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Marine Algal Secondary Metabolites Are a Potential Pharmaceutical Resource for Human Society Developments
Published in Se-Kwon Kim, Marine Biochemistry, 2023
Somasundaram Ambiga, Raja Suja Pandian, Lazarus Vijune Lawrence, Arjun Pandian, Ramu Arun Kumar, Bakrudeen Ali Ahmed Abdul
Almelysin, a new metalloproteinase with significant efficiency in low temperatures, is also other proteinase isolated from the culture filtrate of Alteromonas sp. The metalloprotease secreted by Alteromonas sp. is essential in the strain’s chitin degradation pathway. Aeromonas salmonicida subsp. has been found as a protamine-reducing marine bacterium obtained from marine soil. Extremophile hydrolases have benefits over chemical biocatalysts. These catalysts are non- polluting, environmentally acceptable, extremely specific, and occur in mild reaction circumstances. Such hydrolases may activate in the form of organic liquids, which is crucial for the production of single-isomer chiral medicines. These hydrolases have been used in a variety of ways. L-asparaginase is a hydrolase which produces L-aspartic and ammonia from L-asparagine. L-glutaminase activities is also present in this enzyme. Antileukemia/antilymphoma drugs made from microbial L-asparaginase preparations for biomedical applications presently account for one-third of global demand. L-asparaginases have been widely utilized in children particularly its act as chemotherapy for acute lymphoblastic leukemia, which is considerably greater than various therapeutic enzymes. L-asparaginase has been treated as an anti-tumor therapy in non-lymphoma, bovine lymphoma sarcoma, chronic lymphocytic leukemia Hodgkin’s pancreatic carcinoma, lymphosarcoma, lymphosarcoma, reticulum sarcoma, acute myelomonocytic leukemia, melanoma sarcoma and acute myelocytic leukemia.
Macronutrients
Published in Chuong Pham-Huy, Bruno Pham Huy, Food and Lifestyle in Health and Disease, 2022
Chuong Pham-Huy, Bruno Pham Huy
The name of an enzyme has two parts. The first part is the name of the substrate, and the second part is terminated with a suffix -ase (54). For example, protease is an enzyme of the substrate protein. For the international nomenclature, the name of an enzyme is preceded by the two letters EC (Enzyme Commission) followed by four numbers. For example, E.C.2.7.1.1. The first number denotes one of the six main classes: oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases. The second number denotes the subclass and the third number denotes the sub-subclass. The last number denotes the serial number of the enzyme in its sub-subclass (53–54). Enzymes are classified based on the reactions they catalyze into six classes cited above. Oxidoreductases such as glutathione reductase, lactate dehydrogenase, and glucose-6-phosphate dehydrogenase are the enzymes that catalyze oxidation-reduction reactions of their substrates. Transferases transfer a functional group between two substrates such as a methyl or phosphate group. Hydrolases catalyze the hydrolysis reactions of carbohydrates, proteins, and esters. Lyases cleave various chemical bonds by other means than hydrolysis and oxidation for the formation of double bonds. Isomerases are involved in isomerization of substrate where interconversion of cis-trans isomers is implicated. Ligases such as alanyl-t-RNA synthetase, glutamine synthetase, and DNA ligases join together two substrates with associated hydrolysis of a nucleoside triphosphate (53–54).
Towards the Importance of Fenugreek Proteins
Published in Dilip Ghosh, Prasad Thakurdesai, Fenugreek, 2022
Anti-nutritive compounds like hydrolase inhibitors affect digestive enzymes irreversibly. Trypsin and chymotrypsin inhibitors, as well as α-amylase inhibitors are known as the most important anti-nutritive compounds affecting protein digestibility (Duranti & Gius, 1997). Digestibility is a measure of protein hydrolysis and absorption of the liberated amino acids. Although an indication, digestibility could not thoroughly imply protein quality (Friedman, 1996). However, due to perquisite role of protein digestibility (i.e. susceptibility of peptide bonds to enzyme hydrolysis) on availability of amino acids and their integrity to oxidation, heat, etc., along with their absorption, it is worthy to measure protein digestibility under various conditions.
Anti-phospholipase A2 receptor antibodies directly induced podocyte damage in vitro
Published in Renal Failure, 2022
Yanfen Li, Juntao Yu, Miao Wang, Zhao Cui, Ming-hui Zhao
Functional classification on gene ontology molecular function (GO-MF) of these 120 specific proteins was presented in Figures 3(C–G). There were 163 genes that participated in the expression of 120 specific proteins. 133/163 genes hit the GO-MF database and were involved in 4660 categories in GO-MF, while 37/4660 categories presented significant fold enrichment (p< 0.05). The top 10 categories with the lowest p-value were shown in Figure 3(C). There were 24/37 categories related to binding. Considering the number of gene hits, the categories of catalytic activity and binding constituted more than 80% of GO-MF functional database hits (catalytic activity: 57/133, 42.9%; binding: 50/133, 37.6%) (Figure 4(D)). The categories of hydrolase activity (26/66, 39.4%) and transferase activity (15/66, 22.7%) constituted more than 60% of the functional hits in catalytic activity (Figure 4(E)). The categories of protein binding (28/56, 50.0%) and nucleic acid binding (20/56, 35.7%) constituted more than 80% of the functional hits in binding (Figure 4(F)). The hierarchical relationship of all 133 GO-MF-relevant genes was illustrated in the treemap (Figure 4(G)). The scales of rectangles were defined by the -log10 (p-value) of each entry. The root entries of protein binding, actin filament binding, and microtubule motor activity were the major components in GO-MF categories, which suggested that there might be disorder in the function of cytoskeleton structure, cell junction, migration, and signal transduction, after the treatment of anti-PLA2R antibodies on podocytes.
Peroxisome proliferator-activated receptor-gamma (PPARγ) and its immunomodulation function: current understanding and future therapeutic implications
Published in Expert Review of Clinical Pharmacology, 2022
Carlos Antonio Trindade da Silva, Juliana Trindade Clemente-Napimoga, Henrique Ballassini Abdalla, Rosanna Tarkany Basting, Marcelo Henrique Napimoga
Interestingly, eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) have advantageous effects, exerting their biological effects by activating PPARγ [79]. The activation of PPARγ appears to have anti-atherogenic effects through inhibiting endothelial adhesion molecule expression. Notably, EPA, but not DHA, increased the expression of CYP2J2 in a dose and time-dependent manner in human umbilical vein endothelial cells. The pretreatment with a PPARγ antagonist, GW9662, inhibits EPA-induced CYP2J2 expression [67]. In a recent study, the 15d-PGJ2 revealed that the soluble epoxide hydrolase (sEH) is covalently modified by 15d-PGJ2. This interaction inhibits its hydrolase activity mediated by its covalent adduction to the hydrolase [80]. In agreement, 15d-PGJ2 co-localizes with the sEH enzyme in various cell types, such as astrocytes, macrophages, and small arteries. In this regard, it is possible to speculate that enhanced 15d-PGJ2 levels may imply a more significant inhibition of sEH, which in turn would augment the bioavailability of EETs, EDPs, and other epoxy-fatty acids with anti-inflammatory and analgesic properties, and therefore PPARγ. This synergistic mechanism could contribute to a resolution of the inflammation [81]. Although their low stability and fast degradation is a limitation of bioactive lipids usage, it compensates for their potent analgesic effects mediated by PPARγ, encouraging the development of new strategies for drug delivery.
Liposome as drug delivery system enhance anticancer activity of iridium (III) complex
Published in Journal of Liposome Research, 2021
Yiying Gu, Lan Bai, Yuanyuan Zhang, Huiwen Zhang, Degang Xing, Li Tian, Yi Zhou, Jing Hao, Yunjun Liu
To achieve their vital catabolic functions, a large array of hydrolases is contained in the lysosome. Lysosomal membrane permeabilization (LMP) is a very apical event during signal transduction cascades that regulates the release of lysosomal proteases (cathepsin B and cathepsin D) from the lysosomes into cytoplasm, thereby triggering cell apoptosis and necrotic responses (Arnandis et al. 2012, Galluzzi et al. 2014). Since Ir1 localized at the lysosomes, the changes in lysosomal membrane permeability caused by Ir1Lipo treatment can be detected by metachromatic fluorescent dye AO (acridine orange). AO is a lysomotropic weak base, which has been proved to accumulate inside acidic lysosomal compartments in the form of charged molecules (AOH+) and exhibit orange fluorescence. However, when the lysosomal membranes penetrate, the uncharged AO in the cytoplasm emits yellow or green fluorescence (Ditaranto et al. 2001). The control cells (a) displayed strong red fluorescence totally localized in the lysosomes, while cells handled with Ir1 (b) or Ir1Lipo (c) showed varying degrees of enhanced green fluorescence. The permeabilization of lysosomal membrane is more obvious for Ir1 encapsulated liposome preparation (Figure 3(B)).