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Journal articles on the topic 'Saligenin'

Author: Grafiati

Published: 18 May 2024

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1

Bakker, Daniël J., Arghya Dey, Daniel P. Tabor, Qin Ong, Jérôme Mahé, Marie-Pierre Gaigeot, Edwin L. Sibert, and Anouk M. Rijs. "Fingerprints of inter- and intramolecular hydrogen bonding in saligenin–water clusters revealed by mid- and far-infrared spectroscopy." Physical Chemistry Chemical Physics 19, no. 31 (2017): 20343–56. http://dx.doi.org/10.1039/c7cp01951c.

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2

Saragi, Rizalina Tama, Marcos Juanes, José Luis Abad, Alberto Lesarri, Ruth Pinacho, and José Emiliano Rubio. "Rotational spectroscopy of organophosphorous chemical agents: cresyl and phenyl saligenin phosphates." Physical Chemistry Chemical Physics 21, no. 30 (2019): 16418–22. http://dx.doi.org/10.1039/c9cp03093j.

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Cresyl and phenyl saligenin phosphate have been probed in a jet expansion by broadband chirp-excitation microwave spectroscopy, revealing the most stable confirmations and their structural properties.

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3

Glynn, P., D. J. Read, R. Guo, S. Wylie, and M. K. Johnson. "Synthesis and characterization of a biotinylated organophosphorus ester for detection and affinity purification of a brain serine esterase: neuropathy target esterase." Biochemical Journal 301, no. 2 (July 15, 1994): 551–56. http://dx.doi.org/10.1042/bj3010551.

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We have synthesized a novel stable precursor, saligenin phosphorotrichloridate, which, on reaction with N-monobiotinyldiamines, generates a series of biotinylated covalent inhibitors of serine esterases. A homologue designated S9B [1-(saligenin cyclic phospho)-9-biotinyldiaminononane] was selected to allow detection and rapid isolation of neuropathy target esterase (NTE). This enzyme is the primary target site for those organophosphorus esters (OPs) which cause delayed neuropathy. NTE comprises about 0.03% of the total protein in brain microsomal fractions and has resisted purification attempts over many years. S9B is a potent progressive inhibitor of NTE esteratic activity (second-order rate constant 1.4 x 10(7) M-1.min-1). Incubation of S9B with brain microsomes led to specific covalent labelling of NTE as determined by detection of a biotinylated 155 kDa polypeptide on Western blots. Specificity of S9B labelling was further demonstrated by inhibition with the neuropathic OP mipafox. Biotinyl-NTE in SDS-solubilized S9B-labelled microsomes was adsorbed on to avidin-Sepharose and subsequently eluted, yielding a fraction enriched approx. 1000-fold in NTE by a single step with recoveries of 30%. Essentially pure NTE was obtained after separation from two endogenous biotinylated polypeptides (120 and 70 kDa) in avidin-Sepharose eluates by preparative SDS/PAGE. Other biotinylated saligenin phosphoramidates derived from the same precursor may be useful for detection and isolation of other serine esterases and proteinases.

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4

Singh, Vishwakarma, Punitha Vedantham, and Pramod K. Sahu. "A novel stereoselective total synthesis of (±)-hirsutene from saligenin." Tetrahedron Letters 43, no. 3 (January 2002): 519–22. http://dx.doi.org/10.1016/s0040-4039(01)02183-9.

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5

Lushchekina, S. V., V. S. Polomskikh, S. D. Varfolomeev, and P. Masson. "Molecular modeling of butyrylcholinesterase inhibition by cresyl saligenin phosphate." Russian Chemical Bulletin 62, no. 11 (November 2013): 2527–37. http://dx.doi.org/10.1007/s11172-013-0366-9.

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6

Shiotsuki, Takahiro, Takeshi Kakimoto, and Morifusa Eto. "Irreversible inactivation of glutathione transferases by saligenin cyclic phosphates." Pesticide Biochemistry and Physiology 42, no. 2 (February 1992): 119–27. http://dx.doi.org/10.1016/0048-3575(92)90059-9.

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7

SHIOTSUKI, Takahiro. "Mode of Action of Saligenin Cyclic Phosphates on Organophosphate-Resistant Houseflies." Journal of Pesticide Science 16, no. 3 (1991): 523–31. http://dx.doi.org/10.1584/jpestics.16.523.

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8

Lidsky, T. I., C. Manetto, and M. Ehrich. "Nerve conduction studies in chickens given phenyl saligenin phosphate and corticosterone." Journal of Toxicology and Environmental Health 29, no. 1 (January 1990): 65–75. http://dx.doi.org/10.1080/15287399009531372.

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9

Torgul, M., M. SÜnkÜr, F. B. Kaynak, H. HosgOren, and S. Ozbey. "Saligenin derivative borocryptands: synthesis and structural analysis of new type lithium borocryptate." Journal of Chemical Research (Miniprint) 2003, no. 10 (October 1, 2003): 605. http://dx.doi.org/10.3184/030823503322655670.

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10

Togrul, M., M. SÜnkÜr, F. B. Kaynak, H. HosgOren, and S. Ozbey. "Saligenin derivative borocryptands: synthesis and structural analysis of new type lithium borocryptate." Journal of Chemical Research 2003, no. 10 (October 1, 2003): 605. http://dx.doi.org/10.3184/030823403322655770.

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11

SHIOTSUKI, Takahiro, Akihiro KOISO, and Morifusa ETO. "Glutathione Conjugation as a Mechanism for Glutathione Transferase Inhibition by Saligenin Cyclic Phosphates." Journal of Pesticide Science 14, no. 3 (1989): 337–44. http://dx.doi.org/10.1584/jpestics.14.337.

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12

Xu, Lin-Lin, Meng-Ling Liu, Jing-Lei Wang, Mei Yu, and Jia-Xiang Chen. "Saligenin cyclic-o-tolyl phosphate (SCOTP) induces autophagy of rat spermatogonial stem cells." Reproductive Toxicology 60 (April 2016): 62–68. http://dx.doi.org/10.1016/j.reprotox.2016.01.004.

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13

Jortner, B. S., and M. Enrich. "PATHOLOGICAL EFFECTS OF PHENYL SALIGENIN PHOSPHATE, A POTENT NEUROTOXIC CONGENER OF TRIORTHOTOLYL PHOSPHATE." Journal of Neuropathology and Experimental Neurology 45, no. 3 (May 1986): 359. http://dx.doi.org/10.1097/00005072-198605000-00134.

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14

Flaskos, John, Magdalini Sachana, Michèle Pen, Wayne C. Harris, and Alan J. Hargreaves. "Effects of phenyl saligenin phosphate on phosphorylation of pig brain tubulin in vitro." Environmental Toxicology and Pharmacology 22, no. 1 (July 2006): 70–74. http://dx.doi.org/10.1016/j.etap.2005.12.006.

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15

Saracila, Mihaela, Tatiana Dumitra Panaite, Camelia Puia Papuc, and Rodica Diana Criste. "Heat Stress in Broiler Chickens and the Effect of Dietary Polyphenols, with Special Reference to Willow (Salix spp.) Bark Supplements—A Review." Antioxidants 10, no. 5 (April 27, 2021): 686. http://dx.doi.org/10.3390/antiox10050686.

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Over the last decade, there has been a growing interest in the use of a wide range of phytoadditives to counteract the harmful effects of heat stress in poultry. Willow (Salix spp.) is a tree with a long history. Among various forms, willow bark is an important natural source of salicin, β-O-glucoside of saligenin, but also of polyphenols (flavonoids and condensed tannins) with antioxidant, antimicrobial, and anti-inflammatory activity. In light of this, the current review presents some literature data aiming to: (1) describe the relationship between heat stress and oxidative stress in broilers, (2) present or summarize literature data on the chemical composition of Salix species, (3) summarize the mechanisms of action of willow bark in heat-stressed broilers, and (4) present different biological effects of the extract of Salix species in different experimental models.

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16

Bosak, Anita, Anamarija Knežević, Ivana Gazić Smilović, Goran Šinko, and Zrinka Kovarik. "Resorcinol-, catechol- and saligenin-based bronchodilating β2-agonists as inhibitors of human cholinesterase activity." Journal of Enzyme Inhibition and Medicinal Chemistry 32, no. 1 (January 1, 2017): 789–97. http://dx.doi.org/10.1080/14756366.2017.1326109.

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17

Knežević, Anamarija, Jurica Novak, Anita Bosak, and Marijana Vinković. "Structural isomers of saligenin-based β2-agonists: synthesis and insight into the reaction mechanism." Organic & Biomolecular Chemistry 18, no. 47 (2020): 9675–88. http://dx.doi.org/10.1039/d0ob02095h.

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18

Burka, Leo T., and Robert E. Chapin. "Toxicokinetics of [14C]-saligenin cyclic-o-tolyl phosphate in anesthetized male F-344 rats." Reproductive Toxicology 7, no. 1 (January 1993): 81–86. http://dx.doi.org/10.1016/0890-6238(93)90013-w.

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19

Procopiou, Panayiotis A., Victoria J. Barrett, Alison J. Ford, Brian E. Looker, Gillian E. Lunniss, Deborah Needham, Claire E. Smith, and Graham Somers. "The discovery of long-acting saligenin β2 adrenergic receptor agonists incorporating a urea group." Bioorganic & Medicinal Chemistry 19, no. 20 (October 2011): 6026–32. http://dx.doi.org/10.1016/j.bmc.2011.08.043.

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20

Kuran, Witold, and Ewa Mazanek. "Synthesis of novel monomeric zinc—oxygen compounds containing diethylzinc and pyrocatechol or saligenin moieties." Journal of Organometallic Chemistry 384, no. 1-2 (February 1990): 13–17. http://dx.doi.org/10.1016/0022-328x(90)87048-i.

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21

Kakimoto, Takeshi, Takahiro Shiotsuki, and Morifusa Eto. "Reaction of Saligenin Cyclic Phosphorus Esters with Some Amino Acids and Purine and Pyrimidine Bases." Journal of the Faculty of Agriculture, Kyushu University 37, no. 3/4 (March 1993): 371–77. http://dx.doi.org/10.5109/24030.

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22

Mentzschel, Anke, Gabi Schmuck, Wolfgang Dekant, and Dietrich Henschler. "Genotoxicity of neurotoxic triaryl phosphates: Identification of DNA adducts of the ultimate metabolites, saligenin phosphates." Chemical Research in Toxicology 6, no. 3 (May 1993): 294–301. http://dx.doi.org/10.1021/tx00033a007.

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23

Procopiou, Panayiotis A., Victoria J. Barrett, Nicola J. Bevan, Peter R. Butchers, Richard Conroy, Amanda Emmons, Alison J. Ford, et al. "The discovery of long-acting saligenin β2 adrenergic receptor agonists incorporating hydantoin or uracil rings." Bioorganic & Medicinal Chemistry 19, no. 14 (July 2011): 4192–201. http://dx.doi.org/10.1016/j.bmc.2011.05.064.

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24

Bursian, S. J., E. J. Lehning, L. Correll, and M. Ehrich. "Effect of β‐naphthoflavone ono‐tolyl saligenin phosphate‐induced delayed neuropathy in two lines of chickens." Journal of Toxicology and Environmental Health 28, no. 4 (December 1989): 461–71. http://dx.doi.org/10.1080/15287398909531364.

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25

Shiotsuki, Takahiro, Akihiro Koiso, and Morifusa Eto. "Inhibition of glutathione transferase by S-benzyl glutathione analogous to the conjugate of saligenin cyclic phosphate." Pesticide Biochemistry and Physiology 37, no. 2 (June 1990): 121–29. http://dx.doi.org/10.1016/0048-3575(90)90117-k.

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26

Rishina, Laura A., Svetlana S. Lalayan, Svetlana C. Gagieva, Vladislav A. Tuskaev, Evgeniya O. Perepelitsyna, and Yury V. Kissin. "Polymers of propylene and higher 1-alkenes produced with post-metallocene complexes containing a saligenin-type ligand." Polymer 54, no. 24 (November 2013): 6526–35. http://dx.doi.org/10.1016/j.polymer.2013.09.052.

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27

Felemban, Shatha G., A. Christopher Garner, Fathi A. Smida, David J. Boocock, Alan J. Hargreaves, and John M. Dickenson. "Phenyl Saligenin Phosphate Induced Caspase-3 and c-Jun N-Terminal Kinase Activation in Cardiomyocyte-Like Cells." Chemical Research in Toxicology 28, no. 11 (October 23, 2015): 2179–91. http://dx.doi.org/10.1021/acs.chemrestox.5b00338.

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28

Pruett, Stephen B., and Janice E. Chambers. "Effects of paraoxon, p-nitrophenol, phenyl saligenin cyclic phosphate, and phenol on the rat interleukin 2 system." Toxicology Letters 40, no. 1 (January 1988): 11–20. http://dx.doi.org/10.1016/0378-4274(88)90178-6.

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29

Ehrich, Marion, Linda Shell, Michael Rozum, and B. S. Jortner. "Short-term Clinical and Neuropathologic Effects of Cholinesterase Inhibitors in Rats." Journal of the American College of Toxicology 12, no. 1 (January 1993): 55–68. http://dx.doi.org/10.3109/10915819309140622.

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Adult male Long Evans rats were given a single administration of 3 dosage levels of the organophosphorus compounds tri-ortho-tolyl phosphate (TOTP), diisopropyl fluorophosphate (DFP), phenyl saligenin phosphate (PSP), mipafox, malathion, and dichlorvos or the carbamate carbaryl. Acetylcholinesterase and neurotoxic esterase activities were inhibited in a dose-dependent manner, with the highest dosages of all of these compounds inhibiting activities of these enzymes in brain by at least 37% and 64%, respectively, at 4 and 48 hours after administration. Rats given the high doses of TOTP (1000 mg/kg), DFP (3 mg/kg), malathion (2000 mg/kg), and carbaryl (160 mg/kg) weighed significantly less than control rats 14 days after administration. A functional observational battery (FOB) was used to screen for neurotoxic effects 1, 2, and 3 weeks after exposure. All 7 test compounds were capable of causing changes in parameters indicative of behavioral and central nervous system excitability. In addition, dose-related alterations in response to approach were seen in rats given DFP, malathion, dichlorvos, and carbaryl. Mild to moderate myelinated fiber degeneration was seen in the rostral levels of the fasciculus gracilis in rats given TOTP, DFP, PSP and mipafox, but no significant neuropathologic lesions were noted in rats given dichlorvos, malathion, or carbaryl.

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30

Ducho, Christian, Jan Balzarini, Lieve Naesens, Erik De Clercq, and Chris Meier. "Aryl-Substituted and Benzo-Annulated CycloSal-Derivatives of 2′,3′-Dideoxy-2′,3′-Didehydrothymidine Monophosphate — Correlation of Structure, Hydrolysis Properties and Anti-HIV Activity." Antiviral Chemistry and Chemotherapy 13, no. 2 (April 2002): 129–41. http://dx.doi.org/10.1177/095632020201300206.

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The synthesis of phenyl-substituted and benzo-annulated cycloSal phosphate triesters of the nucleoside analogue 2′,3′-dideoxy-2′,3′-didehydrothymidine (d4T, Zerit™) as lipophilic, membrane-soluble pronucleotides is described. The cycloSal moiety was introduced by using cyclic chlorophosphite agents prepared from phenyl-substituted saligenin derivatives and orthohydroxymethylated naphthols, respectively. Hydrolysis studies (HPLC analysis) of the triesters 2, 3 showed a range of hydrolytic stability from 1.4 h up to 5.1 h and the stability could be correlated with the substitution pattern in the cycloSal moiety. A slight decrease of their stability was observed, if phenyl-substituted derivatives were hydrolyzed in human CEM/O cell extracts. D4T and thymine, possible products of enzymatic cleavage of the pronucleotides, were not detected in the cell extracts. A further investigation of the hydrolysis process was performed by 31P-NMR spectroscopy. This technique allowed a precise monitoring of the degradation products and the exact determination of the product ratio. Finally, the newly synthesized compounds were tested concerning their antiviral activity against HIV in vitro. A strong correlation of the hydrolysis properties and the antiviral activity was found. 3-phenyl- cycloSal-d4TMP showed a threefold increase in its anti-HIV-1 activity and retained full activity in thymidine kinase (TK) deficient cells, indicative of a successful TK-bypass.

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31

Massicotte, Christiane, David S. Barber, Bernard S. Jortner, and Marion Ehrich. "Nerve Conduction and ATP Concentrations in Sciatic-Tibial and Medial Plantar Nerves of Hens Given Phenyl Saligenin Phosphate." NeuroToxicology 22, no. 1 (February 2001): 91–98. http://dx.doi.org/10.1016/s0161-813x(00)00004-8.

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32

Kumar, Sumit, Santosh K. Singh, Camilla Calabrese, Assimo Maris, Sonia Melandri, and Aloke Das. "Structure of saligenin: microwave, UV and IR spectroscopy studies in a supersonic jet combined with quantum chemistry calculations." Physical Chemistry Chemical Physics 16, no. 32 (July 10, 2014): 17163. http://dx.doi.org/10.1039/c4cp01693a.

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33

Rishina, Laura, Svetlana Lalayan, Svetlana Gagieva, Vladislav Тuskaev, Alexander Shchegolikhin, Dimitri Shashkin, and Yury Kissin. "Titanium Complex Containing a Saligenin Ligand - New Universal Post-Metallocene Polymerization Catalyst: Copolymerization of Ethylene with Higher α-Olefins." Journal of Research Updates in Polymer Science 3, no. 4 (January 5, 2015): 216–26. http://dx.doi.org/10.6000/1929-5995.2014.03.04.3.

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34

McCain, W. C., J. Wilcke, J. C. Lee, and M. Ehrich. "Effect of cyclic phenyl saligenin phosphate and paraoxon treatment on vascular response to adrenergic and cholinergic agents in hens." Journal of Toxicology and Environmental Health 44, no. 2 (February 1995): 167–87. http://dx.doi.org/10.1080/15287399509531953.

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35

Harp, Paul, Duke Tanaka, and Carey N. Pope. "Potentiation of Organophosphorus-Induced Delayed Neurotoxicity Following Phenyl Saligenin Phosphate Exposures in 2-, 5-, and 8-Week-Old Chickens." Toxicological Sciences 37, no. 1 (1997): 64–70. http://dx.doi.org/10.1093/toxsci/37.1.64.

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36

Harris, W., D. Muñoz, P. L. R. Bonner, and A. J. Hargreaves. "Effects of phenyl saligenin phosphate on cell viability and transglutaminase activity in N2a neuroblastoma and HepG2 hepatoma cell lines." Toxicology in Vitro 23, no. 8 (December 2009): 1559–63. http://dx.doi.org/10.1016/j.tiv.2009.08.029.

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37

Liyasova, Mariya S., Lawrence M. Schopfer, and Oksana Lockridge. "Cresyl Saligenin Phosphate, an Organophosphorus Toxicant, Makes Covalent Adducts with Histidine, Lysine, and Tyrosine Residues of Human Serum Albumin." Chemical Research in Toxicology 25, no. 8 (July 26, 2012): 1752–61. http://dx.doi.org/10.1021/tx300215g.

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38

Harp, P. "Potentiation of Organophosphorus-Induced Delayed Neurotoxicity Following Phenyl Saligenin Phosphate Exposures in 2-, 5-, and 8-Week-Old Chickens." Fundamental and Applied Toxicology 37, no. 1 (May 1997): 64–70. http://dx.doi.org/10.1006/faat.1997.2301.

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39

Mccain, W. C., J. C. Lee, J. R. Wilcke, and M. Ehrich. "The Effect of Phenyl Saligenin Cyclic Phosphate Induced Delayed Neuropathy on Selected Hemodynamic and Hematologic Parameters in the Hen." Pesticide Biochemistry and Physiology 45, no. 3 (March 1993): 220–27. http://dx.doi.org/10.1006/pest.1993.1024.

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40

Hausherr, Vanessa, Nicole Schöbel, Julia Liebing, and Christoph van Thriel. "Assessment of neurotoxic effects of tri-cresyl phosphates (TCPs) and cresyl saligenin phosphate (CBDP) using a combination of in vitro techniques." NeuroToxicology 59 (March 2017): 210–21. http://dx.doi.org/10.1016/j.neuro.2016.06.005.

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41

Liyasova, Mariya S., Lawrence M. Schopfer, and Oksana Lockridge. "Cresyl saligenin phosphate makes multiple adducts on free histidine, but does not form an adduct on histidine 438 of human butyrylcholinesterase." Chemico-Biological Interactions 203, no. 1 (March 2013): 103–7. http://dx.doi.org/10.1016/j.cbi.2012.07.006.

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42

Fox, Jonathan H., Bernard S. Jortner, David Barber, and Marion F. Ehrich. "Altered expression of transcripts for ?-tubulin and an unidentified gene in the spinal cord of phenyl saligenin phosphate treated hens (Gallus gallus)." Journal of Biochemical and Molecular Toxicology 17, no. 5 (2003): 263–71. http://dx.doi.org/10.1002/jbt.10088.

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43

Masson, Patrick, Sofya Lushchekina, Lawrence M. Schopfer, and Oksana Lockridge. "Effects of viscosity and osmotic stress on the reaction of human butyrylcholinesterase with cresyl saligenin phosphate, a toxicant related to aerotoxic syndrome: kinetic and molecular dynamics studies." Biochemical Journal 454, no. 3 (August 29, 2013): 387–99. http://dx.doi.org/10.1042/bj20130389.

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CSP (cresyl saligenin phosphate) is an irreversible inhibitor of human BChE (butyrylcholinesterase) that has been involved in the aerotoxic syndrome. Inhibition under pseudo-first-order conditions is biphasic, reflecting a slow equilibrium between two enzyme states E and E′. The elementary constants for CSP inhibition of wild-type BChE and D70G mutant were determined by studying the dependence of inhibition kinetics on viscosity and osmotic pressure. Glycerol and sucrose were used as viscosogens. Phosphorylation by CSP is sensitive to viscosity and is thus strongly diffusion-controlled (kon≈108 M−1·min−1). Bimolecular rate constants (ki) are about equal to kon values, making CSP one of the fastest inhibitors of BChE. Sucrose caused osmotic stress because it is excluded from the active-site gorge. This depleted the active-site gorge of water. Osmotic activation volumes, determined from the dependence of ki on osmotic pressure, showed that water in the gorge of the D70G mutant is more easily depleted than that in wild-type BChE. This demonstrates the importance of the peripheral site residue Asp70 in controlling the active-site gorge hydration. MD simulations provided new evidence for differences in the motion of water within the gorge of wild-type and D70G enzymes. The effect of viscosogens/osmolytes provided information on the slow equilibrium E⇌E′, indicating that alteration in hydration of a key catalytic residue shifts the equilibrium towards E′. MD simulations showed that glycerol molecules that substitute for water molecules in the enzyme active-site gorge induce a conformational change in the catalytic triad residue His438, leading to the less reactive form E′.

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44

Almami, Ibtesam S., Maha A. Aldubayan, Shatha G. Felemban, Najiah Alyamani, Richard Howden, Alexander J. Robinson, Tom D. Z. Pearson, et al. "Neurite outgrowth inhibitory levels of organophosphates induce tissue transglutaminase activity in differentiating N2a cells: evidence for covalent adduct formation." Archives of Toxicology 94, no. 11 (August 4, 2020): 3861–75. http://dx.doi.org/10.1007/s00204-020-02852-w.

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Abstract Organophosphate compounds (OPs) induce both acute and delayed neurotoxic effects, the latter of which is believed to involve their interaction with proteins other than acetylcholinesterase. However, few OP-binding proteins have been identified that may have a direct role in OP-induced delayed neurotoxicity. Given their ability to disrupt Ca2+ homeostasis, a key aim of the current work was to investigate the effects of sub-lethal neurite outgrowth inhibitory levels of OPs on the Ca2+-dependent enzyme tissue transglutaminase (TG2). At 1–10 µM, the OPs phenyl saligenin phosphate (PSP) and chlorpyrifos oxon (CPO) had no effect cell viability but induced concentration-dependent decreases in neurite outgrowth in differentiating N2a neuroblastoma cells. The activity of TG2 increased in cell lysates of differentiating cells exposed for 24 h to PSP and chlorpyrifos oxon CPO (10 µM), as determined by biotin-cadaverine incorporation assays. Exposure to both OPs (3 and/or 10 µM) also enhanced in situ incorporation of the membrane permeable substrate biotin-X-cadaverine, as indicated by Western blot analysis of treated cell lysates probed with ExtrAvidin peroxidase and fluorescence microscopy of cell monolayers incubated with FITC-streptavidin. Both OPs (10 µM) stimulated the activity of human and mouse recombinant TG2 and covalent labelling of TG2 with dansylamine-labelled PSP was demonstrated by fluorescence imaging following SDS-PAGE. A number of TG2 substrates were tentatively identified by mass spectrometry, including cytoskeletal proteins, chaperones and proteins involved protein synthesis and gene regulation. We propose that the elevated TG2 activity observed is due to the formation of a novel covalent adduct between TG2 and OPs.

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45

Carlson, Kent, and Marion Ehrich. "Organophosphorus Compound–Induced Delayed Neurotoxicity in White Leghorn Hens Assessed by Fluoro-Jade." International Journal of Toxicology 23, no. 4 (July 2004): 259–66. http://dx.doi.org/10.1080/10915810490504968.

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Certain organophosphorus (OP) compounds can induce a delayed neuropathy, termed OPIDN, that involves central and peripheral nervous system axons, terminals, and perikarya. Historically, OPIDN has been characterized by staining neural sections with silver or hematoxylin and eosin (H&E). This study utilized a novel staining method, Fluoro-Jade, for evaluating the distribution and extent of OPIDN in the central nervous system of hens. Results were then compared to synoptically sectioned and stained H&E preparations. White Leghorn hens were injected with phenyl saligenin phosphate (PSP, 2.5 mg/kg, intramuscular [im]), triphenyl phosphite (TPPi, 500 mg/kg, subcutaneous [sc]), or dimethyl sulfoxide vehicle (DMSO, 0.5 ml/kg, im or sc) and evaluated clinically for signs of neurological dysfunction associated with OPIDN. Hens were sacrificed 7, 14, and 21 days post dosing. Brains and spinal cords were removed immediately following sacrifice, fixed in formalin, and embedded in paraffin. Microtomecut sections (7 μm) were then stained with Fluoro-Jade (0.001%, w/ v) or H&E. Staining with Fluoro-Jade revealed time-dependent degeneration of nerve fibers and terminals (with PSP and TPPi), or cell bodies (with TPPi) in lamina VII, spinocerebellar, and medial pontine-spinal tracts of the lumbar spinal cord, in white matter and mossy fibers of foliae I–V and IX of the cerebellum, and in medullary, pontine, and midbrain nuclei and paleostriatal fibers surrounding the optic tract. TPPi-induced degeneration was more extensive than that induced by PSP and affected additional cerebellar folia, medullary, pontine, midbrain, and forebrain nuclei and fiber tracts. H&E-stained sections revealed fewer sites of neurodegeneration when compared to Fluoro-Jade. These results demonstrate that Fluoro-Jade is a sensitive method for staining neural tissue affected by OPIDN.

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Felemban, Shatha G., Falguni S. Vyas, Lyndsey Durose, Alan J. Hargreaves, and John M. Dickenson. "Phenyl Saligenin Phosphate Disrupts Cell Morphology and the Actin Cytoskeleton in Differentiating H9c2 Cardiomyoblasts and Human-Induced Pluripotent Stem-Cell-Derived Cardiomyocyte Progenitor Cells." Chemical Research in Toxicology 33, no. 9 (August 6, 2020): 2310–23. http://dx.doi.org/10.1021/acs.chemrestox.0c00100.

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McCain, Wilfred C., Diane M. Flaherty, Linda Correll, Bernard Jortner, and Marion Ehrich. "CATECHOLAMINE CONCENTRATIONS AND CONTRACTILE RESPONSES OF ISOLATED VESSELS FROM HENS TREATED WITH CYCLIC PHENYL SALIGENIN PHOSPHATE OR PARAOXON IN THE PRESENCE OR ABSENCE OF VERAPAMIL." Journal of Toxicology and Environmental Health 48, no. 4 (July 1996): 397–411. http://dx.doi.org/10.1080/009841096161276.

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Kart, Asim, and Ali Bilgili. "Effects of organophosphate phenyl saligenin phosphate and polyether carboxylic ionophore lasalocid on motor nerve conduction velocity, neuropathy target esterase enzyme activity, and clinical ataxia in chickens." Toxicology Mechanisms and Methods 19, no. 5 (June 2009): 351–55. http://dx.doi.org/10.1080/15376510903030403.

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Carletti, Eugénie, Lawrence M. Schopfer, Jacques-Philippe Colletier, Marie-Thérèse Froment, Florian Nachon, Martin Weik, Oksana Lockridge, and Patrick Masson. "Reaction of Cresyl Saligenin Phosphate, the Organophosphorus Agent Implicated in Aerotoxic Syndrome, with Human Cholinesterases: Mechanistic Studies Employing Kinetics, Mass Spectrometry, and X-ray Structure Analysis." Chemical Research in Toxicology 24, no. 6 (June 20, 2011): 797–808. http://dx.doi.org/10.1021/tx100447k.

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Duysen, Ellen G., John R. Cashman, Lawrence M. Schopfer, Florian Nachon, Patrick Masson, and Oksana Lockridge. "Differential sensitivity of plasma carboxylesterase-null mice to parathion, chlorpyrifos and chlorpyrifos oxon, but not to diazinon, dichlorvos, diisopropylfluorophosphate, cresyl saligenin phosphate, cyclosarin thiocholine, tabun thiocholine, and carbofuran." Chemico-Biological Interactions 195, no. 3 (February 2012): 189–98. http://dx.doi.org/10.1016/j.cbi.2011.12.006.

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