Spermine

Manufactured by Merck Group

Sourced in United States, Germany, United Kingdom, Portugal

Spermine is a laboratory reagent used in various scientific applications. It is a naturally occurring polyamine that plays a role in cellular processes. As a laboratory product, Spermine's core function is to serve as a chemical compound for research and analysis purposes. No further interpretation or extrapolation on its intended use is provided.

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Lab products found in correlation

171 protocols using spermine

Spermine Protects Podocytes from High Glucose

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Rat podocytes (cat. no. BNCC338697; BeiNa Culture Collection; Beijing Beina Chunglian Biotechnology Research Institute) were cultured at 37°C in a 5% CO₂ humidified incubator in DMEM (Gibco; Thermo Fisher Scientific, Inc.) containing 10% fetal bovine serum (FBS; Gibco; Thermo Fisher Scientific, Inc.) and 1% penicillin. Podocytes were cultured for 6-12 h in DMEM containing 5.5 mM D-glucose (Sigma-Aldrich; Merck KGaA) without FBS before exposure to various experimental conditions. The cells were randomly divided into six groups: i) Normal-glucose group (NG), where the podocytes were incubated in DMEM containing 5.5 mM glucose for 48 h; ii) mannitol group (M), where the podocytes were incubated in DMEM containing 40 mM mannitol and 5.5 mM glucose for 48 h; iii) high-glucose group (HG), where the podocytes were incubated in DMEM containing 40 mM glucose for 48 h; iv) spermine-treated group (HG + Sp), where the podocytes were pretreated with 1, 5, 10, 20 and 50 µM spermine (Sigma-Aldrich; Merck KGaA) for 2 h before being subjected to HG conditions; v) rapamycin-treated group (HG + Rap), where the podocytes were pretreated with 10 mM rapamycin (MCE) for 2 h before being subjected to HG conditions; and vi) Compound C treatment group (HG + Sp + Compound C), where 10 mM Compound C (Selleck Chemicals), an AMPK inhibitor, was added to the medium 1 h before HG and spermine addition.

Zhang X., Zhang L., Chen Z., Li S., Che B., Wang N., Chen J., Xu C, & Wei C. (2021). Exogenous spermine attenuates diabetic kidney injury in rats by inhibiting AMPK/mTOR signaling pathway. International Journal of Molecular Medicine, 47(3), 27.

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Polyamine Supplementation in Mice

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Polyamine spermidine (2 mmol/L, Aladdin) and spermine (2 mmol/L, Sigma) were diluted in drinking water according to previous experiment [16 (link)]. Mice were respectively treated with saline, spermidine, spermine and rapamycin (0.78mg/kg/d, Sigma, intragastric administration) for 8 weeks.

Xu T.T., Li H., Dai Z., Lau G.K., Li B.Y., Zhu W.L., Liu X.Q., Liu H.F., Cai W.W., Huang S.Q., Wang Q, & Zhang S.J. (2020). Spermidine and spermine delay brain aging by inducing autophagy in SAMP8 mice. Aging (Albany NY), 12(7), 6401-6414.

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Nuclei Isolation and Photocrosslinking Protocol

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Combine 250 μl of ice-cold nucleus lysis buffer (10 mM of Tris-HCl, pH 7.5, 10 mM of NaCl, 3 mM of MgCl₂, 0.5% NP-40, 0.15 mM of spermine (Sigma), 0.5 mM of spermidine (Sigma)) with 50 μl of protease inhibitors (Sigma). Add to 5 million cells without fixing. Incubate cell suspension on ice for 5 min. Centrifuge at 500g for 5 min at 4 °C. Discard the supernatant. Wash pelleted nuclei once with 500 μl of nucleus resuspension buffer (10 mM of Tris-HCl pH 7.4, 15 mM of NaCl, 60 mM of KCl, 0.15 mM of spermine (Sigma), 0.5 mM of spermidine (Sigma)). Centrifuge at 500g for 5 min at 4 °C and discard the supernatant. Resuspend the cell pellet in 500 μl of 50 μM dendrimer in methanol. Incubate at 4 °C on a rocker with rotation for 10 min. Photocrosslink the nuclei by irradiating under 365 nm of UV for 15 min at 4 °C. The nuclei should be allowed to rest on ice for 5 min before another 15 min of 365 nm of UV irradiation at 4 °C. Centrifuge for 5 min at 2,500g at 4 °C. Discard the supernatant. Wash pelleted nuclei twice with 500 μl of nucleus resuspension buffer. Centrifuge and discard the supernatant. Resuspend the pellet in proteinase K digestion buffer (420 μl of nucleus resuspension buffer, 50 μl of 10% SDS, 30 μl of 20 mg ml⁻¹ proteinase K). Incubate the resuspension at 65 °C overnight on a thermomixer at 800 r.p.m.

You Q., Cheng A.Y., Gu X., Harada B.T., Yu M., Wu T., Ren B., Ouyang Z, & He C. (2020). Direct DNA crosslinking with CAP-C uncovers transcription-dependent chromatin organization at high resolution. Nature biotechnology, 39(2), 225-235.

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Spermine Dose-Response in Rat Kidneys

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To explore the safe concentration range of spermine in rat kidneys, 50, 100, 150, 200, 250, and 300 µM of spermine (Sigma, S4264) were assessed, and normal saline was used as a control. The principle of randomized grouping was adopted, and five rats in each group were injected intravenously (2 mL/kg body weight). After 72 hours, the rats were anesthetized, the kidneys were harvested by laparotomy, and blood samples from the inferior vena cava were collected into Eppendorf tubes without anticoagulant. After standing at 4 °C for 2 hours, samples were centrifuged at 1,500 ×g for 10 minutes, and the supernatant was cryopreserved. The renal tissue was fixed with 4% paraformaldehyde for 24 hours, and the sections were embedded according to the conventional method (25 (link)).

Yan B., Min S.J., Xu B., Zhang C., Pei J., Zhang W, & Luo G.H. (2021). The protective effects of exogenous spermine on renal ischemia-reperfusion injury in rats. Translational Andrology and Urology, 10(5), 2051-2066.

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Trodusquemine and Spermine Solubilization

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Trodusquemine was synthesized as a hydrochloride salt at a purity >97% as measured by mass spectrometry^{23 (link)}, stored as a lyophilized powder and solubilized in water to a final concentration of 10 mM^{23 (link)}. Spermine (>97% purity, Sigma-Aldrich, MO, USA) was solubilized in water to a final concentration of 100 mM. Both molecules were stored in water at −20 °C until use.

Limbocker R., Chia S., Ruggeri F.S., Perni M., Cascella R., Heller G.T., Meisl G., Mannini B., Habchi J., Michaels T.C., Challa P.K., Ahn M., Casford S.T., Fernando N., Xu C.K., Kloss N.D., Cohen S.I., Kumita J.R., Cecchi C., Zasloff M., Linse S., Knowles T.P., Chiti F., Vendruscolo M, & Dobson C.M. (2019). Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes. Nature Communications, 10, 225.

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Analytical Standards for Metabolite Quantification

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The following standards were acquired from Sigma-Aldrich (Steinheim, Germany): glucose, sucrose, fructose, inositol, spermidine, spermine, cadaverine, putrescine, 1,6-hexaendiamine gallic acid, 6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acid (Trolox), 2,2-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) diammonium salt (ABTS^•+), and benzoyl chloride. Sodium hydroxide was purchased from Fluka (Buchs, Switzerland), and LC-MS grade organic solvents (Methanol, acetonitrile), together with sodium carbonate, Folin-Ciocalteu reagent, and ethyl ether, were purchased from Panreac Química (Barcelona, Spain). SPE cartridges (C18 Sep-Pak cartridges) were obtained from Waters Associates (Milford, MA, USA), and, lastly, ultrapure water was produced by a Millipore water purification system.

Collado-González J., Piñero M.C., Otalora G., López-Marín J, & del Amor F.M. (2022). Enhancement of Bioactive Constituents in Fresh Cauliflower By-Products in Challenging Climate Conditions. Antioxidants, 11(5), 958.

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Gelatin-Based Molecular Beacon Synthesis

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Gelatin with an isoelectric point of 9.0 and the weight-averaged molecular weight of 99,000, prepared by an acidic treatment of pig skin collagen, was kindly supplied from Nitta Gelatin Inc., Osaka, Japan. Molecular beacons (MB) composed of DNA bases for mouse messenger RNA (mRNA) of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and enhanced green fluorescent protein (EGFP) were synthesized by Integrated DNA Technologies, Inc., Coralville, IA, USA. The sequences of MB [26 (link), 30 (link)] were as follows, GAPDH MB: 5’-[TYE^Ⓡ665]-CTGGTAATCCGTTCACACCGACCTTCACCAG-[Iowa Black^ⓇRQ]-3’; EGFP MB: 5’-[TYE^Ⓡ665]-ACGCCTTCTCGTTGGGGTCTTTGCTCGGCGT -[Iowa Black^ⓇRQ]-3’ (underline indicates the stem structure). Target oligonucleotides of DNA for GAPDH MB (specific and non-specific sequences) were synthesized by Hokkaido System Science Co., Ltd, Sapporo, Japan. The sequences of specific and non-specific targets were as follows, specific: 5’-TGGTGAAGGTCGGTGTGAACGGATT-3’; non-specific: 5’-TTTCTGAATGGCCCAGGT-3’. Spermine was purchased from Sigma-Aldrich Inc., St Louis, MO, USA. Concentrated hydrochloric acid (HCl) and 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride (EDC) were purchased from Nacalai Tesque. Inc., Kyoto, Japan. The reagents were used without any purification.

Takehana S., Murata Y., Jo J.I, & Tabata Y. (2021). Complexation design of cationized gelatin and molecular beacon to visualize intracellular mRNA. PLoS ONE, 16(1), e0245899.

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Yeast Media Supplementation Effects

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Yeast rich (YPD) and synthetic (S) minimal media with 2% dextrose (SD) were prepared as described 37 (link). Spermidine (Sigma-Aldrich), spermine (Sigma-Aldrich), DFMO (kindly provided by Dr. Patrick Woster), or CuSO₄were added to the media at various concentrations as indicated. Strains and plasmids used in this study are listed in tables S1 and S2, respectively, in the supplementary information.

Beenukumar R.R., Gödderz D., Palanimurugan R, & Dohmen R.J. (2015). Polyamines directly promote antizyme-mediated degradation of ornithine decarboxylase by the proteasome. Microbial Cell, 2(6), 197-207.

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Dose-response analysis of spermine and BIOD303

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To measure the dose-response curvesof spermine (Sigma) and BIOD303, serial dilutions of each concentrated stock compound were prepared. Each compound was added to a well to produce the indicated final concentration. For spermine, the range of concentrations tested was 10 μm, 30 μm, 100 μm, 300 μm, 1 mm, 3 mm, and 10 mm. For BIOD303 the concentration range was 5 μm, 32.5 μm, 62.5 μm, 125 μm, 250 μm, 500 μm, and 1 mm. Concentrations were then converted to logarithmic scale and the percent change at each concentration was plotted in Prism (GraphPad Software, La Jolla, CA) using a non-linear regression fit for log (agonist) versus normalized response. The data were normalized so that the values for the lowest concentration and the highest concentration were set to 0 and 100%, respectively. EC₅₀ values were calculated empirically using the software.

Moree B., Yin G., Lázaro D.F., Munari F., Strohäker T., Giller K., Becker S., Outeiro T.F., Zweckstetter M, & Salafsky J. (2015). Small Molecules Detected by Second-Harmonic Generation Modulate the Conformation of Monomeric α-Synuclein and Reduce Its Aggregation in Cells. The Journal of Biological Chemistry, 290(46), 27582-27593.

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Optimized Protein Extraction from HepG2 Cells

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Stable cell lines were grown to 80% confluence in 150 mm Petri dishes. Sample preparation and protein extraction were optimized using non-transfected HepG2 cells. The optimizations regarded cell harvesting (scraping vs. in situ lysis), cell disruption (freeze/thaw vs. tip sonication), and washing and lysis buffer. All chemicals were purchased from GE Healthcare (Munich, Germany) unless otherwise specified. Sample buffer components tested included the reducing/oxidizing agent (DTT vs. HED), spermine (Sigma-Aldrich, Taufkirchen, Germany), benzonase (Sigma-Aldrich), as well as the detergent assortment of the ProteoPrep detergent sampler kit (Sigma-Aldrich). Following the optimized protocols, cells were washed three times with Tris buffered sucrose solution containing protease and phosphatase inhibitors (2 mM PMSF—Sigma-Aldrich, 1 mM NaF—Sigma-Aldrich and 0.2 mM Na₃VO₄—Merck, Darmstadt, Germany) and detached with a cell-scraper in the same buffer. Cells were pelleted, then resuspended in 1 ml lysis buffer (7 M urea, 2 M thiourea, 4% CHAPS, 100 mM DTT, 25 mM spermine and 0.5% Pharmalyte 3–10) and disrupted by tip sonication on ice (5 x 30 second cycles 90% of time at 70% power). After 1 h incubation on ice, the protein extract was centrifuged for 30 min at 40000 x g and 4°C and proteins were quantified using RC-DC Quant kit (Bio-Rad, Munich, Germany).

Bertram K., Valcu C.M., Weitnauer M., Linne U, & Görlach A. (2015). NOX1 Supports the Metabolic Remodeling of HepG2 Cells. PLoS ONE, 10(3), e0122002.

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