The Force-Dependent Mechanism of an Integrin α4β7-MAdCAM-1 Interaction.

The interaction between integrin α4β7 and mucosal vascular addressin cell-adhesion molecule-1 (MAdCAM-1) facilitates the adhesion of circulating lymphocytes to the surface of high endothelial venules in inflammatory bowel diseases (IBDs). Lymphocyte adhesion is a multistep cascade involving the tethering, rolling, stable adhesion, crawling, and migration of cells, with integrin α4β7 being involved in rolling and stable adhesions. Targeting the integrin α4β7-MAdCAM-1 interaction may help decrease inflammation in IBDs.

Force-Regulated Calcium Signaling of Lymphoid Cell RPMI 8226 Mediated by Integrin αβ/MAdCAM-1 in Flow.

MAdCAM-1 binds to integrin αβ, which mediates the rolling and arrest of circulating lymphocytes upon the vascular endothelia during lymphocytic homing. The calcium response by adhered lymphocytes is a critical event for lymphocyte activation and subsequent arrest and migration under flow. However, whether the interaction of integrin αβ /MAdCAM-1 can effectively trigger the calcium response of lymphocytes remains unclear, as well as whether the fluid force affects the calcium response.

Comparison of Intermolecular Interactions of Irreversible and Reversible Inhibitors with Bruton's Tyrosine Kinase via Molecular Dynamics Simulations.

Bruton's tyrosine kinase (BTK) is a key protein from the TEC family and is involved in B-cell lymphoma occurrence and development. Targeting BTK is therefore an effective strategy for B-cell lymphoma treatment. Since previous studies on BTK have been limited to structure-function analyses of static protein structures, the dynamics of conformational change of BTK upon inhibitor binding remain unclear.

Construction of a Comprehensive Diagnostic Scoring Model for Prostate Cancer Based on a Novel Six-Gene Panel.

Accumulating evidence indicates that the N6-methyladenosine (mA) modification plays a critical role in human cancers. Given the current understanding of mA modification, this process is believed to be dynamically regulated by mA regulators. Although the discovery of mA regulators has greatly enhanced our understanding of the mechanism underlying mA modification in cancers, the function and role of mA in the context of prostate cancer (PCa) remain unclear.