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Journal articles on the topic 'Therapeutic enzymes'

Author: Grafiati

Published: 4 June 2021

Last updated: 15 February 2022

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1

Städler, Brigitte, and Alexander N. Zelikin. "Enzyme prodrug therapies and therapeutic enzymes." Advanced Drug Delivery Reviews 118 (September 2017): 1. http://dx.doi.org/10.1016/j.addr.2017.10.006.

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2

Bax, Bridget E. "Erythrocytes as Carriers of Therapeutic Enzymes." Pharmaceutics 12, no. 5 (May 8, 2020): 435. http://dx.doi.org/10.3390/pharmaceutics12050435.

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Therapeutic enzymes are administered for the treatment of a wide variety of diseases. They exert their effects through binding with a high affinity and specificity to disease-causing substrates to catalyze their conversion to a non-noxious product, to induce an advantageous physiological change. However, the metabolic and clinical efficacies of parenterally or intramuscularly administered therapeutic enzymes are very often limited by short circulatory half-lives and hypersensitive and immunogenic reactions. Over the past five decades, the erythrocyte carrier has been extensively studied as a strategy for overcoming these limitations and increasing therapeutic efficacy. This review examines the rationale for the different therapeutic strategies that have been applied to erythrocyte-mediated enzyme therapy. These strategies include their application as circulating bioreactors, targeting the monocyte–macrophage system, the coupling of enzymes to the surface of the erythrocyte and the engineering of CD34+ hematopoietic precursor cells for the expression of therapeutic enzymes. An overview of the diverse biomedical applications for which they have been investigated is also provided, including the detoxification of exogenous chemicals, thrombolytic therapy, enzyme replacement therapy for metabolic diseases and antitumor therapy.

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3

Noten, J. B. G. M., W. M. A. Verhoeven, S. Tuinier, and D. Touw. "Therapeutic drug monitoring." Acta Neuropsychiatrica 11, no. 1 (March 1999): 15–16. http://dx.doi.org/10.1017/s0924270800036309.

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SUMMARYThe cytochrome P450 iso-enzyme system plays a key role in the biotransformation of many drugs, including psychotropics. Its activity is determined by both genetic and environmental factors. The most important iso-enzymes for psychiatry in general are P450 IID6, 3A4 and 1A2. Knowledge about the involvement of these enzymes and biotransformation processes is mandatory because of the individual variability in their metabolic capacity. Regular measurement of plasmaconcentrations of (psycho)pharmacological compounds is therefore essential. In addition, the potential value of pheno- and/or genotyping has to be investigated.

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4

Wiederschain, G. Ya, and M. Baldry. "Directory of therapeutic enzymes." Biochemistry (Moscow) 71, no. 11 (November 2006): 1289–90. http://dx.doi.org/10.1134/s0006297906110162.

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5

Alisi, Anna, Sara Tomaselli, Clara Balsano, and Angela Gallo. "Hepatitis C virus therapeutics: Editing enzymes promising therapeutic targets?" Hepatology 54, no. 2 (July 25, 2011): 742. http://dx.doi.org/10.1002/hep.24409.

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6

Sioud, Mouldy, and Marianne Leirdal. "Therapeutic RNA and DNA enzymes." Biochemical Pharmacology 60, no. 8 (October 2000): 1023–26. http://dx.doi.org/10.1016/s0006-2952(00)00395-6.

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7

Maximov, V., V. Reukov, and A. A. Vertegel. "Targeted delivery of therapeutic enzymes." Journal of Drug Delivery Science and Technology 19, no. 5 (2009): 311–20. http://dx.doi.org/10.1016/s1773-2247(09)50066-4.

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8

Kokotos, George. "Lipolytic enzymes as therapeutic targets." European Journal of Lipid Science and Technology 110, no. 12 (December 2008): 1081–83. http://dx.doi.org/10.1002/ejlt.200800249.

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9

Azmi, Wamik, and Shabnam Chaudhary. "ARTHROBACTER AS BIOFACTORY OF THERAPEUTIC ENZYMES." International Journal of Pharmacy and Pharmaceutical Sciences 10, no. 11 (November 1, 2018): 1. http://dx.doi.org/10.22159/ijpps.2018v10i11.25933.

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Therapeutic enzymes are proteins which can be used to treat rare and deadly diseases. They represent a small but profitable market. Therapeutic enzymes are superior to non-enzymatic drugs owing to their high specificity toward the target and also their ability to multiple substrate conversion. They are essential for speeding up all the metabolic processes and many a life-supporting chemical inter-conversions. Actinomycetes including Arthrobacter form an enormous reservoir of secondary metabolites and enzymes. The characterization of L-asparaginase, β-glucosidase, urate oxidase, methionine γ-lyase, acetyl cholinesterase, and arginase activities from actinomycetes Arthrobacter clearly demonstrate the potential of Arthrobacter as potent producer of therapeutic enzymes. These metabolic enzymes can be used either separately or in combination with other therapies for the treatment of several diseases such as leukemia, gout, asthma, and neurological disorders. The objective of this review is to compile the information on the application of therapeutic enzymes produced by Arthrobacter and their future prospects as drugs.

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10

Kaplan, Jeffrey B. "Therapeutic Potential of Biofilm-Dispersing Enzymes." International Journal of Artificial Organs 32, no. 9 (September 2009): 545–54. http://dx.doi.org/10.1177/039139880903200903.

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Surface-attached colonies of bacteria known as biofilms play a major role in the pathogenesis of medical device infections. Biofilm colonies are notorious for their resistance to antibiotics and host defenses, which makes most device infections difficult or impossible to eradicate. Bacterial cells in a biofilm are held together by an extracellular polymeric matrix that is synthesized by the bacteria themselves. Enzymes that degrade biofilm matrix polymers have been shown to inhibit bio film formation, detach established bio film colonies, and render biofilm cells sensitive to killing by antimicrobial agents. This review discusses the potential use of biofilm matrix-degrading enzymes as anti-biofilm agents for the treatment and prevention of device infections. Two enzymes, deoxyribonuclease I and the glycoside hydrolase dispersin B, will be reviewed in detail. In vitro and in vivo studies demonstrating the anti-biofilm activities of these two enzymes will be summarized, and the therapeutic potential and possible drawbacks of using these enzymes as clinical agents will be discussed.

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11

Haeggström, Jesper Z. "Leukotriene biosynthetic enzymes as therapeutic targets." Journal of Clinical Investigation 128, no. 7 (July 2, 2018): 2680–90. http://dx.doi.org/10.1172/jci97945.

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12

Dean, Scott N., Kendrick B. Turner, Igor L. Medintz, and Scott A. Walper. "Targeting and delivery of therapeutic enzymes." Therapeutic Delivery 8, no. 7 (July 2017): 577–95. http://dx.doi.org/10.4155/tde-2017-0020.

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13

Meghwanshi, Gautam Kumar, Navpreet Kaur, Swati Verma, Narendra Kumar Dabi, Abhishek Vashishtha, P. D. Charan, Praveen Purohit, H. S. Bhandari, N. Bhojak, and Rajender Kumar. "Enzymes for pharmaceutical and therapeutic applications." Biotechnology and Applied Biochemistry 67, no. 4 (May 8, 2020): 586–601. http://dx.doi.org/10.1002/bab.1919.

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14

Tandon, Siddhi, Anjali Sharma, Shikha Singh, Sumit Sharma, and Saurabh Jyoti Sarma. "Therapeutic enzymes: Discoveries, production and applications." Journal of Drug Delivery Science and Technology 63 (June 2021): 102455. http://dx.doi.org/10.1016/j.jddst.2021.102455.

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15

Gubergrits, N. B., N. V. Byelyayeva, A. Y. Klochkov, G. М. Lukashevish, and P. G. Fomenko. "Advantages and therapeutic capacities of digestive enzymes preparations of non-animal origin." Bulletin of the Club of Pancreatologists 39, no. 1 (March 6, 2018): 16–21. http://dx.doi.org/10.33149/vkp.2018.01.03.

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The article presents a literature review on the features and benefits of digestive enzymes preparations of non-animal origin, i.e. drugs which include plant, microbial or fungal enzymes. Diseases and conditions upon which such drugs are prescribed have been pathogenetically substantiated. The results of evidence studies are presented, the outcomes of which conclude that the biotechnological enzyme preparation of bacterial origin is effective and safe in the treatment of cystic fibrosis. Peculiar attention is paid to Digest 365 that contains not only amylo-, proteo- and lipolytic enzymes, but also cellulose and lactase.

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16

Eckman, E. A., and C. B. Eckman. "Aβ-degrading enzymes: modulators of Alzheimer's disease pathogenesis and targets for therapeutic intervention." Biochemical Society Transactions 33, no. 5 (October 26, 2005): 1101–5. http://dx.doi.org/10.1042/bst0331101.

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The accumulation of Aβ (amyloid β-protein) peptides in the brain is a pathological hallmark of all forms of AD (Alzheimer's disease) and reducing Aβ levels can prevent or reverse cognitive deficits in mouse models of the disease. Aβ is produced continuously and its concentration is determined in part by the activities ofseveral degradative enzymes, including NEP (neprilysin), IDE (insulin-degrading enzyme), ECE-1 (endothelinconverting enzyme 1) and ECE-2, and probably plasmin. Decreased activity of any of these enzymes due to genetic mutation, or age- or disease-related alterations in gene expression or proteolytic activity, may increase the risk for AD. Conversely, increased expression of these enzymes may confer a protective effect. Increasing Aβ degradation through gene therapy, transcriptional activation or even pharmacological activation of the Aβ-degrading enzymes represents a novel therapeutic strategy for the treatment of AD that is currently being evaluated in cell-culture and animal models. In this paper, we will review the roles of NEP, IDE, ECE and plasmin in determining endogenous Aβ concentration, highlighting recent results concerning the regulation of these enzymes and their potential as therapeutic targets.

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17

R. Temsaah, Hasnaa, Ahmed F. Azmy, Mai Raslan, Amr E. Ahmed, and Walaa G. Hozayen. "Isolation and Characterization of Thermophilic Enzymes Producing Microorganisms for Potential Therapeutic and Industrial Use." Journal of Pure and Applied Microbiology 12, no. 4 (December 30, 2018): 1687–702. http://dx.doi.org/10.22207/jpam.12.4.02.

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18

Verstovsek, Srdan. "Therapeutic potential of JAK2 inhibitors." Hematology 2009, no. 1 (January 1, 2009): 636–42. http://dx.doi.org/10.1182/asheducation-2009.1.636.

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AbstractThe discovery of an activating tyrosine kinase mutation JAK2V617F in myeloproliferative neoplasms (MPNs), polycythemia vera (PV), essential thrombocythemia (ET) and primary myelofibrosis (PMF) has resulted in the development of JAK2 inhibitors, of which several are being evaluated in phase I/II clinical studies. It is important to recognize that because the V617F mutation is localized in a region outside the adenosine triphosphate (ATP)-binding pocket of JAK2 enzyme, ATP-competitive inhibitors of JAK2 kinase (like the current JAK2 inhibitors in the clinic) are not likely to discriminate between wild-type and mutant JAK2 enzymes. Therefore, JAK2 inhibitors, by virtue of their near equipotent activity against wild-type JAK2 that is important for normal hematopoiesis, may have adverse myelosuppression as an expected side effect, if administered at doses that aim to completely inhibit the mutant JAK2 enzyme. While they may prove to be effective in controlling hyperproliferation of hematopoietic cells in PV and ET, they may not be able to eliminate mutant clones. On the other hand, JAK inhibitors may have great therapeutic benefit by controlling the disease for patients with MPNs who suffer from debilitating signs (eg, splenomegaly) or constitutional symptoms (which presumably result from high levels of circulating cytokines that signal through JAK enzymes). Indeed, the primary clinical benefits observed so far in MF patients have been significant reduction is splenomegaly, elimination of debilitating disease-related symptoms, and weight gain. Most importantly, patients with and without the JAK2V617F mutation appear to benefit to the same extent. In this review we summarize current clinical experience with JAK2 inhibitors in MPNs.

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19

Lim, Key-Hwan, and Kwang-Hyun Baek. "Deubiquitinating Enzymes as Therapeutic Targets in Cancer." Current Pharmaceutical Design 19, no. 22 (May 1, 2013): 4039–52. http://dx.doi.org/10.2174/1381612811319220013.

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20

Martins, M. B. F., A. P. V. Conçoives, J. C. Jorge, and M. E. M. Cruz. "Acylated enzymes: properties and potential therapeutic applications." European Journal of Pharmacology 183, no. 2 (July 1990): 401. http://dx.doi.org/10.1016/0014-2999(90)93282-u.

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21

López-Jaramillo, P., and J. P. Casas. "Blockade of endothelial enzymes: new therapeutic targets." Journal of Human Hypertension 16, S1 (March 2002): S100—S103. http://dx.doi.org/10.1038/sj.jhh.1001353.

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22

Barghout, Samir H., and Aaron D. Schimmer. "E1 Enzymes as Therapeutic Targets in Cancer." Pharmacological Reviews 73, no. 1 (November 11, 2020): 1–56. http://dx.doi.org/10.1124/pharmrev.120.000053.

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23

ROSSI, J., and N. SARVER. "RNA enzymes (ribozymes) as antiviral therapeutic agents." Trends in Biotechnology 8 (1990): 179–83. http://dx.doi.org/10.1016/0167-7799(90)90169-x.

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24

Gomez-Larrauri, Ana, Upasana Das Adhikari, Marta Aramburu-Nuñez, Antía Custodia, and Alberto Ouro. "Ceramide Metabolism Enzymes—Therapeutic Targets against Cancer." Medicina 57, no. 7 (July 19, 2021): 729. http://dx.doi.org/10.3390/medicina57070729.

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Sphingolipids are both structural molecules that are essential for cell architecture and second messengers that are involved in numerous cell functions. Ceramide is the central hub of sphingolipid metabolism. In addition to being the precursor of complex sphingolipids, ceramides induce cell cycle arrest and promote cell death and inflammation. At least some of the enzymes involved in the regulation of sphingolipid metabolism are altered in carcinogenesis, and some are targets for anticancer drugs. A number of scientific reports have shown how alterations in sphingolipid pools can affect cell proliferation, survival and migration. Determination of sphingolipid levels and the regulation of the enzymes that are implicated in their metabolism is a key factor for developing novel therapeutic strategies or improving conventional therapies. The present review highlights the importance of bioactive sphingolipids and their regulatory enzymes as targets for therapeutic interventions with especial emphasis in carcinogenesis and cancer dissemination.

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25

Mishra, Abhinav P., Suresh Chandra, Ruchi Tiwari, Ashish Srivastava, and Gaurav Tiwari. "Therapeutic Potential of Prodrugs Towards Targeted Drug Delivery." Open Medicinal Chemistry Journal 12, no. 1 (October 23, 2018): 111–23. http://dx.doi.org/10.2174/1874104501812010111.

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In designing of Prodrugs, targeting can be achieved in two ways: site-specified drug delivery and site-specific drug bioactivation. Prodrugs can be designed to target specific enzymes or carriers by considering enzyme-substrate specificity or carrier-substrate specificity in order to overcome various undesirable drug properties. There are certain techniques which are used for tumor targeting such as Antibody Directed Enzyme Prodrug Therapy [ADEPT] Gene-Directed Enzyme Prodrug Therapy [GDEPT], Virus Directed Enzyme Prodrug Therapy [VDEPT] and Gene Prodrug Activation Therapy [GPAT]. Our review focuses on the Prodrugs used in site-specific drug delivery system specially on tumor targeting.

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26

Zhang, Weisheng, Min Chen, David B. West, and Anthony F. Purchio. "Visualizing Drug Efficacy In Vivo." Molecular Imaging 4, no. 2 (April 1, 2005): 153535002005051. http://dx.doi.org/10.1162/15353500200505109.

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Many enzymes are therapeutic targets for drug discovery, whereas other enzymes are important for understanding drug metabolism and pharmacokinetics during compound testing in animals. Testing of drug efficacy and metabolism in an animal model requires the measurement of disease endpoints as well as assays of enzyme activity in specific tissues at selected time points during treatment. This requires the removal of tissue and biochemical assays. Techniques to noninvasively assess drug effects on enzyme activity using imaging technology would facilitate understanding of drug efficacy, pharmacokinetics, and drug metabolism. Using a commercially available cytochrome P−450 3A substrate whose oxidized product is a luciferase substrate, we show for the first time that cytochrome P−450 enzyme activity can be measured in vivo in real time by bioluminescent imaging. This imaging approach could be applicable to study drug effects on therapeutic target enzymes, as well as drug metabolism enzymes.

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27

Fathi, Marziyeh, Azam Safary, and Jaleh Barar. "Therapeutic impacts of enzyme-responsive smart nanobiosystems." BioImpacts 10, no. 1 (November 25, 2019): 1–4. http://dx.doi.org/10.15171/bi.2020.01.

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An important arena of the sophisticated nanosystems (NSs) is the combination of the responsive features of NSs with the biocatalytic properties of enzymes. The development of such smart drug delivery systems (DDSs) has seminal effectiveness in targeting, imaging, and monitoring of cancer. These NSs can exhibit site-specific delivery of the toxic cargo in response to the endogenous/exogenous stimuli. Enzyme responsive/targeted DDSs display enhanced accumulation of cargo molecules in the tumor microenvironment (TME) with a spatiotemporal controlled-release behavior. Based on the unique features of enzyme responsive/targeted DDSs, they offer incredible promise in overcoming some limitations of the currently used conventional DDSs. Taken all, targeting TME with the enzyme-responsive targeted DDSs may lead to versatile clinical outcomes in various malignancies.

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28

Kim, Woo-Jin, Hye-Lim Shin, Bong-Soo Kim, Hyun-Jung Kim, and Hyun-Mo Ryoo. "RUNX2-modifying enzymes: therapeutic targets for bone diseases." Experimental & Molecular Medicine 52, no. 8 (August 2020): 1178–84. http://dx.doi.org/10.1038/s12276-020-0471-4.

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Abstract RUNX2 is a master transcription factor of osteoblast differentiation. RUNX2 expression in the bone and osteogenic front of a suture is crucial for cranial suture closure and membranous bone morphogenesis. In this manner, the regulation of RUNX2 is precisely controlled by multiple posttranslational modifications (PTMs) mediated by the stepwise recruitment of multiple enzymes. Genetic defects in RUNX2 itself or in its PTM regulatory pathways result in craniofacial malformations. Haploinsufficiency in RUNX2 causes cleidocranial dysplasia (CCD), which is characterized by open fontanelle and hypoplastic clavicles. In contrast, gain-of-function mutations in FGFRs, which are known upstream stimulating signals of RUNX2 activity, cause craniosynostosis (CS) characterized by premature suture obliteration. The identification of these PTM cascades could suggest suitable drug targets for RUNX2 regulation. In this review, we will focus on the mechanism of RUNX2 regulation mediated by PTMs, such as phosphorylation, prolyl isomerization, acetylation, and ubiquitination, and we will summarize the therapeutics associated with each PTM enzyme for the treatment of congenital cranial suture anomalies.

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29

Almeida, Fausto, Julie M. Wolf, and Arturo Casadevall. "Virulence-Associated Enzymes of Cryptococcus neoformans." Eukaryotic Cell 14, no. 12 (October 9, 2015): 1173–85. http://dx.doi.org/10.1128/ec.00103-15.

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ABSTRACTEnzymes play key roles in fungal pathogenesis. Manipulation of enzyme expression or activity can significantly alter the infection process, and enzyme expression profiles can be a hallmark of disease. Hence, enzymes are worthy targets for better understanding pathogenesis and identifying new options for combatting fungal infections. Advances in genomics, proteomics, transcriptomics, and mass spectrometry have enabled the identification and characterization of new fungal enzymes. This review focuses on recent developments in the virulence-associated enzymes fromCryptococcus neoformans. The enzymatic suite ofC. neoformanshas evolved for environmental survival, but several of these enzymes play a dual role in colonizing the mammalian host. We also discuss new therapeutic and diagnostic strategies that could be based on the underlying enzymology.

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30

de la Fuente, Miguel, Laura Lombardero, Alfonso Gómez-González, Cristina Solari, Iñigo Angulo-Barturen, Arantxa Acera, Elena Vecino, Egoitz Astigarraga, and Gabriel Barreda-Gómez. "Enzyme Therapy: Current Challenges and Future Perspectives." International Journal of Molecular Sciences 22, no. 17 (August 25, 2021): 9181. http://dx.doi.org/10.3390/ijms22179181.

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In recent years, enzymes have risen as promising therapeutic tools for different pathologies, from metabolic deficiencies, such as fibrosis conditions, ocular pathologies or joint problems, to cancer or cardiovascular diseases. Treatments based on the catalytic activity of enzymes are able to convert a wide range of target molecules to restore the correct physiological metabolism. These treatments present several advantages compared to established therapeutic approaches thanks to their affinity and specificity properties. However, enzymes present some challenges, such as short in vivo half-life, lack of targeted action and, in particular, patient immune system reaction against the enzyme. For this reason, it is important to monitor serum immune response during treatment. This can be achieved by conventional techniques (ELISA) but also by new promising tools such as microarrays. These assays have gained popularity due to their high-throughput analysis capacity, their simplicity, and their potential to monitor the immune response of patients during enzyme therapies. In this growing field, research is still ongoing to solve current health problems such as COVID-19. Currently, promising therapeutic alternatives using the angiotensin-converting enzyme 2 (ACE2) are being studied to treat COVID-19.

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31

Jacomin, Anne-Claire, Emmanuel Taillebourg, and Marie-Odile Fauvarque. "Deubiquitinating Enzymes Related to Autophagy: New Therapeutic Opportunities?" Cells 7, no. 8 (August 19, 2018): 112. http://dx.doi.org/10.3390/cells7080112.

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Autophagy is an evolutionary conserved catabolic process that allows for the degradation of intracellular components by lysosomes. This process can be triggered by nutrient deprivation, microbial infections or other challenges to promote cell survival under these stressed conditions. However, basal levels of autophagy are also crucial for the maintenance of proper cellular homeostasis by ensuring the selective removal of protein aggregates and dysfunctional organelles. A tight regulation of this process is essential for cellular survival and organismal health. Indeed, deregulation of autophagy is associated with a broad range of pathologies such as neuronal degeneration, inflammatory diseases, and cancer progression. Ubiquitination and deubiquitination of autophagy substrates, as well as components of the autophagic machinery, are critical regulatory mechanisms of autophagy. Here, we review the main evidence implicating deubiquitinating enzymes (DUBs) in the regulation of autophagy. We also discuss how they may constitute new therapeutic opportunities in the treatment of pathologies such as cancers, neurodegenerative diseases or infections.

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32

Giles, Gregory, and Ram Sharma. "Topoisomerase Enzymes as Therapeutic Targets for Cancer Chemotherapy." Medicinal Chemistry 1, no. 4 (June 1, 2005): 383–94. http://dx.doi.org/10.2174/1573406054368738.

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33

Poondla, Naresh, Arun Pandian Chandrasekaran, Kye-Seong Kim, and Suresh Ramakrishna. "Deubiquitinating enzymes as cancer biomarkers: new therapeutic opportunities?" BMB Reports 52, no. 3 (March 31, 2019): 181–89. http://dx.doi.org/10.5483/bmbrep.2019.52.3.048.

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34

Keppler, Brian R., and Trevor K. Archer. "Chromatin-modifying enzymes as therapeutic targets – Part 1." Expert Opinion on Therapeutic Targets 12, no. 10 (September 9, 2008): 1301–12. http://dx.doi.org/10.1517/14728222.12.10.1301.

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35

Keppler, Brian R., and Trevor K. Archer. "Chromatin-modifying enzymes as therapeutic targets – Part 2." Expert Opinion on Therapeutic Targets 12, no. 11 (October 14, 2008): 1457–67. http://dx.doi.org/10.1517/14728222.12.11.1457.

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36

Meletis, Chris D., and Jason E. Barker. "Therapeutic Enzymes: Using the Body's Helpers as Healers." Alternative and Complementary Therapies 11, no. 2 (April 2005): 74–77. http://dx.doi.org/10.1089/act.2005.11.74.

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37

Falagas, Matthew E., Drosos E. Karageorgopoulos, and Patrice Nordmann. "Therapeutic options for infections withEnterobacteriaceaeproducing carbapenem-hydrolyzing enzymes." Future Microbiology 6, no. 6 (June 2011): 653–66. http://dx.doi.org/10.2217/fmb.11.49.

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38

Estrada, Lina Herrera, Stanley Chu, and Julie A. Champion. "Protein Nanoparticles for Intracellular Delivery of Therapeutic Enzymes." Journal of Pharmaceutical Sciences 103, no. 6 (June 2014): 1863–71. http://dx.doi.org/10.1002/jps.23974.

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39

Itel, Fabian, Philipp S. Schattling, Yan Zhang, and Brigitte Städler. "Enzymes as key features in therapeutic cell mimicry." Advanced Drug Delivery Reviews 118 (September 2017): 94–108. http://dx.doi.org/10.1016/j.addr.2017.09.006.

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40

Wiseman, Alan. "Therapeutic proteins and enzymes from genetically engineered yeasts." Endeavour 20, no. 3 (January 1996): 130–32. http://dx.doi.org/10.1016/0160-9327(96)10025-9.

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41

Vachher, Meenakshi, Aparajita Sen, Rachna Kapila, and Arti Nigam. "Microbial therapeutic enzymes: A promising area of biopharmaceuticals." Current Research in Biotechnology 3 (2021): 195–208. http://dx.doi.org/10.1016/j.crbiot.2021.05.006.

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42

Pyatakova, N. V., and I. S. Severina. "Soluble guanylate cyclase in the molecular mechanism underlying the therapeutic action of drugs." Biomeditsinskaya Khimiya 58, no. 1 (January 2012): 32–42. http://dx.doi.org/10.18097/pbmc20125801032.

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The influence of ambroxol - a mucolytic drug - on the activity of human platelet soluble guanylate cyclase and rat lung soluble guanylate cyclase and activation of both enzymes by NO-donors (sodium nitroprusside and Sin-1) were investigated. Ambroxol in the concentration range from 0.1 to 10 μM had no effect on the basal activity of both enzymes. Ambroxol inhibited in a concentration-dependent manner the sodium nitroprusside-induced human platelet soluble guanylate cyclase and rat lung soluble guanylate cyclase with the IC50 values 3.9 and 2.1 μM, respectively. Ambroxol did not influence the stimulation of both enzymes by protoporphyrin IX.The influence of artemisinin - an antimalarial drug - on human platelet soluble guanylate cyclase activity and the enzyme activation by NO-donors were investigated. Artemisinin (0.1-100 μM) had no effect on the basal activity of the enzyme. Artemisinin inhibited in a concentration-dependent manner the sodium nitroprusside-induced activation of human platelet guanylate cyclase with an IC50 value 5.6 μM. Artemisinin (10 μM) also inhibited (by 71±4.0%) the activation of the enzyme by thiol-dependent NO-donor the derivative of furoxan, 3,4-dicyano-1,2,5-oxadiazolo-2-oxide (10 μM), but did not influence the stimulation of soluble guanylate cyclase by protoporphyrin IX. It was concluded that the sygnalling system NO-soluble guanylate cyclase-cGMP is involved in the molecular mechanism of the therapeutic action of ambroxol and artemisinin.

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Duskey, Jason Thomas, Federica da Ros, Ilaria Ottonelli, Barbara Zambelli, Maria Angela Vandelli, Giovanni Tosi, and Barbara Ruozi. "Enzyme Stability in Nanoparticle Preparations Part 1: Bovine Serum Albumin Improves Enzyme Function." Molecules 25, no. 20 (October 9, 2020): 4593. http://dx.doi.org/10.3390/molecules25204593.

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Enzymes have gained attention for their role in numerous disease states, calling for research for their efficient delivery. Loading enzymes into polymeric nanoparticles to improve biodistribution, stability, and targeting in vivo has led the field with promising results, but these enzymes still suffer from a degradation effect during the formulation process that leads to lower kinetics and specific activity leading to a loss of therapeutic potential. Stabilizers, such as bovine serum albumin (BSA), can be beneficial, but the knowledge and understanding of their interaction with enzymes are not fully elucidated. To this end, the interaction of BSA with a model enzyme B-Glu, part of the hydrolase class and linked to Gaucher disease, was analyzed. To quantify the natural interaction of beta-glucosidase (B-Glu,) and BSA in solution, isothermal titration calorimetry (ITC) analysis was performed. Afterwards, polymeric nanoparticles encapsulating these complexes were fully characterized, and the encapsulation efficiency, activity of the encapsulated enzyme, and release kinetics of the enzyme were compared. ITC results showed that a natural binding of 1:1 was seen between B-Glu and BSA. Complex concentrations did not affect nanoparticle characteristics which maintained a size between 250 and 350 nm, but increased loading capacity (from 6% to 30%), enzyme activity, and extended-release kinetics (from less than one day to six days) were observed for particles containing higher B-Glu:BSA ratios. These results highlight the importance of understanding enzyme:stabilizer interactions in various nanoparticle systems to improve not only enzyme activity but also biodistribution and release kinetics for improved therapeutic effects. These results will be critical to fully characterize and compare the effect of stabilizers, such as BSA with other, more relevant therapeutic enzymes for central nervous system (CNS) disease treatments.

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Ma, Dik-Lung, Modi Wang, Zhifeng Mao, Chao Yang, Chan-Tat Ng, and Chung-Hang Leung. "Rhodium complexes as therapeutic agents." Dalton Transactions 45, no. 7 (2016): 2762–71. http://dx.doi.org/10.1039/c5dt04338g.

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Kerr, William G., Chiara Pedicone, Shawn Dormann, Angela Pacherille, and John D. Chisholm. "Small molecule targeting of SHIP1 and SHIP2." Biochemical Society Transactions 48, no. 1 (February 12, 2020): 291–300. http://dx.doi.org/10.1042/bst20190775.

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Modulating the activity of the Src Homology 2 (SH2) — containing Inositol 5′-Phosphatase (SHIP) enzyme family with small molecule inhibitors provides a useful and unconventional method of influencing cell signaling in the PI3K pathway. The development of small molecules that selectively target one of the SHIP paralogs (SHIP1 or SHIP2) as well as inhibitors that simultaneously target both enzymes have provided promising data linking the phosphatase activity of the SHIP enzymes to disorders and disease states that are in dire need of new therapeutic targets. These include cancer, immunotherapy, diabetes, obesity, and Alzheimer's disease. In this mini-review, we will provide a brief overview of research in these areas that support targeting SHIP1, SHIP2 or both enzymes for therapeutic purposes.

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Fultang, Livingstone, Sarah Booth, Orli Yogev, Barbara Martins da Costa, Vanessa Tubb, Silvia Panetti, Victoria Stavrou, et al. "Metabolic engineering against the arginine microenvironment enhances CAR-T cell proliferation and therapeutic activity." Blood 136, no. 10 (September 3, 2020): 1155–60. http://dx.doi.org/10.1182/blood.2019004500.

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Abstract Hematological and solid cancers catabolize the semiessential amino acid arginine to drive cell proliferation. However, the resulting low arginine microenvironment also impairs chimeric antigen receptor T cells (CAR-T) cell proliferation, limiting their efficacy in clinical trials against hematological and solid malignancies. T cells are susceptible to the low arginine microenvironment because of the low expression of the arginine resynthesis enzymes argininosuccinate synthase (ASS) and ornithine transcarbamylase (OTC). We demonstrate that T cells can be reengineered to express functional ASS or OTC enzymes, in concert with different chimeric antigen receptors. Enzyme modifications increase CAR-T cell proliferation, with no loss of CAR cytotoxicity or increased exhaustion. In vivo, enzyme-modified CAR-T cells lead to enhanced clearance of leukemia or solid tumor burden, providing the first metabolic modification to enhance CAR-T cell therapies.

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Gurung, Neelam, Sumanta Ray, Sutapa Bose, and Vivek Rai. "A Broader View: Microbial Enzymes and Their Relevance in Industries, Medicine, and Beyond." BioMed Research International 2013 (2013): 1–18. http://dx.doi.org/10.1155/2013/329121.

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Enzymes are the large biomolecules that are required for the numerous chemical interconversions that sustain life. They accelerate all the metabolic processes in the body and carry out a specific task. Enzymes are highly efficient, which can increase reaction rates by 100 million to 10 billion times faster than any normal chemical reaction. Due to development in recombinant technology and protein engineering, enzymes have evolved as an important molecule that has been widely used in different industrial and therapeutical purposes. Microbial enzymes are currently acquiring much attention with rapid development of enzyme technology. Microbial enzymes are preferred due to their economic feasibility, high yields, consistency, ease of product modification and optimization, regular supply due to absence of seasonal fluctuations, rapid growth of microbes on inexpensive media, stability, and greater catalytic activity. Microbial enzymes play a major role in the diagnosis, treatment, biochemical investigation, and monitoring of various dreaded diseases. Amylase and lipase are two very important enzymes that have been vastly studied and have great importance in different industries and therapeutic industry. In this review, an approach has been made to highlight the importance of different enzymes with special emphasis on amylase and lipase in the different industrial and medical fields.

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Galliani, Marianna, Chiara Tremolanti, and Giovanni Signore. "Nanocarriers for Protein Delivery to the Cytosol: Assessing the Endosomal Escape of Poly(Lactide-co-Glycolide)-Poly(Ethylene Imine) Nanoparticles." Nanomaterials 9, no. 4 (April 23, 2019): 652. http://dx.doi.org/10.3390/nano9040652.

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Therapeutic proteins and enzymes are a group of interesting candidates for the treatment of numerous diseases, but they often require a carrier to avoid degradation and rapid clearance in vivo. To this end, organic nanoparticles (NPs) represent an excellent choice due to their biocompatibility, and cross-linked enzyme aggregates (CLEAs)-loaded poly (lactide-co-glycolide) (PLGA) NPs have recently attracted attention as versatile tools for targeted enzyme delivery. However, PLGA NPs are taken up by cells via endocytosis and are typically trafficked into lysosomes, while many therapeutic proteins and enzymes should reach the cellular cytosol to perform their activity. Here, we designed a CLEAs-based system implemented with a cationic endosomal escape agent (poly(ethylene imine), PEI) to extend the use of CLEA NPs also to cytosolic enzymes. We demonstrated that our system can deliver protein payloads at cytoplasm level by two different mechanisms: Endosomal escape and direct translocation. Finally, we applied this system to the cytoplasmic delivery of a therapeutically relevant enzyme (superoxide dismutase, SOD) in vitro.

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Oliveira, Maycon Douglas de, Carlos Johnantan Tolentino Vaz, Liliane Maciel de Oliveira, and Carla Zanella Guidini. "L-asparaginase: therapeutic use and applications in the food industry – a review." Research, Society and Development 10, no. 10 (August 21, 2021): e596101018980. http://dx.doi.org/10.33448/rsd-v10i10.18980.

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L-asparaginase (L-asnase) is an amino hydrolase that has been used in the last decades for leukemia treatment, which boosted scientific studies on production, purification and immobilization of this enzyme. More recently, L-asnase has called food industry attention because of its effect on acrylamide formation in fried and baked foods. Several studies have been carried out in order to evaluate the effect of L-asnase in reducing acrylamide formation in different food models. This review brings up an overview in L-asnase kinetic parameters from different sources, immobilization methods, its therapeutic use in leukemia treatment and food processing applications. This review also discusses acrylamide formation in fried and baked foods. Commercial L-asnase is produced by two microorganisms, Escherichia coli and Erwinia sp. However, studies using different microorganisms have shown the possibility of producing this enzyme from different sources, obtaining enzymes with interesting kinetic properties. Immobilization strategies have provided enzymes with greater activity and stability, which could contribute to maintain L-asnase activity in the body for longer periods. Researches applying L-asnase in food products have shown significant reduction in acrylamide production, above 90% in some cases. For this purpose, during enzyme application some variables must be taken into account, as enzyme dose, food matrix, pretreatment, processing time and temperature. Medical and food applications make L-asnase a multipurpose enzyme. Reducing prices, improving enzyme stability and reducing co-lateral effects in leukemia treatment are still challenges to overcome.

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Jeng, Arco Y., Paul Mulder, Aij-Lie Kwan, and Bruno Battistini. "Nonpeptidic endothelin-converting enzyme inhibitors and their potential therapeutic applications." Canadian Journal of Physiology and Pharmacology 80, no. 5 (May 1, 2002): 440–49. http://dx.doi.org/10.1139/y02-025.

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Endothelins (ETs) are potent vasoconstrictors, promitogens, and inflammatory mediators. They have been implicated in the pathogenesis of various cardiovascular, renal, pulmonary, and central nervous system diseases. Since the final step of the biosynthesis of ETs is catalyzed by a family of endothelin-converting enzymes (ECEs), inhibitors of these enzymes may represent novel therapeutic agents. Currently, seven isoforms of these metalloproteases have been identified; they all share a significant amino acid sequence identity with neutral endopeptidase 24.11 (NEP), another metalloprotease. Therefore, it is not surprising that the majority of ECE inhibitors also possess potent NEP inhibitory activity. To date, three classes of ECE inhibitors have been synthesized: dual ECE/NEP inhibitors, triple ECE/NEP/ACE inhibitors, and selective ECE inhibitors. Potential clinical applications of these compounds in hypertension, chronic heart failure, restenosis, renal failure, and cerebral vasospasm deduced from studies with relevant animal models are reviewed.Key words: endothelin-converting enzyme, ECE, inhibitors, phosphoramidon, CGS 26303, CGS 35066, FR 901533, SCH 54470, metalloprotease.

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