2. Sachs SM, Morton JH, Schwartz SI: Acute mesenteric ischemia. Surgery 1982, 92:646–653.PubMed 3. Park WM, Gloviczki P, Cherry KJ: Contemporary management of acute mesenteric ischemia: Factors associated with survival. J Vasc Surg 2002, 35:445–452.Entinostat datasheet PubMedCrossRef 4. Kirkpatrick ID, Kroeker MA, Greenberg HM: Biphasic CT with mesenteric CT angiography in the evaluation of acute mesenteric ischemia: initial experience. Radiology 2003, 229:91–98.PubMedCrossRef 5. Ofer A: Multidetector CT, angiography in the evaluation of acute mesenteric ischemia. Eur Radiol 2009, 19:24–30.PubMedCrossRef 6. Schoots IG, Levi MM, Reekers JA: Thrombolytic therapy for acute superior mesenteric artery occlusion.

J Vasc Interv Radiol 2005, 16:317–329.PubMedCrossRef 7. Resch PFT�� manufacturer TA, Acosta S, Sonesson B: Endovascular techniques in acute arterial mesenteric ischemia. Semin Vasc Surg 2010, 23:29–35.PubMedCrossRef 8. Sauerland S, Agresta F, Bergamaschi

R: Laparoscopy for abdominal emergencies: Savolitinib chemical structure evidence-based guidelines of the European Association for Endoscopic Surgery. Surg Endosc 2006, 20:14–29.PubMedCrossRef 9. Yanar H, Taviloglu K, Ertekin C: Planned second-look laparoscopy in the management of acute mesenteric ischemia. World J Gastroenterol 2007, 13:3350–3353.PubMed 10. Howard TJ, Plaskon LA, Wiebke EA: Nonocclusive mesenteric ischemia remains a diagnostic dilemma. Am J Surg 1996, 171:405–408.PubMedCrossRef Celecoxib 11. Bjorck M, Acosta S, Lindberg F: Revascularization of the superior mesenteric artery after acute thromboembolic occlusion. Br J Surg 2002, 89:923–927.PubMedCrossRef 12. Giannetti A, Biscontri M, Randisi P: Contrast-enhanced sonography in the diagnosis of acute mesenteric ischemia: case report. J Clin Ultrasound 2010, 38:156–160.PubMed 13. Aschoff AJ, Stuber G, Becker

BW: Evaluation of acute mesenteric ischemia: accuracy of biphasic mesenteric multi-detector CT angiography. Abdom Imaging 2009, 34:345–357.PubMedCrossRef 14. Myers MC: Acute mesenteric ischemia: diagnostic approach and surgical treatment. Semin Vasc Surg 2010, 23:9–20.CrossRef 15. Arthurs ZM, Titus J, Bannazadeh M: A comparison of endovascular revascularization with traditional therapy for the treatment of acute mesenteric ischemia. J Vasc Surg 2011, 53:698–704.PubMedCrossRef 16. Cortese B, Limbruno U: Acute mesenteric ischemia: primary percutaneous therapy. Catheter Cardiovasc Interv 2010, 75:283–285.PubMedCrossRef 17. Berland T, Oldenburg WA: Acute mesenteric ischemia. Curr Gastroenterol Rep 2008, 10:341–346.PubMedCrossRef 18. Herbert GS, Steele SR: Acute and chronic mesenteric ischemia. Surg Clin North Am 2007, 87:1115–1134.PubMedCrossRef Competing interests All authours have no conflict of interests. Authors’ contributions FY, OA writting of the manuscript. OA and ISS conception and design of the manuscript, OA and ISS acquisition of data analiying and interpretation of data. ES follow up the patients.

p16INK4a specifically binds to the cyclin-dependent kinases CDK4/6, thereby inhibiting the phosphorylation of the retinoblastoma protein (pRB) and causing cell-cycle arrest at the G1 phase [5]. p14ARF interacts with MDM2, which targets p53 for degradation, thereby inducing p53-dependent cell-cycle arrest in both G1 and G2 Luminespib concentration phases [6, 7]. p53 participates in a wide range of activities including growth arrest, DNA repair and apoptosis and nearly 50% of human tumors have defects in p53 [8]. Less is known about p12; check details pRB-independent growth suppression by p12 was reported in pancreatic cells,

but the tumor suppressive and cell-cycle effects of this protein are as yet unclear [4]. Figure 1 The three transcriptional variants of CDKN2A. The CDKN2A gene located at 9p21 generates three transcriptional variants at transcription: p16INK4a, p14ARF and p12. p16INK4a utilizes exon1α, and p14ARF utilizes exon 1β which is about 20 kb upstream of exon 1α. p16INK4a and p14ARF share common exon 2 and exon 3 but use different reading frames. p12 uses an alternative splice donor site within intron1 of p16INK4a. The CDKN2A locus is frequently inactivated in a wide variety of tumors[9–12]. Kamb examined 290 tumor cell lines and detected CDKN2A deletion in 133 of them [13]. Park examined 31 non-small cell lung cancer (NSCLC) cell lines and found that the inactivation rate

of p16INK4a and p14ARF was 84% and 55% respectively. Significantly, p16INK4a was inactivated in all cell lines in which p14ARF was inactivated[14]. Montelukast Sodium Conversely, restoration of the transcripts in tumors with endogenous expression

deficiency https://www.selleckchem.com/products/sch772984.html has been shown to reverse the malignant phenotypes of many tumors. In lung cancer cells, for examples, Zhang X et al restored the expression of p16INK4a in A549 cells and showed that p16INK4a could suppress cell growth and block G1-S cell cycle transition both in vitro and in vivo[15]. Elevated p16INK4a protein expression also enhanced the sensitivity to cisplatin treatment of NSCLC cells[16]. Xie Qi-chao et al co-transfected p16INK4a and p14ARF into the A549 cells and found that cell growth arrest and apoptosis were induced [17]. As for p12, little is known about its status and tumor-suppressive effects. Keith et al transfected a p12 eukaryotic expression vector into C-33A and PANC-1 cells and found that the expression of the protein suppressed cell growth by 40% and 60%, respectively, and found no relationship with RB state. While all three transcripts are potential tumor suppressors in different genetic backgrounds, they may have different effects and mechanisms. So far, the activity of the transcriptional variants under the same condition has not been studied, nor is it known which variant has the strongest suppression effect. Inactivation of the CDKN2A locus has been shown to efficiently impair expression of the three transcripts simultaneously [18].

We are now interested in CD151’s role in PCa as a motility and metastasis promoter. Human PCa cell lines LNCaP and PC3 were used in cell migration and invasion

assays (Matrigel membrane; BD). The motility and invasiveness of wild-type LNCaP (low endogenous level of CD151) vs. CD151 transfected LNCaP cells and PC3 (high endogenous level of CD151) vs. CD151 knock-down PC3 cells (KD PC3) was analyzed. LNCaPs transfected with CD151 showed increased cell motility and invasion compared to control LNCaPs (P < 0.05), while KD PC3 cells demonstrated reduced cell motility and invasion compared Selleck SCH772984 to control PC3s (P < 0.05). Currently, paired primary and secondary PCa tumors generated using a SCID mouse model bearing implanted human PCa cell lines are being examined ABT-263 purchase for expression of CD151, and its relationship to the density of blood and lymphatic vasculature markers assessed using immunohistochemistry. Although its mechanism in tumor progression is still unknown, CD151 could be a valuable biological marker for the prognosis of PCa.

1 Maecker HT et al. FASEB J. (1997) 11: 428–442 2 Testa JE et al. Cancer Research (1999) 59: 3812–3820 3 Ang J et al. Cancer Epidemiol Biomarkers & JPH203 ic50 Prevention (2004) 13: 1717–21 Poster No. 67 – Cancelled Poster No. 68 Bone Marrow Mesenchymal Stem Cells are Altered in B-Cell Chronic Lymphocytic Leukemia Cytidine deaminase Frédérique Dubois-Galopin 1 , Richard Veyrat-Masson1, Céline Pebrel-Richard1, Jean-Jacques Guérin1, Laurent Guillouard1, Jacques Chassagne1, Jacques-Olivier Bay2, Olivier Tournilhac2, Karin Tarte3, Marc Berger1 1 Hematoly Biology, CHU Clermont-Ferrand,

Clermont-Ferrand, France, 2 Hematology, CHU Clermont-Ferrand, Clermont-Ferrand, France, 3 INSERM U917-MICA, Faculté de médecine, Rennes, France In B-cell chronic lymphocytic leukemia (B-CLL), malignant cells are not susceptible to apoptosis in vivo, while they die rapidly in vitro in the absence of specialized non-hematopoietic feeder cells, such as mesenchymal stem cells (MSC). Recent observations have suggested that there is a functional relationship between B cell clone and the bone marrow (BM) stroma. We have thus compared BM-MSC obtained from B-CLL patients and healthy subjects. We found that most BM-MSC cultures from B-CLL patients failed under standard culture conditions, in contrast with normal BM. In agreement, CD45negCD14negCD73pos cells in unmanipulated BM samples (subset previously shown to contain CFU-F (Veyrat-Masson et al., BJH, 2007)), were under the threshold of detection in most of B-CLL BM samples. In productive cultures, we found more CFU-F from B-CLL formed by large, polygonal MSC. These cells proliferated poorly and in most cases could not be further amplified.

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M, Menand A, Blavette D, Deconihout B: Design of a femtosecond laser assisted tomographic atom probe. Rev Sci Instrum 2006,77(4):043705.CrossRef 25. Talbot E, Roussel M, Genevois C, Pareige P, Khomenkova L, Portier Selleck JAK inhibitor X, Gourbilleau F: Atomic

scale observation of phase separation and formation of silicon clusters in Hf high-κ silicates. J Appl Phys 2012,111(10):103519.CrossRef 26. Cadel E, Vurpillot F, Larde R, Duguay S, Deconihout B: Depth resolution function of the laser assisted tomographic atom probe in the investigation of semiconductors. J Appl Phys 2009,106(4):044908.CrossRef 27. Cadel E, Barreau N, Kessler J, Pareige P: Atom probe study of sodium distribution in polycrystalline Cu(In,Ga)Se2 thin film. Acta Materialia 2010,58(7):2634–2637.CrossRef 28. Lardé R, Talbot E, Pareige P, Bieber H, Schmerber G, Colis S, Trichostatin A concentration Pierron-Bohnes V, Dinia A: Evidence of superparamagnetic Co clusters in pulsed Mirabegron laser deposition-grown Zn0.9Co0.1O thin films using atom probe tomography. J Am Chem MK-8776 mw Soc 2011,133(5):1451–1458.CrossRef 29. Hijazi K, Rizk R, Cardin J, Khomenkova L, Gourbilleau F: Towards an optimum coupling between Er ions and Si-based sensitizers for integrated active photonics. J Appl Phys 2009,106(2):024311.CrossRef 30. Vurpillot F, Bostel A, Blavette D: Trajectory overlaps and local magnification in three-dimensional atom probe. Appl Phys Lett 2000,76(21):3127–3129.CrossRef 31. Tsoukalas D, Tsamis C, Normand P: Diffusivity measurements of silicon dioxide layers

using isotopically pure material. J Appl Phys 2001, 89:7809.CrossRef 32. Tsoukalas D, Tsamis C, Normand P: Use of isotopically pure silicon material to estimate silicon diffusivity in silicon dioxide. Mater Res Soc Symp Proc 2001, 669:J.3.7.1.CrossRef 33. Xu F, Xiao Z, Cheng G, Yi Z, Zhang T, Gu L, Wang X: Erbium-doped silicon-rich silicon dioxide/silicon thin films fabricated by metal vapour vacuum arc ion source implantation. J Phys: Condensed Matter 2002,14(3):L63-L69.CrossRef 34. Kashtiban RJ, Bangert U, Crowe I, Halsall MP, Sherliker B, Harvey AJ, Eccles J, Knights AP, Gwilliam R, Gass M: Structural and compositional study of erbium-doped silicon nanocrystals by HAADF , EELS and HRTEM techniques in an aberration corrected STEM. J Phys: Conf Series 2009, 209:012043.CrossRef 35.

Vaccine 2007, 25:6842–6844.PubMedCrossRef 13. Andersen P, Doherty TM: The success and failure of BCG – implications for a novel tuberculosis vaccine. Nat Rev Microbiol 2005,

3:656–662.PubMedCrossRef 14. Antas PR, Castello-Branco LR: New vaccines against tuberculosis: lessons learned from BCG immunisation in Brazil. Trans R Soc Trop Med Hyg 2008, 102:628–630.PubMedCrossRef 15. Castillo-Rodal AI, Castanon-Arreola M, Hernandez-Pando R, Calva JJ, Sada-Diaz E, Lopez-Vidal Y: Mycobacterium bovis BCG substrains confer different levels of protection against Mycobacterium tuberculosis Sotrastaurin cost infection in a BALB/c model of progressive pulmonary tuberculosis. Infect Immun 2006, 74:1718–1724.PubMedCrossRef 16. Rodriguez-Alvarez M, Mendoza-Hernandez G, Encarnacion S, Calva JJ, Lopez-Vidal Y: Phenotypic differences between BCG vaccines at the proteome level. Tuberculosis (Edinb) 2009, buy Poziotinib 89:126–135.CrossRef 17. Brandt L, Feino Cunha J, Weinreich Olsen A, Chilima B, Hirsch P, Appelberg R, Andersen P: Failure of the Mycobacterium bovis BCG vaccine: some species of environmental mycobacteria block multiplication of BCG and induction of protective immunity to tuberculosis. Infect Immun 2002, 70:672–678.PubMedCrossRef 18. Colditz GA, Brewer TF, Berkey CS, Wilson

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b Comparison of gene expression with (+) and without (-) glucose, genes with a +/- ratio of ≤ 0.5 or ≥2 in the wild-type and the mutant were considered to be regulated) * Genes containing putative cre-sites Metabolic pathways under the control of CcpA In S. aureus, glucose

is mainly catabolized to pyruvate via glycolysis [30] (Fig. 4). The PLX-4720 mouse enzymes catalyzing the central parts of glycolysis of S. aureus are encoded by five genes: a glyceraldehyde-3-phosphate dehydrogenase (gap), phosphoglycerate kinase (pgk), triosephosphate isomerase (tpi), phosphoglyceromutase (pgm), FDA-approved Drug Library cost and enolase (eno). We found that in the presence of glucose, only tpi and pgk were up-regulated by a factor of more than two in a CcpA-dependent manner (Fig. 4, Additional BMS345541 chemical structure file 4: CcpA-dependent up-regulation by glucose). The absence of putative cre-sites indicated indirect control by CcpA. The other glycolytic genes also tended to show an up-regulation in transcription in response to glucose, however, below the threshold-level, and this tendency was also observed for the mutant (see Additional file 4: CcpA-dependent up-regulation by glucose). Figure 4 Overview on CcpA- and glucose-dependent genes of glycolysis, gluconeogenesis and TCA cycle. Assignment of genes coding for enzymes of

glycolysis, gluconeogenesis and the TCA cycle which are regulated by CcpA. ackA, acetate kinase;acsA, acetyl-CoA synthetase; citB, aconitate hydratase; citC, citrate dehydrogenase; citG, fumarate hydratase; citZ, citrate synthase; eno, enolase; fbpA, fructose-bisphosphate aldolase; fbp, fructose-1,6-bisphosphatase; gap, glyceraldehyde-3-phosphate dehydrogenase; gapB, glyceraldehyde-3-phosphate dehydrogenase; glcK, glucokinase; mqo2, malate:quinone-oxidoreductase; odhA, 2-oxoglutarate dehydrogenase

component E1; odhB, 2-oxoglutarate dehydrogenase component E2; pckA, phosphoenolpyruvate carboxykinase; pdhABCD, pyruvate dehydrogenase; pfk, phosphofructokinase; pgi, glucose-6-phosphate isomerase; pgk, phosphoglycerate kinase; pgm, phosphoglycerate mutase; pycA, Erythromycin pyruvate carboxylase; pykA, pyruvate kinase; SA2155, malate:quinone-oxidoreductase; sdhA, succinate dehydrogenase; sucC, succinyl-CoA synthetase, beta subunit; sucD, succinyl-CoA synthetase, alpha subunit; tpi, triose-3-phosphate isomerase. *, genes with putative cre-sites; red, regulated genes. Our microarrays confirmed previous findings [24, 31], reporting a glucose-induced CcpA-mediated repression of PEP carboxykinase (pckA) (Fig. 4, Additional file 3: CcpA-dependent down-regulation by glucose), which is involved in gluconeogenesis.

Furthermore, some techniques to analyze the physiological BIBW2992 chemical structure status of the cells will be

summarized. Media, culture treatment, and illumination conditions In contrast to inducing micronutrient deficiency in C. reinhardtii, which takes a lot of effort to exclude trace amounts of metal ions from the growth medium (Quinn and Merchant 1998), it is not difficult to deprive C. reinhardtii cells of the macronutrient sulphur (S). Standard TAP medium (Harris 1989, 2009) contains about 0.5 mM of sulphate. 400 μM of the latter derive from the salt solution, and about 100 μM originates from the trace element solution, which contains sulphate salts of Zn, Cu, and Fe. To prepare S-free medium, AZD5363 in vivo the standard Selleckchem Bafilomycin A1 TAP recipe is used, but the Beijerinck’s salt solution is prepared with MgCl2 instead of using MgSO4. Accordingly, the trace element solution contains the chloride salts of Zn, Cu, and Fe. Double distilled water should be used for the preparation of the stock solutions and the media to avoid sulphate contamination. To induce S deprivation in C. reinhardtii, the cells are grown in standard TAP medium in the light and then transferred to S-free medium. For this purpose, the cells are centrifuged as described above, the supernatant is discarded, and the cell pellet is gently resuspended in the original volume of S-free medium. Another centrifugation

step follows, the supernatant is discarded once more, and the cells are resuspended in

S-free medium again. There are several philosophies on how many washing steps should be carried out. Some research groups carry out up to five washing steps (e.g., Kosourov et al. 2002), whereas others wash only once (Hemschemeier et al. 2008). It should be kept in mind that every centrifugation step affects the algal cells and may induce an anaerobic metabolism already, on the other hand, some sulphate might stick to the cells so that one washing Sitaxentan step could be insufficient to remove any S from the cells. The procedure might be chosen according to the experimental aims. An alternative approach to deprive algal cells of S is to inoculate them in a medium with a limited amount of sulphate (Zhang et al. 2002). We experienced that inoculating a low amount of C. reinhardtii cells grown in standard TAP medium in new medium containing 50 μM sulphate (by adding a sterile MgSO4 stock solution to S-free TAP medium) allows them to grow until they reach a chlorophyll content of about 20 μg ml−1. Then, they will pass to the S-deprived stage and induce the set of adaptations figured out below. There is an easy method to check whether the Chlamydomonas culture already experiences S starvation. Several green algal species such as C. reinhardtii secrete a periplasmatic arylsulfatase as soon as they sense limitations of sulphate (Lien and Schreiner 1975).

Procter & Gamble: speaking, consulting, research support (through the university). sanofi-aventis: speaking, consulting.. Frederick A Anderson: Research grant: sanofi-aventis: GRACE, GLOW, ENDORSE; The Medicines Company: STAT; Scios: Orthopedic Registry; Consultant/Advisory Board: sanofi-aventis, Scios,

GlaxoSmithKline, The Medicines Company, Millennium Pharmaceuticals. Pierre Delmas: None Open Access This article CX-5461 mouse is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited. References 1. Hays J, Hunt JR, Hubbell FA, Anderson GL, Limacher M, Allen C, Rossouw JE (2003) The Women’s Health Initiative recruitment methods and results. Ann Epidemiol 13:S18–S77PubMedCrossRef 2. Cummings SR, Nevitt MC, Browner WS, Stone K, Fox KM, Ensrud KE, Cauley J, Black

D, Vogt TM (1995) Risk factors for hip fracture in white women. Study of osteoporotic fractures research AZ 628 cost group. N Engl J Med 332:767–773PubMedCrossRef 3. Tanko LB, Bagger YZ, Nielsen SB, Christiansen C (2003) Does serum cholesterol contribute to vertebral bone loss in postmenopausal women? Bone 32:8–14PubMedCrossRef 4. European Prospective Osteoporosis Study Group (2002) Incidence of vertebral fracture in Europe: results from the European Prospective Osteoporosis Study (EPOS). J Bone Miner Res 17:716–724CrossRef 5. Hofman A, Grobbee DE, de Jong PT, van den Ouweland FA (1991) Determinants of disease and disability in the elderly: the Rotterdam Elderly Study. Eur J Epidemiol 7:403–422PubMedCrossRef 6. O’Neill TW, Felsenberg D, Varlow J, Cooper C, Kanis JA, Silman AJ (1996) The prevalence of vertebral deformity in European men and women: the European Vertebral Osteoporosis Study. J Bone Miner Res 11:1010–1018PubMedCrossRef 7. Ismail AA, Pye SR, Cockerill WC, Lunt Carnitine palmitoyltransferase II M, Silman AJ, Reeve J, Banzer D, Benevolenskaya LI, Bhalla A, Bruges Armas J, Cannata JB, Cooper C, Delmas PD, see more Dequeker J, Dilsen G, Falch JA, Felsch B, Felsenberg D, Finn JD, Gennari C, Hoszowski K, Jajic I, Janott J, Johnell O, Kanis JA, Kragl

G, Lopez Vaz A, Lorenc R, Lyritis G, Marchand F, Masaryk P, Matthis C, Miazgowski T, Naves-Diaz M, Pols HA, Poor G, Rapado A, Raspe HH, Reid DM, Reisinger W, Scheidt-Nave C, Stepan J, Todd C, Weber K, Woolf AD, O’Neill TW (2002) Incidence of limb fracture across Europe: results from the European Prospective Osteoporosis Study (EPOS). Osteoporos Int 13:565–571PubMedCrossRef 8. Adachi JD, Loannidis G, Berger C, Joseph L, Papaioannou A, Pickard L, Papadimitropoulos EA, Hopman W, Poliquin S, Prior JC, Hanley DA, Olszynski WP, Anastassiades T, Brown JP, Murray T, Jackson SA, Tenenhouse A (2001) The influence of osteoporotic fractures on health-related quality of life in community-dwelling men and women across Canada. Osteoporos Int 12:903–908PubMedCrossRef 9.

Gametocytogenesis was induced following the procedure of Cyclosporin A Ifediba and Vanderberg [32]. Mature gametocyte cultures (stages IV and V) that were 14–16 days old were used to feed mosquitoes in 37°C warmed membrane feeders for 30 minutes. To determine the level of infection, the midguts were dissected and stained with 0.05% (w/v) mercurochrome in water and oocysts counted by light microscopy 7–9 days post blood feeding. Distribution of oocyst numbers per midgut was analyzed using the Kolmogorov-Smirnov test.

dsRNA synthesis cDNA fragments of 500–600 bp were amplified for each gene using the primers shown in Additional File 1 and cDNA from 4-day-old An. gambiae females as template. The cDNA fragments were cloned into the pCR II-TOPO® vector (Invitrogen, Carlsbad, CA) and T7 sites introduced

at both ends using the following vector primers (5′ to 3′) to amplify the cDNA insert; M13-Fw: GTAAAACGACGGCCAGT and T7-M13Rev: CTCGAGTAATACGACTCACTA find more TAGGGCAGGAAACAGCTATGAC. dsRNA was synthesized and purified using the MEGAscript kit (Ambion, Austin, TX). The eluted dsRNA was further cleaned and concentrated to 3 μg/μl using a Microcon YM-100 filter (Millipore, Bedford, MA). Silencing An. gambiae genes dsRNA (207 ng in 69 nl) for each of the genes tested was injected into the thorax of cold-anesthetized 1- to 2-day-old female mosquitoes using a nano-injector (Nanoject; Drummond Scientific, Broomall, PA). In each experiment, a control group was injected with dsLacZ or dsGFP to serve as reference for intensity of infection. Gene silencing was confirmed 4 days after dsRNA injection by RT-qPCR using the ribosomal S7 gene for normalization. Poly(A) mRNA was isolated from groups of 10 adult females using Oligotex-dT beads (Qiagen, Valencia, CA) following the manufacturer’s instructions. First-strand cDNA was synthesized using random hexamers and Superscript II reverse transcriptase (Invitrogen). The primers

used for each gene are shown in Additional File 2. Gene expression was assessed by SYBR green qPCR (DyNAmo HS; New England Biolabs, Beverly, MA) in a Chromo4 system (Bio-Rad). PCR involved an initial denaturation Resveratrol at 95°C for 15 minutes, 44 cycles of 10 seconds at 94°C, 20 seconds at 58°C, and 30 seconds at 72°C. Fluorescence readings were taken at 72°C after each cycle. A final extension at 72°C for 5 minutes was completed before deriving a melting curve (70°C–95°C) to confirm the identity of the PCR product. qPCR measurements were made in duplicate. Silencing An. stephensi genes Because all the genes tested are highly conserved Compound C across species, we tested whether it was possible to silence An. stephensi genes by injecting them with dsRNA from orthologous genes of An. gambiae. An. stephensi female mosquitoes (1–2 days old) were injected with dsRNA from An. gambiae cDNAs following the same procedure described above. Silencing efficiency was determined using qPCR 4 days after mosquitoes were injected with dsRNA.

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