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Published: 7 September 2023

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1

Zhan, Minglang, Xiaolei Wei, Weimin Huang, Yongqiang Wei, and Ru Feng. "PKM2 Inhibition Enhances the Sensitivity of Doxorubicin in ABC Diffuse Large B-Cell Lymphoma Cells." Blood 138, Supplement 1 (November 5, 2021): 4336. http://dx.doi.org/10.1182/blood-2021-146371.

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Abstract Background: Pyruvate kinase muscle isoenzyme 2 (PKM2) is a key enzyme in aerobic glycolysis and thought to contribute to cancer cell metabolic reprogramming and regulating the reactive oxygen species (ROS). Doxorubicin has been showed to induced activated-B cell types diffuse large B-cell lymphoma (ABC-DLBCL) cells death by ROS accumulation. Our purpose was to evaluate whether PKM2 inhibition could enhance the sensitivity of doxorubicin in ABC-DLBCL. Methods: MTT assay was used to evaluate the proliferation of 2 ABC-DLBCL cell lines by treated with PKM2 inhibitor, PKM2 shRNA and doxorubicin. Apoptosis were detected by FCM after staining with Annexin V/SYTOX Green. Western Blot was used to evaluated the expression of PARP, Mcl1, Bcl2, Bax, Bim, p38 and JNK in ABC-DLBCL cells treated with PKM2 inhibition, PKM2 shRNA and doxorubicin. Results: PKM2 expression was found in both U2932 and SuDHL2 cell lines. Both PKM2 inhibitor and doxorubicin could inhibit the proliferation and induce apoptosis in ABC-DLBCL cell lines. PKM2 inhibitor could enhance the doxorubicin-induced apoptosis. ShRNA was used to knock down the PKM2 expression in ABC-DLBCL cell lines and PKM2 KD cell lines were more sensitive to doxorubicin. PKM2 inhibition could increase the expression of cleaved PARP, Bax, Bim, p38 and JNK as well as decrease Mcl1 and Bcl2 expression Conclusions: PKM2 inhibition could sensitize ABC-DLBCL cell lines to the cytotoxic effects of doxorubicin. Key words: PKM2, Doxorubicin, Diffuse large B cell lymphoma Disclosures No relevant conflicts of interest to declare.

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Luker, Kathryn E., and Gary D. Luker. "The CXCL12/CXCR4/ACKR3 Signaling Axis Regulates PKM2 and Glycolysis." Cells 11, no. 11 (May 28, 2022): 1775. http://dx.doi.org/10.3390/cells11111775.

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In response to CXCL12, CXCR4 and ACKR3 both recruit β-arrestin 2, regulating the assembly of interacting proteins that drive signaling and contribute to the functions of both receptors in cancer and multiple other diseases. A prior proteomics study revealed that β-arrestin 2 scaffolds pyruvate kinase M2 (PKM2), an enzyme implicated in shifting cells to glycolytic metabolism and poor prognosis in cancer. We hypothesized that CXCL12 signaling regulates PKM2 protein interactions, oligomerization, and glucose metabolism. We used luciferase complementation in cell-based assays and a tumor xenograft model of breast cancer in NSG mice to quantify how CXCR4 and ACKR3 change protein interactions in the β-arrestin-ERK-PKM2 pathway. We also used mass spectrometry to analyze the effects of CXCL12 on glucose metabolism. CXCL12 signaling through CXCR4 and ACKR3 stimulated protein interactions among β-arrestin 2, PKM2, ERK2, and each receptor, leading to the dissociation of PKM2 from β-arrestin 2. The activation of both receptors reduced the oligomerization of PKM2, reflecting a shift from tetramers to dimers or monomers with low enzymatic activity. Mass spectrometry with isotopically labeled glucose showed that CXCL12 signaling increased intermediate metabolites in glycolysis and the pentose phosphate pathway, with ACKR3 mediating greater effects. These data establish how CXCL12 signaling regulates PKM2 and reprograms cellular metabolism.

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Darwish, Ibrahim, Samy Emara, Hassan Askal, Nawal El-Rabbat, Toshifumi Akizawa, and Masanori Yoshiokab. "Enzyme-linked immunosorbent assay for 2-deoxycytidine." Analytica Chimica Acta 404, no. 2 (January 2000): 179–86. http://dx.doi.org/10.1016/s0003-2670(99)00701-1.

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4

Gonzalez, Isabel, Rosario Martin, Teresa Garcia, Paloma Morales, Bernabe Sanz, and Pablo Hernandez. "Antibody Sandwich Enzyme-Linked lmmunosorbent Assay." Journal of Dairy Science 77, no. 12 (December 1994): 3552–57. http://dx.doi.org/10.3168/jds.s0022-0302(94)77298-2.

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5

Volland, Hervé, Brigitte Vulliez Le Normand, Suzanne Mamas, Jacques Grassi, Christophe Créminon, Eric Ezan, and Philippe Pradelles. "Enzyme immunometric assay for leukotriene C4." Journal of Immunological Methods 175, no. 1 (September 1994): 97–105. http://dx.doi.org/10.1016/0022-1759(94)90335-2.

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6

Matsumoto, Akiko, Toshihiro Ino, Mitsuhiro Ohta, Tetsuya Otani, Sachiko Hanada, Atsushi Sakuraoka, Akane Matsumoto, Masayoshi Ichiba, and Megumi Hara. "Enzyme-linked immunosorbent assay of nicotine metabolites." Environmental Health and Preventive Medicine 15, no. 4 (January 8, 2010): 211–16. http://dx.doi.org/10.1007/s12199-009-0129-2.

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7

Klein, Gérard, and Jean-Louis Reymond. "An Enzyme Assay Using pM." Angewandte Chemie 113, no. 9 (May 4, 2001): 1821–23. http://dx.doi.org/10.1002/1521-3757(20010504)113:9<1821::aid-ange18210>3.0.co;2-p.

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8

Klein, Gérard, and Jean-Louis Reymond. "An Enzyme Assay Using pM." Angewandte Chemie International Edition 40, no. 9 (May 4, 2001): 1771–73. http://dx.doi.org/10.1002/1521-3773(20010504)40:9<1771::aid-anie17710>3.0.co;2-m.

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9

Osawa, Hisao, Olivera Josimovic-Alasevic, and Tibor Diamantstein. "Enzyme-linked immunosorbent assay of mouse interleukin-2 receptors." Journal of Immunological Methods 92, no. 1 (August 1986): 109–15. http://dx.doi.org/10.1016/0022-1759(86)90510-7.

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10

TAKAISHI, Masatoshi, Mitoshi AKIYAMA, Tomonori HAYASHI, Yuko HIRAI, Yoshie MURAKAMI, Ryuzo UEDA, Kaori TATSUGAWA, Michio YAMAKIDO, and Tokuo TSUBOKURA. "ASSAY FOR THE SOLUBLE INTERLEUKIN-2 RECEPTOR BY SANDWICH ENZYME LINKED IMMUNOSORBENT ASSAY." Japanese Journal of Medical Science and Biology 43, no. 5 (1990): 151–61. http://dx.doi.org/10.7883/yoken1952.43.151.

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11

Sansom, P. A., C. T. Marlow, M. Lapsley, and F. V. Flynn. "A Sandwich Enzyme-Linked Immunosorbent Assay for 2-Glycoprotein I." Annals of Clinical Biochemistry: An international journal of biochemistry and laboratory medicine 28, no. 3 (March 1, 1991): 283–89. http://dx.doi.org/10.1177/000456329102800315.

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12

Elased, Khalid M., Tatiana S. Cunha, Susan B. Gurley, Thomas M. Coffman, and Mariana Morris. "New Mass Spectrometric Assay for Angiotensin-Converting Enzyme 2 Activity." Hypertension 47, no. 5 (May 2006): 1010–17. http://dx.doi.org/10.1161/01.hyp.0000215588.38536.30.

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13

Marcus, G. J., and R. Durnford. "A simple enzyme-linked immunosorbent assay for testosterone." Steroids 46, no. 6 (December 1985): 975–86. http://dx.doi.org/10.1016/s0039-128x(85)80005-2.

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14

Butterfield, Phillip W., Alex M. Bargmeyer, Anne K. Camper, and Joel A. Biederman. "Modified enzyme activity assay to determine biofilm biomass." Journal of Microbiological Methods 50, no. 1 (June 2002): 23–31. http://dx.doi.org/10.1016/s0167-7012(02)00005-2.

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15

Zhang, Bao-Zhen, Xiao-Tong Guo, Jian-Wei Chen, Yuan Zhao, Xia Cong, Zhong-Ling Jiang, Rong-Feng Cao, Kai Cui, Shan-Song Gao, and Wen-Ru Tian. "Saikosaponin-D Attenuates Heat Stress-Induced Oxidative Damage in LLC-PK1 Cells by Increasing the Expression of Anti-Oxidant Enzymes and HSP72." American Journal of Chinese Medicine 42, no. 05 (January 2014): 1261–77. http://dx.doi.org/10.1142/s0192415x14500797.

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Heat stress stimulates the production of reactive oxygen species (ROS), which cause oxidative damage in the kidney. This study clarifies the mechanism by which saikosaponin-d (SSd), which is extracted from the roots of Bupleurum falcatum L, protects heat-stressed pig kidney proximal tubular (LLC-PK1) cells against oxidative damage. SSd alone is not cytotoxic at concentrations of 1 or 3 μg/mL as demonstrated by a 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay. To assess the effects of SSd on heat stress-induced cellular damage, LLC-PK1 cells were pretreated with various concentrations of SSd, heat stressed at 42°C for 1 h, and then returned to 37°C for 9 h. DNA ladder and MTT assays demonstrated that SSd helped to prevent heat stress-induced cellular damage when compared to untreated cells. Additionally, pretreatment with SSd increased the activity of superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GPx) but decreased the concentration of malondialdehyde (MDA) in a dose-dependent manner when compared to controls. Furthermore, real-time PCR and Western blot analysis demonstrated that SSd significantly increased the expression of copper and zinc superoxide dismutase (SOD-1), CAT, GPx-1 and heat shock protein 72 (HSP72) at both the mRNA and protein levels. In conclusion, these results are the first to demonstrate that SSd ameliorates heat stress-induced oxidative damage by modulating the activity of anti-oxidant enzymes and HSP72 in LLC-PK1 cells.

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16

Dipti, Tanjeem Rabika, Mohammad Shaiful Azam, Mohammad Humayun Sattar, and Shahana Rahman. "Detection of Antinuclear Antibody in Childhood Rheumatic Diseases by Immunofluorescence Assay and Enzyme Immuno Assay." Bangladesh Journal of Child Health 35, no. 2 (April 15, 2012): 49–52. http://dx.doi.org/10.3329/bjch.v35i2.10355.

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Background: Anti-nuclear antibodies (ANAs) are specific antibodies directed against a variety of nuclear antigens. Indirect immunofluorecence (ANA-IFA) and Enzyme Immunoassay (ANA-EIA) are commonly used methods for ANA detection. The positivity of ANA-IFA using HEp-2 cell substrate is 90-100% in systemic rheumatic diseases. On the other hand positivity of ANA-EIA is found to be much lower in different studies. In Bangladesh most of the laboratories use ANA-EIA method.Objectives: To detect ANA by Immunofluorecence Assay (using HEp-2 cell substrate) and Enzyme Immuno Assay in childhood rheumatic diseases and to compare ANA positivity by these two methods.Materials and methods: Cross sectional comparative study. Total 40 patients of different childhood rheumatic diseases were enrolled in this study. Serum sample was collected and tested for detection of ANA by Immunofluorecence Assay using HEp-2 cell substrate and Enzyme Immuno Assay.Result: Among total 40 cases, 67.5% were ANA positive by IFA method and 27.5% were ANA positive by EIA method.Conclusion: ANA-IFA is superior to ANA-EIA for detection of ANA in childhood rheumatic diseases.DOI: http://dx.doi.org/10.3329/bjch.v35i2.10355Bangladesh J Child Health 2011; Vol 35 (2): 49-52

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17

Muruzabal, Damian, Sabine A. S. Langie, Bertrand Pourrut, and Amaya Azqueta. "The enzyme-modified comet assay: Enzyme incubation step in 2 vs 12-gels/slide systems." Mutation Research/Genetic Toxicology and Environmental Mutagenesis 845 (September 2019): 402981. http://dx.doi.org/10.1016/j.mrgentox.2018.11.005.

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18

Codd, A. A., M. S. Sprott, H. K. Narang, P. B. Crone, and R. H. Turner. "Competitive enzyme-linked immunosorbent assay for Treponema pallidum antibodies." Journal of Medical Microbiology 26, no. 2 (June 1, 1988): 153–57. http://dx.doi.org/10.1099/00222615-26-2-153.

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19

Kadima, Tenshuk A., and Michael A. Pickard. "A colorimetric assay for immobilized chloroperoxidase." Canadian Journal of Microbiology 36, no. 4 (April 1, 1990): 302–4. http://dx.doi.org/10.1139/m90-053.

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A rapid and sensitive colorimetric assay was developed for the estimation of chloroperoxidase activity. N,N,N′,N′-Tetramethyl-p-phenylenediamine was chosen from four potential chromogenic substrates because the blue product resulting from chloroperoxidase conversion gave the highest molar absorption. This product exhibited two absorbance maxima, at 563 and 610 nm. Activity was monitored at 563 nm, and the product absorbance was stable for at least 1 h at 10 °C after treatment with an equal volume of a mixture (40:1) of methanol and phosphoric acid (85% w/v), pH 2. The linear range of the assay with respect to enzyme amount was determined. The assay was developed using soluble chloroperoxidase but worked well with the enzyme immobilized on glass beads. Key words: immobilized enzyme, chloroperoxidase, enzyme assay.

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20

LEERDAM, M., F. HUDIG, W. ROOIJEN, E. SLAATS, A. GERAEDTS, and G. TYTGAT. "11-dehydro-thromboxane B2 enzyme immuno assay, a suitable screening assay for aspirin use?" Gastroenterology 120, no. 5 (April 2001): A596. http://dx.doi.org/10.1016/s0016-5085(01)82963-2.

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21

Watanabe, Hiroo, Atsuko Satake, Yasumasa Kido, and Akio Tsuji. "Monoclonal-based enzyme-linked immunosorbent assay and immunochromatographic rapid assay for dihydrostreptomycin in milk." Analytica Chimica Acta 472, no. 1-2 (November 2002): 45–53. http://dx.doi.org/10.1016/s0003-2670(02)00983-2.

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22

Wang, Ding, Tim Wood, Martin Sadilek, C. Ronald Scott, Frantisek Turecek, and Michael H. Gelb. "Tandem Mass Spectrometry for the Direct Assay of Enzymes in Dried Blood Spots: Application to Newborn Screening for Mucopolysaccharidosis II (Hunter Disease)." Clinical Chemistry 53, no. 1 (January 1, 2007): 137–40. http://dx.doi.org/10.1373/clinchem.2006.077263.

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Abstract Background: A treatment for mucopolysaccharidosis II (Hunter syndrome) has recently become available. Therefore, we developed a high-throughput assay method appropriate for newborn screening for the relevant enzyme, iduronate 2-sulfatase. Methods: We synthesized a new iduronate 2-sulfatase substrate that can be used to assay the enzyme by use of tandem mass spectrometry together with an internal standard. The assay uses a dried blood spot on a newborn screening card as the enzyme source. Results: When the assay was tested on dried blood spots, the iduronate 2-sulfatase activity measured for 13 patients with Hunter syndrome was well below the interval found for 57 randomly chosen newborns. The assay was more sensitive than previously reported iduronate 2-sulfatase assays. Conclusions: This newly developed tandem mass spectrometry assay has the potential to be adopted for newborn screening of Hunter syndrome. This method also has the potential to be carried out in multiplex fashion to assay several different enzymes relevant to lysosomal storage diseases that are assayed in a single infusion into the mass spectrometer.

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23

Plested, Joyce S., Mingzhu Zhu, Shane Cloney-Clark, Edmond Massuda, Urvashi Patel, Andrew Klindworth, Michael J. Massare, et al. "Severe Acute Respiratory Syndrome Coronavirus 2 Receptor (Human Angiotensin-Converting Enzyme 2) Binding Inhibition Assay: A Rapid, High-Throughput Assay Useful for Vaccine Immunogenicity Evaluation." Microorganisms 11, no. 2 (February 1, 2023): 368. http://dx.doi.org/10.3390/microorganisms11020368.

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Emerging variants of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) show immune evasion of vaccine-derived immunity, highlighting the need for better clinical immunogenicity biomarkers. To address this need, an enzyme-linked immunosorbent assay-based, human angiotensin-converting enzyme 2 (hACE2) binding inhibition assay was developed to measure antibodies against the ancestral strain of SARS-CoV-2 and was validated for precision, specificity, linearity, and other parameters. This assay measures the inhibition of SARS-CoV-2 spike (S) protein binding to the receptor, hACE2, by serum from vaccine clinical trials. Inter- and intra-assay precision, specificity, linearity, lower limit of quantitation, and assay robustness parameters successfully met the acceptance criteria. Heme and lipid matrix effects showed minimal interference on the assay. Samples were stable for testing in the assay even with 8 freeze/thaws and up to 24 months in −80 °C storage. The assay was also adapted for variants (Delta and Omicron BA.1/BA.5), with similar validation results. The hACE2 assay showed significant correlation with anti-recombinant S immunoglobulin G levels and neutralizing antibody titers. This assay provides a rapid, high-throughput option to evaluate vaccine immunogenicity. Along with other clinical biomarkers, it can provide valuable insights into immune evasion and correlates of protection and enable vaccine development against emerging COVID-19 variants.

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24

Varela, Yolanda, Enrique Ortega, and Beatriz Gómez. "Quantitation of rubella virus by competitive enzyme immunosorbent assay." Journal of Virological Methods 19, no. 1 (January 1988): 79–87. http://dx.doi.org/10.1016/0166-0934(88)90009-2.

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25

Wong, Yu-Wah, and David W. Kinniburgh. "Evaluation of a kinetic assay for angiotensin converting enzyme." Clinical Biochemistry 20, no. 5 (October 1987): 323–27. http://dx.doi.org/10.1016/s0009-9120(87)80080-2.

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26

Danilov, Dmitry V., Olga A. Shmeleva, Alexander S. Lunin, Liubov I. Kozlovskaya, Anastasia N. Piniaeva, and Anna A. Shishova. "Development of a biosafe ELISA-based platform for assessing immunogenicity in the production of an inactivated whole-virion coronavirus vaccine." Medical academic journal 2, no. 2 (November 6, 2022): 163–69. http://dx.doi.org/10.17816/maj108717.

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BACKGROUND: SARS-CoV-2 vaccine immunogenicity is evaluated in neutralization test with live virus. It is performed in a biosafety level 3 zone because requires live virus stage. Therefore, control laboratories should be certified for this class of work. The development of technology based on enzyme-linked immunosorbent assay as an analogue of the neutralization reaction makes it possible to create an immunobiological product in a shorter time and in conditions without special requirements for control laboratories. AIM: Development of an enzyme-linked immunosorbent assay for assessing SARS-CoV-2 vaccine immunogenicity by measuring neutralizing antibodies production in immunized animals. MATERIALS AND METHODS: Recombinant receptor-binding domain fused to a С-terminal hexahistidine sequence was produced in Escherichia coli cells and purified via metal-affinity chromatography on WorkBeads NiMAC (Bio-Works). Purified protein was used in enzyme-linked immunosorbent assay as an antigen for sorption. The sera of mice immunized with the vaccine preparation were tested for neutralizing activity against the SARS-CoV-2, as well as in the developed enzyme-linked immunosorbent assay. RESULTS: Sera with high neutralizing titers showed a high degree of binding to recombinant receptor-binding domain fused to a С-terminal hexahistidine sequence in enzyme-linked immunosorbent assay, while sera from non-immunized animals or sera with neutralization titers less than 1:8 were not reactive in enzyme-linked immunosorbent assay. The Spearman and Pearson correlation coefficients for neutralization test titers and optical density in enzyme-linked immunosorbent assay were 0.759 and 0.76, respectively. The developed assay can be used as a semi-quantitative method for assessing the immunogenicity of a vaccine against coronavirus infection. CONCLUSIONS: The developed platform makes it possible to reliably assess the immunogenicity of an inactivated coronavirus vaccine under conditions that do not require a high biosafety conditions.

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27

NAGAYAMA, S., S. SATO, O. KAWAMURA, K. OHTANI, and Y. UENO. "Detection of T-2 toxin with an enzyme-linked immunosorbent assay." Mycotoxins 1987, no. 25 (1987): 40–42. http://dx.doi.org/10.2520/myco1975.1987.40.

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28

Conzelmann, Carina, Andrea Gilg, Rüdiger Groß, Desiree Schütz, Nico Preising, Ludger Ständker, Bernd Jahrsdörfer, et al. "An enzyme-based immunodetection assay to quantify SARS-CoV-2 infection." Antiviral Research 181 (September 2020): 104882. http://dx.doi.org/10.1016/j.antiviral.2020.104882.

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29

Hassel, Bret A., and Paul O. P. Ts'o. "A sensitive assay for the IFN-regulated 2–5A synthetase enzyme." Journal of Virological Methods 50, no. 1-3 (December 1994): 323–34. http://dx.doi.org/10.1016/0166-0934(94)90187-2.

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30

Lee, Rachel C., Ru-Dong Wei, and Fun S. Chu. "Enzyme-Linked Immunosorbent Assay for T-2 Toxin Metabolites in Urine." Journal of AOAC INTERNATIONAL 72, no. 2 (March 1, 1989): 345–48. http://dx.doi.org/10.1093/jaoac/72.2.345.

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Abstract A direct competitive enzyme-linked immunosorbent assay (ELISA) for determination of total T-2 toxin metabolites in urine was developed. The assay involves coating anti-3-acetyl-neosolaniol-hemisuccinate- bovine serum albumin conjugate (anti-3-Ac-NEOS-HS-BSA) antibody to the ELISA plate and using 3-Ac-NEOS-HS-peroxidase as the enzyme marker. Competitive ELISA revealed that the antibody had good cross-reactivity with acetyldiacetoxyscirpenol (Ac-DAS), T-2 tetraol tetraacetate, 3'-OH-Ac-T-2, 3-Ac-NEOS, and 3,4,15- triacetyl-12,13-epoxytrichothec-9-en-8-one (Ac-T-2-8-one), but less cross-reactivity with Ac-T-2 toxin and T-2 toxin. All metabolites of T-2 toxin in urine were converted to T-2 tetraol tetraacetate (T-2- 4ol-4Ac) by acetylation of the sample extract before ELISA. To test the ELISA accuracy, a radioimmunoassay (RIA) was performed simultaneously. The linear portion of the standard curve of this direct ELISA for T-2-4ol-4Ac was 0.2-2.0 ng/mL, which was 10 times more sensitive than RIA. The minimum detection level for T-2-4ol- 4Ac was 0.02 ng/mL (0.4 pg/assay) in the absence of urine sample. The overall analytical recoveries for T-2 toxin, HT-2, T-2-4ol, 3'- OH-HT-2, NEOS, and a mixture of these 5 toxins added to the urine samples in the ELISA at concentrations of 0.05 and 0.2 ng/mL were 87 and 94%, respectively.

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31

Onyeogaziri, Favour Chinyere, and Christos Papaneophytou. "A General Guide for the Optimization of Enzyme Assay Conditions Using the Design of Experiments Approach." SLAS DISCOVERY: Advancing the Science of Drug Discovery 24, no. 5 (February 25, 2019): 587–96. http://dx.doi.org/10.1177/2472555219830084.

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Many factors must be considered during the optimization of an enzyme assay. These include the choice of buffer and its composition, the type of enzyme and its concentration, as well as the type of substrate and concentrations, the reaction conditions, and the appropriate assay technology. The process of an enzyme assay optimization, in our experience, can take more than 12 weeks using the traditional one-factor-at-a-time approach. In contrast, the design of experiments (DoE) approaches have the potential to speed up the assay optimization process and provide a more detailed evaluation of tested variables. However, not all researchers are aware of DoE approaches or believe that it is easy to employ a DoE approach for the optimization of an assay. In order to facilitate enzyme assay developers to use DoE methodologies, we present in detail the steps required to identify in less than 3 days (1) the factors that significantly affect the activity of an enzyme and (2) the optimal assay conditions using a fractional factorial approach and response surface methodology. This is exemplified with the optimization of assay conditions for the human rhinovirus-3C protease, and the methodology used could be employed as a basic guide for the speedy identification of the optimum assay conditions for any enzyme.

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32

Ghosh, Arun K., Dana Shahabi, Monika Yadav, Satish Kovela, Brandon J. Anson, Emma K. Lendy, Connie Bonham, et al. "Chloropyridinyl Esters of Nonsteroidal Anti-Inflammatory Agents and Related Derivatives as Potent SARS-CoV-2 3CL Protease Inhibitors." Molecules 26, no. 19 (September 24, 2021): 5782. http://dx.doi.org/10.3390/molecules26195782.

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We report the design and synthesis of a series of new 5-chloropyridinyl esters of salicylic acid, ibuprofen, indomethacin, and related aromatic carboxylic acids for evaluation against SARS-CoV-2 3CL protease enzyme. These ester derivatives were synthesized using EDC in the presence of DMAP to provide various esters in good to excellent yields. Compounds are stable and purified by silica gel chromatography and characterized using 1H-NMR, 13C-NMR, and mass spectral analysis. These synthetic derivatives were evaluated in our in vitro SARS-CoV-2 3CLpro inhibition assay using authentic SARS-CoV-2 3CLpro enzyme. Compounds were also evaluated in our in vitro antiviral assay using quantitative VeroE6 cell-based assay with RNAqPCR. A number of compounds exhibited potent SARS-CoV-2 3CLpro inhibitory activity and antiviral activity. Compound 9a was the most potent inhibitor, with an enzyme IC50 value of 160 nM. Compound 13b exhibited an enzyme IC50 value of 4.9 µM. However, it exhibited a potent antiviral EC50 value of 24 µM in VeroE6 cells. Remdesivir, an RdRp inhibitor, exhibited an antiviral EC50 value of 2.4 µM in the same assay. We assessed the mode of inhibition using mass spectral analysis which suggested the formation of a covalent bond with the enzyme. To obtain molecular insight, we have created a model of compound 9a bound to SARS-CoV-2 3CLpro in the active site.

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33

Jiang, Y., W. Weng, Y. Liang, S. Zhong, Y. Pan, and J. Gu. "POS0426 PKM2 PROMOTES PRO-INFLAMMATORY MACROPHAGE ACTIVATION IN ANKYLOSING SPONDYLITIS." Annals of the Rheumatic Diseases 82, Suppl 1 (May 30, 2023): 469.2–469. http://dx.doi.org/10.1136/annrheumdis-2023-eular.2926.

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BackgroundMacrophages are vital effector cells in ankylosing spondylitis (AS), leading to autoimmune tissue inflammation through varied effector functions [1]. The pro-inflammation potential of macrophages depends on their metabolic environment. Macrophages also work as principal regulators in T lymphocyte activation. To meet amplified bioenergetic and biosynthetic demands, metabolic pathways are joined to facilitate the proliferation and effector molecule production. A critical question is whether glycolysis and the rate-limiting enzyme, pyruvate kinase isoenzyme M2 (PKM2) could positively influence AS macrophages’ inflammatory function.ObjectivesThe objectives of the study was to investigate the effect of glycolysis and PKM2 on AS macrophage functions featured by the secretion of inflammatory cytokines and the presentations of co-stimulatory signals.MethodsPeripheral blood mononuclear cells (PBMC) were isolated from AS patients and differentiated into macrophages by M-CSF. Macrophages were further differentiated into M1 or M2 macrophages by stimulation with IFN-γ and LPS, or IL-4 and of IL-13. For glycolysis inhibition, cells were treated with 10mM of 2-Deoxy-D-glucose (2-DG). For inhibition ofPKM2, macrophages were treated with 0.25μM of Shikonin. The RNA expressions of proinflammatory cytokines and glycolysis-related genes were detected by qPCR. Immunoblotting, ELISA and confocal miroscopy was applied to examine the expression ofPKM2. Extracellular acidification rate (ECAR) analysis was performed to assess glycolysis. The expressions of surface molecule CD80, CD86, and HLA-DR were measured using CytoFLEX flow cytometer.ResultsAS macrophages are prone to produce excessive inflammation, includingTNFα,IL1β, andIL23,and are at overactive status by exhibiting stronger co-stimulatory signals, such as CD80, CD86, and HLA-DR. Meanwhile, we found that patient-derived M1 macrophages intensified glycolysis, captured as a higher ECAR. Obviously, upregulation ofPKM2andGLUT1has been observed on AS-derived monocytes and macrophages, especially on M1 macrophages, indicating a glucose metabolic alteration in AS macrophages. To investigate how glycolysis impacts macrophage inflammatory ability, 2-DG and Shikonin were applied to AS M1 macrophages, respectively. Consequently, both inhibitors could lessen pro-inflammatory function and reverse overactive status of AS macrophages, potentially favoring disease treatment.ConclusionWe emphasized hyper-metabolic M1 macrophages of AS and suggested an essential role for PKM2 in inflammatory effector functions of AS macrophages. Targeting PKM2 to inhibit glycolysis in an overactive macrophage may provide novel therapeutic methods for AS inflammation.Reference[1]Mauro D, Thomas R, Guggino G, Lories R, Brown MA, Ciccia F. Ankylosing spondylitis: an autoimmune or autoinflammatory disease? Nat Rev Rheumatol. 2021;17(7):387-404. doi:10.1038/s41584-021-00625-y.Figure 1.AS-derived M1 macrophage presents with more PKM2 and glycolysis.Circulating monocytes from HC and AS were differentiated into moncyte-derived macrophages. They were then activated into M1 type with LPS/IFN-γ for 24 h.A. Concentrations of PKM2 in HC and AS plasma measured by ELISA. N=6.B-C. Immunoblotting of PKM2 protein among HC and AS patients. N=16.D. Correlation between serum CRP andPKM2mRNA expression. N=17.E-F. Confocal images were acquired in ex vivo–generated macrophages stimulated with LPS/IFN-γ for 24 h and stained with anti-PKM2 (green). Nuclei were localized by DAPI (blue). The bar graph represents averaged data from experiments quantifying the fluorescent signal (n = 4 HC and 4 AS patients).G-K. Glycolysis assays in macrophages were evaluated with the Seahorse Bioscience XF96 analyzer by adding test agents in order of 1, oligomycin; 2, FCCP; 3, antimycin A/rotenone. Summarized graphs from 6 HC and 8 AS patients were shown.AcknowledgementsThis work was supported by the Scientific and Technological Planning Project of Guangzhou City [202102020150], Guangdong Provincial Basic and Applied Basic Research Fund Project [2021A1515111172], National Natural Science Foundation of China Youth Fund [82201998], Third Affiliated Hospital of Sun Yat-Sen University Cultivating Special Fund Project for the National Natural Science Foundation of China [2022GZRPYQN01] and National Natural Science Foundation of China [82271849].Disclosure of InterestsNone Declared.

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Ukita, Yoshiaki, Toshifumi Asano, Kuniyo Fujiwara, Katsuhiro Matsui, Masahiro Takeo, Seiji Negoro, and Yuichi Utsumi. "Enzyme-linked immunosorvent assay using vertical microreactor stack with microbeads." Microsystem Technologies 14, no. 9-11 (April 12, 2008): 1573–79. http://dx.doi.org/10.1007/s00542-008-0587-2.

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Goedken, Eric R., Andrew I. Gagnon, Gary T. Overmeyer, Junjian Liu, Richard A. Petrillo, Andrew F. Burchat, and Medha J. Tomlinson. "HTRF-Based Assay for Microsomal Prostaglandin E2 Synthase-1 Activity." Journal of Biomolecular Screening 13, no. 7 (July 1, 2008): 619–25. http://dx.doi.org/10.1177/1087057108321145.

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Microsomal prostaglandin E2 synthase-1 (mPGES-1) catalyzes the formation of prostaglandin E2 (PGE2) from the endoperoxide prostaglandin H 2 (PGH2). Expression of this enzyme is induced during the inflammatory response, and mouse knockout experiments suggest it may be an attractive target for antiarthritic therapies. Assaying the activity of this enzyme in vitro is challenging because of the unstable nature of the PGH 2 substrate. Here, the authors present an mPGES-1 activity assay suitable for characterization of enzyme preparations and for determining the potency of inhibitor compounds. This plate-based competition assay uses homogenous time-resolved fluorescence to measure PGE2 produced by the enzyme. The assay is insensitive to DMSO concentration up to 10% and does not require extensive washes after the initial enzyme reaction is concluded, making it a simple and convenient way to assess mPGES-1 inhibition. ( Journal of Biomolecular Screening 2008:619-625)

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Zhang, X. Kate, Carole S. Elbin, Wei-Lien Chuang, Samantha K. Cooper, Carla A. Marashio, Christa Beauregard, and Joan M. Keutzer. "Multiplex Enzyme Assay Screening of Dried Blood Spots for Lysosomal Storage Disorders by Using Tandem Mass Spectrometry." Clinical Chemistry 54, no. 10 (October 1, 2008): 1725–28. http://dx.doi.org/10.1373/clinchem.2008.104711.

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Abstract Background: Reports of the use of multiplex enzyme assay screening for Pompe disease, Fabry disease, Gaucher disease, Niemann-Pick disease types A and B, and Krabbe disease have engendered interest in the use of this assay in newborn screening. We modified the assay for high-throughput use in screening laboratories. Methods: We optimized enzyme reaction conditions and procedures for the assay, including the concentrations of substrate (S) and internal standard (IS), assay cocktail compositions, sample clean-up procedures, and mass spectrometer operation. The S and IS for each enzyme were premixed and bottled at an optimized molar ratio to simplify assay cocktail preparation. Using the new S:IS ratio, we validated the modified assay according to CLSI guidelines. Stability of the S, IS, and assay cocktails were investigated. Dried blood spots from 149 healthy adults, 100 newborns, and 60 patients with a lysosomal storage disorder (LSD) were tested using the modified assay. Results: In our study, the median enzyme activity measured in adults was generally increased 2–3–fold compared to the original method, results indicating higher precision. In the multiplex format, each of the 5 modified enzyme assays enabled unambiguous differentiation between samples from healthy individuals (adults and newborns) and the corresponding disease-specific samples. Conclusions: The modified multiplex enzyme assay with premixed S and IS is appropriate for use in high-throughput screening laboratories.

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Dildar, Shabnam, Asma Danish, Mehjabeen Imam, Arshi Naz, and Tahir Sultan Shamsi. "Diagnostic Performance of Three Serological Assays for Anti-SARS-CoV-2 Antibody Detection." National Journal of Health Sciences 5, no. 4 (July 12, 2021): 162–65. http://dx.doi.org/10.21089/njhs.54.0162.

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Abstract: Objective: To evaluate the diagnostic performance of Electrochemiluminescence (ECLIA) enzyme linked immunosorbent (ELISA) and lateral flow Immunofluorescence (LFIA) for anti-SARS-COV-2 antibody detection. Materials and Methods: Sensitivity was calculated with convalescent plasma (CP) donor’s samples. Specificity was checked by using pre-pandemic October 2019 samples. All samples were tested for anti-SARS-COV-2 antibody by using Electrochemiluminescence (ECLIA), Enzyme Linked Immunosorbent Assay (ELISA) and Lateral flow Immunofluorescence (LFIA) assay. Results: Total 55 patients were included, 45 patients were CP donors and 10 were Pre-Pandemic October 2019 samples archived from our blood bank. The ECLIA-total antibody, ELISA-IgG and LLFIA-IgG were positive in 41 (91.1%), 34 (75.5%) and 44 (97.75%) respectively. The highest sensitivity was observed for LFIA with highest specificity among all three assays. There was almost perfect agreement between LFIA and ECLIA (k=0.936, p<0.001) but there was fair agreement between LFIA and ELISA (k=0.412, p=0.001) and ECLIA and ELISA (k=0.357, p=0.001). Conclusion: The LFIA showed a higher sensitivity and specificity in comparison with ECLIA and ELISA. It might be due to fact that LFIA detect antibody against ncleocapsid and spike protein as well of SARS- COV-2 virus, while ECLIA and ELISA detects antibodies only against “N” Protein of SARS- COV-2 virus. Keywords: Convalescent plasma donors, Lateral flow Immunofluorescence assay, Electrochemiluminescence assay, Enzyme linked immunosorbent assay, Performance.

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Kanelakis, Kimon C., Heather L. Palomino, Lina Li, Jiejun Wu, Wen Yan, Mark D. Rosen, Michele C. Rizzolio, et al. "Characterization of a Robust Enzymatic Assay for Inhibitors of 2-Oxoglutarate-Dependent Hydroxylases." Journal of Biomolecular Screening 14, no. 6 (June 4, 2009): 627–35. http://dx.doi.org/10.1177/1087057109333976.

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The prolyl-4-hydroxylase proteins regulate the hypoxia-inducible transcription factors (HIFs) by hydroxylation of proline residues targeting HIF-1α for proteasomal degradation. Using the purified catalytic domain of prolyl hydroxylase 2 (PHD2181-417), an enzymatic assay has been developed to test inhibitors of the enzyme in vitro. Because PHD2 hydroxylates HIF-1α, with succinic acid produced as an end product, radiolabeled [5-14C]-2-oxoglutaric acid was used and formation of [14C]-succinic acid was measured to quantify PHD2181-417 enzymatic activity. Comparison of the separation of 2-oxoglutaric acid and succinic acid by either ion exchange chromatography or precipitation with phenylhydrazine showed similar results, but the quantification and throughput were vastly increased using the latter method. The PHD2 reaction was substrate and concentration dependent. The addition of iron to the enzyme reaction mix resulted in an increase in enzymatic activity. The Km value for 2-oxoglutaric acid was determined to be 0.9 µM, and known PHD2 inhibitors were used to validate the assay. In addition, the authors demonstrate that this assay can be applied to other 2-oxoglutaric acid-dependent enzymes, including the asparaginyl hydroxylase, factor-inhibiting HIF-1α (FIH). A concentration-dependent increase in succinic acid production using recombinant FIH enzyme with a synthetic peptide substrate was observed. The authors conclude that a by-product enzyme assay measuring the conversion of 2-oxoglutaric acid to succinic acid using the catalytic domain of the human PHD2 provides a convenient method for the biochemical evaluation of inhibitors of the 2-oxoglutaric acid-dependent hydroxylases. ( Journal of Biomolecular Screening 2009:627-635)

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Kunishima, ShinjI, Klyotaka Hayashi, Sentaro Kobayashi, Tomokl Naoe, and Ryuzo Ohno. "New enzyme-linked immunosorbent assay for glycocalicin in plasma." Clinical Chemistry 37, no. 2 (February 1, 1991): 169–72. http://dx.doi.org/10.1093/clinchem/37.2.169.

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Abstract A new sandwich-type enzyme-linked immunosorbent assay for quantifying glycocalicin, a proteolytic fragment of platelet membrane glycoprotein Ib, is described. The assay is based on the use of two monoclonal antibodies raised against glycoprotein Ib and involves the avidin-biotin technique. The detection limit is 7 micrograms/L and the range of glycocalicin determined in plasma is 0.01 to 1 mg/L. Assay time is 2 h. The intra-assay CV ranged from 3.6% to 5.2%, the interassay CV from 5.4% to 8.0%. Analytical recovery of purified glycocalicin added to a plasma pool averaged 96%. In 36 healthy subjects, the mean glycocalicin concentration in plasma was 0.36 (SD 0.07) mg/L (2.7 nmol/L). We conclude that this assay is suitable for measuring glycocalicin in plasma and is also more sensitive and precise than the previously published immunoassays based on competitive binding assay.

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Patel, P. D., and G. B. Hawes. "Estimation of food-grade galactomannans by enzyme-linked lectin assay." Food Hydrocolloids 2, no. 2 (June 1988): 107–18. http://dx.doi.org/10.1016/s0268-005x(88)80009-2.

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Rauser, Wilfried E., AndréA Quesnel, Joseph S. Lam, and Gordon G. Southam. "An enzyme-linked immunosorbent assay for plant cadmium-binding peptide." Plant Science 57, no. 1 (January 1988): 37–43. http://dx.doi.org/10.1016/0168-9452(88)90139-2.

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Mansueto, S., G. Vitale, C. Mocciaro, R. Librizzi, I. Friscia, V. Usticano, G. Gambino, and G. Reina. "Laboratory diagnosis of boutonneuse fever by enzyme-linked immunosorbent assay." Transactions of the Royal Society of Tropical Medicine and Hygiene 83, no. 6 (November 1989): 855–57. http://dx.doi.org/10.1016/0035-9203(89)90353-2.

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Moss, D. W., C. H. Self, Katrine B. Whitaker, Elaine Bailyes, K. Siddle, A. Johannsson, C. J. Stanley, and E. H. Cooper. "An enzyme-amplified monoclonal immunoenzymometric assay for prostatic acid phosphatase." Clinica Chimica Acta 152, no. 1-2 (October 1985): 85–94. http://dx.doi.org/10.1016/0009-8981(85)90179-2.

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Sakaki, Shujiro, Nobuo Nakabayashi, and Kazuhiko Ishihara. "Stabilization of an antibody conjugated with enzyme by 2-methacryloyloxyethyl phosphorylcholine copolymer in enzyme-linked immunosorbent assay." Journal of Biomedical Materials Research 47, no. 4 (December 15, 1999): 523–28. http://dx.doi.org/10.1002/(sici)1097-4636(19991215)47:4<523::aid-jbm8>3.0.co;2-j.

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Bury, J., and M. Rosseneu. "Quantification of human serum apolipoprotein AI by enzyme immunoassay." Clinical Chemistry 31, no. 2 (February 1, 1985): 247–51. http://dx.doi.org/10.1093/clinchem/31.2.247.

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Abstract We developed a quantitative assay for apolipoprotein AI (apo AI) in human serum, using a "sandwich"-type enzyme-linked immunosorbent assay. Diluted serum samples were pipetted into the wells of polystyrene microtiter plates that had been previously coated with purified rabbit anti-human apo AI antibodies. After incubation for 2 h and washing, antibodies conjugated to horseradish peroxidase (EC 1.11.1.7) were added and incubated for 2 h; after further washing, the bound enzyme was assayed by oxidation of o-phenylenediamine. Assay conditions were optimized for the incubation time and the amounts of coating antibodies and conjugate. Assay sensitivity is about 0.5 ng of apo AI, with a working range of 1 to 14 ng, similar to that of radioimmunoassays for human apo AI. The standard curves for apo AI in serum or HDL and for purified apo AI were parallel. Delipidation, heat treatment, or addition of detergents did not affect the amount of immunoassayable apo AI in human serum. The intra- and interassay CVs were 4 and 8%, respectively. Results for 100 serum samples compared well with those by immunonephelometry (r = 0.94).

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Nugent, A., E. McDermott, K. Duffy, N. O'Higgins, J. J. Fennelly, and M. J. Duffy. "Enzyme-Linked Immunosorbent Assay of C-Erbb-2 Oncoprotein in Breast Cancer." Clinical Chemistry 38, no. 8 (August 1, 1992): 1471–74. http://dx.doi.org/10.1093/clinchem/38.8.1471.

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Abstract Amplification or increased expression of the c-erbB-2 gene has previously been reported to be a prognostic marker for breast cancer. Gene amplification is usually measured by Southern blotting, whereas increased protein expression is usually detected by immunocytochemistry. We measured c-erbB-2 protein with an enzyme-linked immunosorbent assay (ELISA). High concentrations of oncoprotein were found in 25 of 161 (16%) primary breast cancers and in 3 of 6 (50%) breast cancer metastases. High concentrations were not found in normal breast tissue or benign breast tumors. In the primary cancers, high concentrations of c-erbB-2 protein were found more frequently (a) in estrogen receptor-negative tumors than in estrogen receptor-positive tumors, (b) in progesterone receptor-negative tumors than in progesterone-positive tumors, and (c) in axillary node-positive cancers than in node-negative cancers. Patients with tumors containing high amounts of the c-erbB-2 protein had a significantly shorter (P less than 0.001) disease-free interval and overall survival rate than did patients with low amounts. We conclude that assay of c-erbB-2 protein by ELISA is simple, rapid, and quantitative and offers important prognostic information in breast cancer.

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Honda, Mitsuo, Shigeki Nagao, Naoki Yamamoto, Yuetsu Tanaka, Hideki Tozawa, and Tohru Tokunaga. "Flourescence sandwich enzyme-linked immunosorbent assay for detecting human interleukin-2 receptors." Journal of Immunological Methods 110, no. 1 (May 1988): 129–36. http://dx.doi.org/10.1016/0022-1759(88)90092-0.

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AL-SHAMAHY, H. A., and S. G. WRIGHT. "Enzyme-linked immunosorbent assay for brucella antigen detection in human sera." Journal of Medical Microbiology 47, no. 2 (February 1, 1998): 169–72. http://dx.doi.org/10.1099/00222615-47-2-169.

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Manclús, Juan J., and Angel Montoya. "Development of an Enzyme-Linked Immunosorbent Assay for 3,5,6-Trichloro-2-pyridinol. 2. Assay Optimization and Application to Environmental Water Samples." Journal of Agricultural and Food Chemistry 44, no. 11 (January 1996): 3710–16. http://dx.doi.org/10.1021/jf950657h.

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Gniffke, Edward P., Whitney E. Harrington, Nicholas Dambrauskas, Yonghou Jiang, Olesya Trakhimets, Vladimir Vigdorovich, Lisa Frenkel, D. Noah Sather, and Stephen E. P. Smith. "Plasma From Recovered COVID-19 Patients Inhibits Spike Protein Binding to ACE2 in a Microsphere-Based Inhibition Assay." Journal of Infectious Diseases 222, no. 12 (August 15, 2020): 1965–73. http://dx.doi.org/10.1093/infdis/jiaa508.

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Abstract We present a microsphere-based flow cytometry assay that quantifies the ability of plasma to inhibit the binding of spike protein to angiotensin-converting enzyme 2. Plasma from 22 patients who had recovered from mild coronavirus disease 2019 (COVID-19) and expressed anti–spike protein trimer immunoglobulin G inhibited angiotensin-converting enzyme 2–spike protein binding to a greater degree than controls. The degree of inhibition was correlated with anti–spike protein immunoglobulin G levels, neutralizing titers in a pseudotyped lentiviral assay, and the presence of fever during illness. This inhibition assay may be broadly useful to quantify the functional antibody response of patients recovered from COVID-19 or vaccine recipients in a cell-free assay system.

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