood mononuclear cells from healthy donors as well as in purified CD19+ B cells[3]. In purified CD19+ B cells from healthy donors, 17-HDHA (10-100 nM; 6 days) increases the PPARγ binding activity induced by Dexamethasone, whereas used alone it has no effect on PPARγ binding activity[3]. Bcl-6 protein expression in purified CD19+ B cells derived from healthy donors is enhanced by 17-HDHA (10-100 nM; 4 h), while Dexamethasone pretreatment lowers Bcl-6 expression irrespective of 17-HDHA treatment[3]. On purified naive CD19+ B cells from C57BL/6 mice activated with CpG plus anti-IgM, expression of CD80 and CD86 is upregulated by 17-HDHA (10-100 nM; given every day for 6 consecutive days, with a 30 min preincubation before stimulation), and expression of MHC class II is not altered[4]. In purified naive CD19+ B cells from C57BL/6 mice activated with CpG plus anti-IgM, IgM and IgG production is enhanced by 17-HDHA (10-100 nM; given every day for 6 consecutive days, with a 30 min preincubation before stimulation), which also upregulates the mRNA and protein levels of Blimp-1[4]. In peripheral blood mononuclear cells from healthy donors, 17-HDHA (10-100 nM; 4 h) strengthens binding of Bcl-6 to the εGLT promoter region, and Dexamethasone pretreatment blocks this enhancing effect[3]. Naive CD19+CD138− B cells from plasma cell-depleted C57BL/6 mice differentiate into IgM− secreting cells, IgG-secreting cells and plasmablasts under 17-HDHA (10-100 nM; given every day for 5-6 days, with a 30 min preincubation before stimulation); IL-10 production rises, while cell proliferation and the production of IL-6/TNF-α remain unaffected[4]. Replication of pH1N1/E3 influenza virus in MDCK cells is not inhibited by 17-HDHA (0.4-50 μM; 48 h during viral infection) at the highest concentration[4]. Aggregation of washed human platelets induced by collagen is inhibited by 17-HDHA (5-25 μM; 10 min) at 5 μM, aggregation induced by thrombin is inhibited at 25 μM, and no agonist activity is exhibited[5]. Levels of specific D-series resolvins and 10S,17S-dihydroxydocosahexaenoic acid (10S,17S-diHDHA) rise upon 17-HDHA (300-1000 nM; 4-24 h) in human primary great saphenous vein endothelial cells (ECs) as well as in vascular smooth muscle cells (VSMCs). Moreover, RvD1 production follows concentration- and time-dependent patterns beginning at 300 nM 17-HDHA[6]. In primary human great saphenous vein endothelial cells (an increase absent in vascular smooth muscle cells), 5-LOX protein expression is increased by 94% with 17-HDHA (1 μM; 24 h)[6]. In primary human great saphenous vein endothelial cells (ECs) as well as vascular smooth muscle cells (VSMCs), 17-HDHA (1 μM; 5 h) drives 5-LOX translocation from the nucleus to the cytoplasm, and relative cytoplasmic 5-LOX expression levels go up by 28% in ECs and 37% in VSMCs[6]. Adhesion of TNF-α-stimulated U937 monocytes to ECs is attenuated by medium conditioned with human primary great saphenous vein endothelial cells (ECs) that were treated with 17-HDHA (1 μM; 24 h), an effect partially mediated through RvD1 signaling via ALX/FPR2 and GPR32 receptors[6].
Western Blot Analysis[2]
| Cell Line | mouse pulmonary artery smooth muscle cells (PASMCs) |
|---|---|
| Concentration | 10 nM |
| Incubation Time | 24 h |
| Result | Promoted PPARγ nuclear translocation in PDGFbb-stimulated mouse PASMCs, reversing the PDGFbb-induced reduction in nuclear PPARγ. Suppressed PDGFbb-induced Stat3 phosphorylation in these cells. |
ELISA Assay[3]
| Cell Line | PBMCs from asthma patients; B cells from healthy donors |
|---|---|
| Concentration | 10 and 100 nM |
| Incubation Time | 6 days |
| Result | Significantly reduced spontaneous and induced IgE production; dexamethasone pretreatment blocked this effect. |
RT-PCR[3]
| Cell Line | B cells from healthy donors |
|---|---|
| Concentration | 10 and 100 nM |
| Incubation Time | 1 day (εGLT) or 3 days (mature IgE mRNA) |
| Result | Decreased εGLT and mature IgE mRNA levels; dexamethasone pretreatment blocked this effect. |
Western Blot Analysis[3]
| Cell Line | B cells from healthy donors |
|---|---|
| Concentration | 10 and 100 nM |
| Incubation Time | 4 h |
| Result | Increased Bcl-6 protein expression in a concentration-dependent manner; dexamethasone pretreatment reduced basal Bcl-6 expression and blocked this effect. |
ELISA Assay[4]
| Cell Line | Mouse B cells (CD19⁺) |
|---|---|
| Concentration | 10 and 100 nM |
| Incubation Time | 6 days |
| Result | Increased IgM and IgG production in a concentration-dependent manner, with a ~2-fold increase at 100 nM. |
Immunofluorescence
| Cell Line | Endothelial cells and vascular smooth muscle cells |
|---|---|
| Concentration | 1 μM |
| Incubation Time | 5 h |
| Result | Induced translocation of 5-LOX from nucleus to cytoplasm, with a ~28% (ECs) and ~37% (VSMCs) increase in cytoplasmic/nuclear fluorescence ratio. |
ELISA Assay
| Cell Line | Human ECs and VSMCs |
|---|---|
| Concentration | 300, 500 and 1000 nM |
| Incubation Time | 4, 8 and 24 h |
| Result | Concentration- and time-dependently increased RvD1 production, with significant increases at 300 nM and peak at 8 h. |
In Vivo
In diet-induced obese male C57BL/6J mice, 17-HDHA (50 ng/g, i.p., every 12 hours for 8 days; osmotic pump, administered continuously for 15 days in total) lowers adipose tissue inflammation associated with obesity and improves glucose tolerance and insulin sensitivity; among these regimens, 15 days of continuous administration significantly lowers fasting insulin levels and HOMA-IR[1]. In mice, endogenous 17-HDHA generated by eosinophils through arachidonic acid 15-lipoxygenase inhibits the pathological changes of pulmonary hypertension induced by Sugen/hypoxia[2]. In OVA-immunized mice, 17-HDHA (1 μg; i.p.; single synchronized injection) increases antigen-specific IgM and IgG production, with significantly higher titers detected at key time points after immunization[4]. In mice immunized with HA combined with CpG ODN, 17-HDHA (1 μg; intramuscular injection; given together with the primary and booster immunizations) enhances HA-specific IgG production, with significantly elevated antibody titers detected at multiple time points post-immunization[4]. In mice immunized with HA alone, 17-HDHA (1 μg; intramuscular injection; given together with each immunization during weeks 0-4) enhances HA-specific antibody production and plasma cell differentiation in the bone marrow, with significant increases in IgG titers and in the frequency of antibody-secreting cells[4]. 17-HDHA (1 μg; intramuscular injection; given together with each immunization during weeks 0-4) strengthens the protective efficacy of influenza HA vaccine in mice, resulting in detectable neutralizing antibodies, minimal body weight loss, and a 100% survival rate after live influenza virus challenge[4].
| Animal Model | C57BL/6J (male, wild-type, diet-induced obesity via 60% kcal high-fat diet for 17 weeks)[1] |
|---|---|
| Dosage | 50 ng/g body weight |
| Administration | i.p.; every 12 h; 8 days; osmotic pump; continuous; 15 days |
| Result | Reduced mRNA expression of inflammatory genes (MCP-1, TNF-α, IL-6, OPN, NF-κB) in gonadal adipose tissue. Increased IκBα protein level in gonadal adipose tissue. Reduced CD11c+/CD206+ adipose tissue macrophage ratio. Enhanced mRNA expression of PPARγ, PPARα, GLUT-4, and adiponectin in gonadal adipose tissue. Moderately improved glucose tolerance with reduced plasma insulin at 45 minutes post-glucose challenge. Achieved 30% reduction in fasting insulin concentration and 40% lower HOMA-IR (non-significant trends). Showed trend toward improved insulin tolerance at 60, 90, and 120 minutes post-insulin injection. Significantly decreased fasting insulin concentration and HOMA-IR. Showed trend toward reduced blood glucose at 30 minutes post-insulin injection. Significantly lowered blood glucose at 15 minutes post-glucose challenge. Reduced plasma insulin levels at baseline and 45 minutes post-glucose challenge. |
| Animal Model | C57BL/6J (male, 8-10 wk old) were immunized via intraperitoneal injection with OVA protein (10 μg/mouse) emulsified in complete Freund's adjuvant (CFA). Immediately after the primary immunization, the compound was administered via intraperitoneal injection at the same site. Blood samples were collected at 2 and 6 weeks after the primary immunization to measure OVA-specific IgM and IgG antibody levels. At week 10, mice received a booster immunization via intraperitoneal injection with OVA (10 μg/mouse) in PBS. Blood samples were collected again at 2 weeks after the booster immunization for antibody detection [4] |
|---|---|
| Dosage | 1 μg |
| Administration | i.p.; single concurrent injection |
| Result | Showed significantly higher OVA-specific IgM titers at weeks 6 and 12 compared with vehicle controls. Showed significantly higher OVA-specific IgG titers at week 6 compared with vehicle controls. Showed a decreasing trend in OVA-specific IgE levels compared with vehicle controls. |
| Animal Model | C57BL/6J (male, 8-10 wk old) were primed via intramuscular injection at week 0 with recombinant HA protein (H1N1 A/Brisbane/59/2007, 5 μg/mouse), CpG ODN 1826 (10 μg/mouse), and the compound (1 μg/mouse). Booster immunizations were given at weeks 2 and 4 in the same manner. [4] |
|---|---|
| Dosage | 1 μg |
| Administration | i.m.; concurrent with primary and booster immunizations |
| Result | Showed significantly higher HA-specific IgG titers at weeks 3, 6, and 11 compared with vehicle controls. Showed no significant differences in HA-specific IgM titers at any time point compared with vehicle controls. |
| Animal Model | C57BL/6J (male, 8-10 wk old) were immunized via intramuscular injection at weeks 0, 2, and 4 with recombinant HA protein (H1N1 A/California/04/2009, 2 μg/mouse) and the compound (1 μg/mouse)[4] |
|---|---|
| Dosage | 1 μg |
| Administration | i.m.; concurrent with each immunization at weeks 0, 2, and 4 |
| Result | Showed a 2-fold increase in HA-specific IgM titers at week 2 compared with mock and vehicle controls. Showed a 9-fold increase in HA-specific IgG titers at week 2 compared with mock and vehicle controls. Showed a 3-fold increase in HA-specific IgG titers at week 4 compared with vehicle controls. Showed a 9-fold increase in HA-specific IgG titers at week 6 compared with vehicle controls. Showed a 2-fold increase in the percentage of CD19+ CD138+ plasma cells in the bone marrow compared with mock and vehicle controls. Showed a 2-fold increase in HA-specific IgG-secreting bone marrow cells compared with mock and vehicle controls. Showed no differences in splenic CD19+ CD138+ plasma cells compared with controls. |
| Animal Model | C57BL/6J (male, 8-10 wk old) were immunized via intramuscular injection at weeks 0, 2, and 4 with recombinant HA protein (H1N1 A/California/04/2009, 2 μg/mouse) and 17-HDHA (1 μg/mouse) or vehicle control (3 immunizations in total). Blood was collected at 14 days after the last immunization (week 6), and serum neutralizing antibody titers were measured by GFP-based microneutralization assay. At 28 days after the last immunization (week 8), mice were challenged intranasally with 300 PFU/mouse of mouse-adapted live influenza virus H1N1 A/California/04/E3/2009[4] |
|---|---|
| Dosage | 1 μg |
| Administration | i.m.; concurrent with each immunization at weeks 0, 2, and 4 |
| Result | Showed 44% of treated mice with detectable neutralizing antibody titers (≥40) at week 6, compared with 0% of mock and vehicle controls. Showed minimal weight loss following viral infection, while mock and vehicle-treated mice experienced dramatic weight loss. Showed a 100% survival rate following viral infection, compared with 30% for mock controls and 80% for vehicle controls. |
Data provided by the manufacturer. Numbered citations refer to the Literature Cited list in the product description.
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