ITGB4 upregulation is associated with progression of lower grade glioma.

Gliomas originating in the neuroepithelium account for about 80% of brain malignancies and are the most common cancer of the central nervous system. Clinical management of gliomas remains challenging despite significant advances in comprehensive therapies, including radiotherapy, chemotherapy, and surgery. The ITGB4 (Integrin subunit beta 4) gene encodes a receptor for laminins and its upregulation in tumor tissues is associated with poor prognosis. However, its role in glioma is not well understood. First, we performed a pan cancer analysis of ITGB4 expression in The Cancer Genome Atlas (TCGA) dataset. Survival analysis was done on Chinese Glioma Genome Atlas (CGGA) and TCGA. Immunohistochemistry was then used to validate the expression and role of ITGB4 in glioma. We finally analyzed the possible mechanism by immune infiltration and single-cell sequencing analysis. Here, we found that ITGB4 is upregulated in glioma and accurately predicts the prognosis of lower grade glioma (LGG). Univariate and multivariate Cox regression analyses showed that ITGB4 is a risk factor for LGG. Immunohistochemical analysis confirmed that ITGB4 accurately predicts LGG prognosis. Non-negative matrix factorization (NMF) cluster analysis showed that ITGB4 was closely related to immune related genes. Immune cell infiltration and single cell sequencing analyses indicated that ITGB4 may be closely related to the microenvironment of gliomas, especially tumor-associated fibroblasts. ITGB4 is a promising diagnostic and therapeutic factor in LGG patients.

Characterization of binding interactions between selected phenylpropanoid glycosides and trypsin.

Phenylpropanoid glycosides (PPGs) are important bioactive polyphenolic compounds that are widely distributed in plants. In this paper, the inhibitory effects of four selected PPGs against trypsin were investigated. The interactions between these PPGs and trypsin were further investigated by multiple spectroscopic methods and molecular docking studies. The results showed that the binding of each of these PPGs to trypsin induced changes in the natural conformation of trypsin, which inhibited the enzyme in the following order: acteoside>syringalide A 3'-α-l-rhamnopyranoside>lipedoside A-I>osmanthuside B. The binding constant (Ka) values followed the same trend. The hydrogen bond force played an important role in the interaction between each PPG and trypsin. Interestingly, the binding affinity and inhibitory effect increased as the number of phenolic hydroxyl groups increased. In addition, the effect of the phenolic hydroxyl group on the A ring had a greater effect than one on the B ring.