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Malignant tumor cells can obtain proliferative benefits from deviant metabolic networks. Emerging evidence suggests that lipid metabolism are dramatically altered in gliomas and excessive fatty acd accumulation is detrimentally correlated with the prognosis of glioma patients. Glioma cells possess remarkably high levels of free fatty acids, which, in turn, enhance post-translational modifications (e.g. palmitoylation). Our and other groups found that palmitoylational modification is essential for remaining intracellular homeostasis and cell survival. Disrupting the balance between palmitoylation and depalmitoylation affects glioma cell viability, apoptosis, invasion, self-renew and pyroptosis. In this review, we focused on summarizing roles and relevant mechanisms of protein palmitoylational modification in gliomas.

CaAl-LDHs and sodium dodecyl benzene sulfonate (SDBS) intercalated CaAl-LDHs (SDBS-CaAl-LDHs) was acquired by co-precipitation. The two samples were characterized by XRD, XPS, FT-IR, TG and SEM. The factors affecting adsorption (pH, adsorption time，initial concentration) of Pb2+ by two adsorbents were studied. The results showed that SDBS-CaAl-LDHs has higher adsorption ability for lead ions removal than that of CaAl-LDHs. Kinetic data for lead ions were in keeping with pseudo-2nd-order model, the adsorption isotherms followed Langmuir and Freundlich isotherm model for CaAl-LDHs. The adsorption by SDBS-CaAl-LDHs were in keeping with the pseudo-second-order kinetic and Langmuir model, suggesting lead ions were chemical adsorption. Adsorption was thought to form through Pb species in the precipitates, such as formation of hydroxides and carbonates for lead ions by XRD analysis. Therefore, based on the structural and morphological features, as well as XRD, XPS and SEM, the lead ion adsorption mechanism on SDBS-CaAl-LDHs involved the electrostatic attraction, precipitation, complexation and ion exchange. The Langmuir adsorption capacities for SDBS-CaAl-LDHs were found as 797.63, 828.76, 854.29 mg×g−1 at 293k, 303k, 313k, respectively, when the pH is about 5.2, and thus, making it a highly economical adsorbent for the treatment of contaminated water.

Isocitrate dehydrogenase (IDH) is an essential metabolic enzyme in the tricarboxylic acid cycle (TAC). The high mutation frequency of the IDH gene plays a complicated role in gliomas. In addition to affecting gliomas directly, mutations in IDH can also alter their immune microenvironment and can change immune-cell function in direct and indirect ways. IDH mutations mediate immune-cell infiltration and function by modulating immune-checkpoint gene expression and chemokine secretion. In addition, IDH mutation-derived D2-hydroxyglutarate can be absorbed by surrounding immune cells, also affecting their functioning. In this review, we summarize current knowledge about the effects of IDH mutations as well as other gene mutations on the immune microenvironment of gliomas. We also describe recent preclinical and clinical data related to IDH-mutant inhibitors for the treatment of gliomas. Finally, we discuss different types of immunotherapy and the immunotherapeutic potential of IDH mutations in gliomas.

The interaction between angiotensin I-converting enzyme (ACE) and the inhibitory peptide KNFL from Wakame was explored using isothermal titration calorimetry, multiple spectroscopic techniques and molecular dynamics simulations, and an inhibition model was established based on free energy binding theory. The experiments revealed that the binding of KNFL to ACE was a spontaneous exothermic process driven by enthalpy and entropy and occurred via multiple binding sites to form stable complexes. The complexes may be formed through multiple steps of inducing fit and conformational selection. The peptide KNFL had a fluorescence quenching effect on ACE and its addition not only affected the microenvironment around the ACE Trp and Tyr residues, but also increased the diameter and altered the conformation of ACE. This study should prove useful for improving our understanding of the mechanism of ACE inhibitory peptides.