Background: Cadmium is a non-essential heavy metal, which is toxic even in relatively low concentrations. Although the mechanisms of Cd toxicity are well documented, there is limited information concerning the recovery of plants after exposure to this metal. Methods: The present study describes the recovery of soybean plants treated for 48 h with Cd at two concentrations: 10 and 25 mg/L. In the frame of the study the growth, cell viability, level of membrane damage makers, mineral content, photosynthesis parameters, and global methylation level have been assessed directly after Cd treatment and/or after 7 days of growth in optimal conditions. Results: The results show that exposure to Cd leads to the development of toxicity symptoms such as growth inhibition, increased cell mortality, and membrane damage. After a recovery period of 7 days, the exposed plants showed no differences in relation to the control in all analyzed parameters, with an exception of a slight reduction in root length and changed content of potassium, magnesium, and manganese. Conclusions: The results indicate that soybean plants are able to efficiently recover even after relatively severe Cd stress. On the other hand, previous exposure to Cd stress modulated their mineral uptake.

Noonan syndrome (NS) and related Noonan syndrome with multiple lentigines (NSML) contribute to the pathogenesis of human diseases in the RASopathy family. This family of genetic disorders constitute one of the largest groups of developmental disorders with variable penetrance and severity, associated with distinctive congenital disabilities, including facial features, cardiopathies, growth and skeletal abnormalities, developmental delay/mental retardation, and tumor predisposition. NS was first clinically described decades ago, and several genes have since been identified, providing a molecular foundation to understand their physiopathology and identify targets for therapeutic strategies. These genes encode proteins that participate in or regulate RAS/MAPK signalling. The RAS pathway regulates cellular metabolism by controlling mitochondrial homeostasis, dynamics, and energy production; however, little is known about the role of mitochondrial metabolism in NS and NSML. This manuscript comprehensively reviews the most frequently mutated genes responsible for NS and NSML, covering their role in cellular signalling pathways, and focuses on the pathophysiological outcomes on mitochondria and energy metabolism.

The human PTPN11 gene encodes for the src tyrosine phosphatase protein (SHP2) is now gaining much attention in many disorders, particularly its oncogenic involvement in many types of cancer. Efforts in developing molecules targeting SHP2 with high efficacy are the future of drug discovery and chemotherapy. However, the interaction of a new camptothecin analog with the catalytic domain of SHP2 protein remains unknown. Therefore, this study aims to provide in silico rationale for the recognition and binding of FL118 and irinotecan with the catalytic domain of human protein tyrosine phosphatase-SHP2 (PTPc-SH2-SHP2, chain A). The docking interaction of the human SHP2 protein’s catalytic domain as well as Y279C and R465G mutants with FL118 and irinotecan ligands were calculated and analyzed using the Autodock 4.2 programme, setting the docking grid to target the protein’s active site. The camptothecin analog FL118 had the best lowest negative affinity energies with PTPc-SHP2 wildtype and SHP2-Y279C mutant model (−7.54 Kcal/mol and −6.94 Kcal/mol, respectively). Moreover, the protein-ligand complexes revealed several hydrogen bond interactions reflecting the degree of stability that each structure possesses, with the FL118-SHP2-wildtype forming the most stable complex among the structures. In addition, the FL118-SHP2 wildtype complex was validated for RMSD, RMSF, hydrogen bonds, and salt bridges. This revealed that the complex generated became stable over time. This in silico rationale identifies the novel FL118 camptothecin analog as a potent selective inhibitor of PTPc-SH2 domain of SHP2 protein, paving way for further in vitro investigations into the interactions and binding activity of analogs with SHP2 for potential therapeutic applications in PTPN11-associated disorders.

Tumor cells use amino acids to rewire metabolic pathways to meet increased demands for energy, reducing equivalents, and cellular biosynthesis. Aside acting as building blocks for protein synthesis, amino acids also function as metabolic intermediates for ATP generation and redox homeostasis, as well as fueling biosynthetic pathways. Tumor-related metabolic changes influence every stage of the interaction between cells and their metabolites. Over the years, advancements in molecular methods such as transcriptomics and metabolomics have emerged to provide in-depth knowledge into the functions, interactions, and actions of molecules in cells of organisms. These technologies surfaced as methods that provide a more complete picture of disease pathophysiology, facilitating the elucidation of disease mechanisms and identification of potential biomarkers (metabolites) and targets (genes) respectively. Though Omics in cancer research have been explored in different concepts, however, employing these methods in amino acid metabolism in hematological cancers still requires attention. Therefore, this mini review discusses an up-to-date knowledge of principal regulators and their role in amino acid metabolism in hematological malignancies. In that perspective, we cover relevant findings from transcriptomics and metabolomics, thereby constructing mechanistic insights associated with disease pathogenesis.